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<article article-type="research-article" dtd-version="1.3" xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xml:lang="ru"><front><journal-meta><journal-id journal-id-type="publisher-id">nefr</journal-id><journal-title-group><journal-title xml:lang="ru">Нефрология</journal-title><trans-title-group xml:lang="en"><trans-title>Nephrology (Saint-Petersburg)</trans-title></trans-title-group></journal-title-group><issn pub-type="ppub">1561-6274</issn><issn pub-type="epub">2541-9439</issn><publisher><publisher-name>Pavlov First Saint-Petersburg State Medical University</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="doi">10.24884/1561-6274-2012-16-3/1-54-71</article-id><article-id custom-type="elpub" pub-id-type="custom">nefr-596</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="ru"><subject>ОБЗОРЫ И ЛЕКЦИИ</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="en"><subject>REVIEWS AND LECTURES</subject></subj-group></article-categories><title-group><article-title>СТРЕСС ЭНДОПЛАЗМАТИЧЕСКОГО РЕТИКУЛУМА ГЛАЗАМИ НЕФРОЛОГА (СООБЩЕНИЕ I)</article-title><trans-title-group xml:lang="en"><trans-title>NEPHROLOGIST’S IMPRESSION OF ENDOPLASMATIC RETICULUM STRESS (TEXT 1)</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Зверев</surname><given-names>Я. Ф.</given-names></name><name name-style="western" xml:lang="en"><surname>Zverev</surname><given-names>Ya. F.</given-names></name></name-alternatives><bio xml:lang="ru"><p>кафедра фармакологии</p><p>656038, г. Барнаул, пр. Ленина, д. 40. Тел.: (3852)26-08-35</p></bio><email xlink:type="simple">zver@asmu.ru</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Брюханов</surname><given-names>В. М.</given-names></name><name name-style="western" xml:lang="en"><surname>Bruhanov</surname><given-names>V. M.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Кафедра фармакологии</p></bio><xref ref-type="aff" rid="aff-1"/></contrib></contrib-group><aff xml:lang="ru" id="aff-1"><institution>Алтайского государственного медицинского университета</institution><country>Russian Federation</country></aff><pub-date pub-type="collection"><year>2012</year></pub-date><pub-date pub-type="epub"><day>10</day><month>03</month><year>2012</year></pub-date><volume>16</volume><issue>3/1</issue><fpage>54</fpage><lpage>71</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Зверев Я.Ф., Брюханов В.М., 2012</copyright-statement><copyright-year>2012</copyright-year><copyright-holder xml:lang="ru">Зверев Я.Ф., Брюханов В.М.</copyright-holder><copyright-holder xml:lang="en">Zverev Y.F., Bruhanov V.M.</copyright-holder><license xml:lang="ru" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>Данная работа распространяется под лицензией Creative Commons Attribution 4.0.</license-p></license><license xml:lang="en" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>This work is licensed under a Creative Commons Attribution 4.0 License.</license-p></license></permissions><self-uri xlink:href="https://journal.nephrolog.ru/jour/article/view/596">https://journal.nephrolog.ru/jour/article/view/596</self-uri><abstract><p>В обзоре приводятся данные, касающиеся стресса эндоплазматического ретикулума (ЭПР-стресса). Приводятся сведения относительно биологической роли ЭПР-стресса, причин его возникновения, внутриклеточных событий, обеспечивающих развитие адаптивного и проапоптозного биохимических каскадов, лежащих в основе UPR, реакции на ЭПР-стресс, и определяющих судьбу клетки, подвергшейся воздействию этого стресса. Обсуждаются физиологические и патофизиологические аспекты ЭПР-стресса, его связь с гипоксией, воспалением, оксидативным стрессом. Рассматривается роль ЭПР-стресса в патогенезе ряда заболеваний.</p></abstract><trans-abstract xml:lang="en"><p>Review provides data about endoplasmatic reticulum stress (ER-stress). Data about biological role of ER-stress, its causes, intracellular events which provide adaptive and proapoptotic biochemical cascades underlying UPR, ER-stress reaction and identifying fortune of cell which has been exposed to influence of this stress is given. Physiological and pathophysiological aspects of ER-stress are discussed, its connection with hypoxia, inflammation, oxidative stress. ER-stress role in pathogenesis of some diseases is observed.</p></trans-abstract><kwd-group xml:lang="ru"><kwd>стресс эндоплазматического ретикулума</kwd><kwd>реакция клетки</kwd><kwd>физиологическая и патофизиологическая роль</kwd></kwd-group><kwd-group xml:lang="en"><kwd>endoplasmatic reticulum stress</kwd><kwd>cell’s reaction</kwd><kwd>physiological and pathophysiological role</kwd></kwd-group></article-meta></front><back><ref-list><title>References</title><ref id="cit1"><label>1</label><citation-alternatives><mixed-citation xml:lang="ru">Gaut JR, Hendershot LM. The modification and assembly of proteins in the endoplasmic reticulum. Curr Opin Cell Biol 1993; 5: 589-595</mixed-citation><mixed-citation xml:lang="en">Gaut JR, Hendershot LM. The modification and assembly of proteins in the endoplasmic reticulum. Curr Opin Cell Biol 1993; 5: 589-595</mixed-citation></citation-alternatives></ref><ref id="cit2"><label>2</label><citation-alternatives><mixed-citation xml:lang="ru">Ni M, Lee AS. ER chaperones in mammalian development and human diseases. FEBS Lett 2007; 581: 3641-3651</mixed-citation><mixed-citation xml:lang="en">Ni M, Lee AS. ER chaperones in mammalian development and human diseases. FEBS Lett 2007; 581: 3641-3651</mixed-citation></citation-alternatives></ref><ref id="cit3"><label>3</label><citation-alternatives><mixed-citation xml:lang="ru">Cybulsky AV. Endoplasmic reticulum stress in proteinuric kidney disease. Kidney Int 2010; 77 (3): 187-193</mixed-citation><mixed-citation xml:lang="en">Cybulsky AV. Endoplasmic reticulum stress in proteinuric kidney disease. Kidney Int 2010; 77 (3): 187-193</mixed-citation></citation-alternatives></ref><ref id="cit4"><label>4</label><citation-alternatives><mixed-citation xml:lang="ru">Lee AS The glucose-regulated proteins: stress induction and clinical applications. Trends Biochem Sci 2001; 26: 504-510</mixed-citation><mixed-citation xml:lang="en">Lee AS The glucose-regulated proteins: stress induction and clinical applications. Trends Biochem Sci 2001; 26: 504-510</mixed-citation></citation-alternatives></ref><ref id="cit5"><label>5</label><citation-alternatives><mixed-citation xml:lang="ru">Szegezdi E, Logue SE, Gorman AM, Samali A. Mediatirs of endoplasmic reticulum stresss-induced apoptosis. EMBO Rep 2006; 7 (9): 880-885</mixed-citation><mixed-citation xml:lang="en">Szegezdi E, Logue SE, Gorman AM, Samali A. Mediatirs of endoplasmic reticulum stresss-induced apoptosis. EMBO Rep 2006; 7 (9): 880-885</mixed-citation></citation-alternatives></ref><ref id="cit6"><label>6</label><citation-alternatives><mixed-citation xml:lang="ru">Kitamura M. Endoplasmic reticulum stress and unfolded protein response in renal pathophysiology: Janus faces. Am J Physiol Renal Physiol 2008; 295 (2): F323-F334</mixed-citation><mixed-citation xml:lang="en">Kitamura M. Endoplasmic reticulum stress and unfolded protein response in renal pathophysiology: Janus faces. Am J Physiol Renal Physiol 2008; 295 (2): F323-F334</mixed-citation></citation-alternatives></ref><ref id="cit7"><label>7</label><citation-alternatives><mixed-citation xml:lang="ru">Zhang K, Kaufman DJ. Identification and characterization of endoplasmic reticulum stress-induced apoptosis in vivo. Methods Enzymol 2008; 442: 395-419</mixed-citation><mixed-citation xml:lang="en">Zhang K, Kaufman DJ. Identification and characterization of endoplasmic reticulum stress-induced apoptosis in vivo. Methods Enzymol 2008; 442: 395-419</mixed-citation></citation-alternatives></ref><ref id="cit8"><label>8</label><citation-alternatives><mixed-citation xml:lang="ru">Inagi R. Endoplasmic reticulum stress in the kidney as a novel mediator of kidney injury. Nephron Exp Nephrol 2009; 112 (1): e1-e9</mixed-citation><mixed-citation xml:lang="en">Inagi R. Endoplasmic reticulum stress in the kidney as a novel mediator of kidney injury. Nephron Exp Nephrol 2009; 112 (1): e1-e9</mixed-citation></citation-alternatives></ref><ref id="cit9"><label>9</label><citation-alternatives><mixed-citation xml:lang="ru">Kleizen B, Braakman I. Protein folding and quality control in the endoplasmic reticulum. Curr Opin Cell Biol 2004; 16: 343-349</mixed-citation><mixed-citation xml:lang="en">Kleizen B, Braakman I. Protein folding and quality control in the endoplasmic reticulum. Curr Opin Cell Biol 2004; 16: 343-349</mixed-citation></citation-alternatives></ref><ref id="cit10"><label>10</label><citation-alternatives><mixed-citation xml:lang="ru">Kitamura M. Endoplasmic reticulum stress in the kidney. Clin Exp Nephrol 2008; 12: 317-325</mixed-citation><mixed-citation xml:lang="en">Kitamura M. Endoplasmic reticulum stress in the kidney. Clin Exp Nephrol 2008; 12: 317-325</mixed-citation></citation-alternatives></ref><ref id="cit11"><label>11</label><citation-alternatives><mixed-citation xml:lang="ru">Malhotra JD, Kaufman RJ. Endoplasmic reticulum stress: a vicious cycle or a double-edged sword? Antioxid Redox Signal 2007; 9: 2277-2293</mixed-citation><mixed-citation xml:lang="en">Malhotra JD, Kaufman RJ. Endoplasmic reticulum stress: a vicious cycle or a double-edged sword? Antioxid Redox Signal 2007; 9: 2277-2293</mixed-citation></citation-alternatives></ref><ref id="cit12"><label>12</label><citation-alternatives><mixed-citation xml:lang="ru">Kitamura M. Endoplasmic reticulum stress in glomerulonephritis: the bad guy turns good? J Am Soc Nephrol 2009; 20 (9): 1871-1873</mixed-citation><mixed-citation xml:lang="en">Kitamura M. Endoplasmic reticulum stress in glomerulonephritis: the bad guy turns good? J Am Soc Nephrol 2009; 20 (9): 1871-1873</mixed-citation></citation-alternatives></ref><ref id="cit13"><label>13</label><citation-alternatives><mixed-citation xml:lang="ru">Ron D, Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 2007; 8: 519-529</mixed-citation><mixed-citation xml:lang="en">Ron D, Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 2007; 8: 519-529</mixed-citation></citation-alternatives></ref><ref id="cit14"><label>14</label><citation-alternatives><mixed-citation xml:lang="ru">Dickhout JG, Krepinsky JC. Endoplasmic reticulum stress and renal disease. Antioxid Redox Signal 2009; 11 (9): 2341-2352</mixed-citation><mixed-citation xml:lang="en">Dickhout JG, Krepinsky JC. Endoplasmic reticulum stress and renal disease. Antioxid Redox Signal 2009; 11 (9): 2341-2352</mixed-citation></citation-alternatives></ref><ref id="cit15"><label>15</label><citation-alternatives><mixed-citation xml:lang="ru">Yoshida H, Matsui T, Yamamoto A et al. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 2001; 107: 881-891</mixed-citation><mixed-citation xml:lang="en">Yoshida H, Matsui T, Yamamoto A et al. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 2001; 107: 881-891</mixed-citation></citation-alternatives></ref><ref id="cit16"><label>16</label><citation-alternatives><mixed-citation xml:lang="ru">Lee AH, Iwakoshi NN, Glimcher LH. XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol Cell Biol 2003; 23: 7448-7459</mixed-citation><mixed-citation xml:lang="en">Lee AH, Iwakoshi NN, Glimcher LH. XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol Cell Biol 2003; 23: 7448-7459</mixed-citation></citation-alternatives></ref><ref id="cit17"><label>17</label><citation-alternatives><mixed-citation xml:lang="ru">Yamamoto K, Sato T, Matsui T et al. Transcriptional induction of mammalian ERquality control proteins is mediated by single or combined action of ATF6α and XBP1. Dev Cell 2007; 13: 365-376</mixed-citation><mixed-citation xml:lang="en">Yamamoto K, Sato T, Matsui T et al. Transcriptional induction of mammalian ERquality control proteins is mediated by single or combined action of ATF6α and XBP1. Dev Cell 2007; 13: 365-376</mixed-citation></citation-alternatives></ref><ref id="cit18"><label>18</label><citation-alternatives><mixed-citation xml:lang="ru">Voges D, Zwicki P, Baumeister W. The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu Rev Biochem 1999; 68: 1015-1068</mixed-citation><mixed-citation xml:lang="en">Voges D, Zwicki P, Baumeister W. The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu Rev Biochem 1999; 68: 1015-1068</mixed-citation></citation-alternatives></ref><ref id="cit19"><label>19</label><citation-alternatives><mixed-citation xml:lang="ru">Brodsky JL. The protective and destructive roles played by molecular chaperones during ERAD (endoplasmic-reticulumassociated degradation). Biochem J 2007; 404: 353-363</mixed-citation><mixed-citation xml:lang="en">Brodsky JL. The protective and destructive roles played by molecular chaperones during ERAD (endoplasmic-reticulumassociated degradation). Biochem J 2007; 404: 353-363</mixed-citation></citation-alternatives></ref><ref id="cit20"><label>20</label><citation-alternatives><mixed-citation xml:lang="ru">Cybulsky AV, Takano T, Papillon J et al. Glomerular epithelial cell injury associated with mutant α-actinin-4. Am J Physiol Renal Physiol 2009; 297 (4): F987-F995</mixed-citation><mixed-citation xml:lang="en">Cybulsky AV, Takano T, Papillon J et al. Glomerular epithelial cell injury associated with mutant α-actinin-4. Am J Physiol Renal Physiol 2009; 297 (4): F987-F995</mixed-citation></citation-alternatives></ref><ref id="cit21"><label>21</label><citation-alternatives><mixed-citation xml:lang="ru">Harding HP, Zhang Y, Ron D. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 1999; 397: 271-274</mixed-citation><mixed-citation xml:lang="en">Harding HP, Zhang Y, Ron D. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 1999; 397: 271-274</mixed-citation></citation-alternatives></ref><ref id="cit22"><label>22</label><citation-alternatives><mixed-citation xml:lang="ru">Harding HP, Zhang Y, Bertolotti A et al. Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol Cell 2000; 5: 897-904</mixed-citation><mixed-citation xml:lang="en">Harding HP, Zhang Y, Bertolotti A et al. Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol Cell 2000; 5: 897-904</mixed-citation></citation-alternatives></ref><ref id="cit23"><label>23</label><citation-alternatives><mixed-citation xml:lang="ru">Zhang DD. Mechanistic studies of Nrf2-Keap1 signaling pathway. Drug Metab Rev 2006; 28: 769-789</mixed-citation><mixed-citation xml:lang="en">Zhang DD. Mechanistic studies of Nrf2-Keap1 signaling pathway. Drug Metab Rev 2006; 28: 769-789</mixed-citation></citation-alternatives></ref><ref id="cit24"><label>24</label><citation-alternatives><mixed-citation xml:lang="ru">Schroder M, Kaufman RJ. The mammalian unfolded protein response. Ann Rev Biochem 2005; 74: 739-789</mixed-citation><mixed-citation xml:lang="en">Schroder M, Kaufman RJ. The mammalian unfolded protein response. Ann Rev Biochem 2005; 74: 739-789</mixed-citation></citation-alternatives></ref><ref id="cit25"><label>25</label><citation-alternatives><mixed-citation xml:lang="ru">Adachi Y, Yamamoto K, Okada T et al. ATF6 is a transcription factor specializing in the regulation of quality control proteins in the endoplasmic reticulum. Cell Struct Funct 2008; 33: 75-89</mixed-citation><mixed-citation xml:lang="en">Adachi Y, Yamamoto K, Okada T et al. ATF6 is a transcription factor specializing in the regulation of quality control proteins in the endoplasmic reticulum. Cell Struct Funct 2008; 33: 75-89</mixed-citation></citation-alternatives></ref><ref id="cit26"><label>26</label><citation-alternatives><mixed-citation xml:lang="ru">Wu J, Rutkowski DT, Dubois M et al. ATF6alpha optimizes longterm endoplasmic reticulum function to protect cells from chronic stress. Dev Cell 2007; 13: 351-364</mixed-citation><mixed-citation xml:lang="en">Wu J, Rutkowski DT, Dubois M et al. ATF6alpha optimizes longterm endoplasmic reticulum function to protect cells from chronic stress. Dev Cell 2007; 13: 351-364</mixed-citation></citation-alternatives></ref><ref id="cit27"><label>27</label><citation-alternatives><mixed-citation xml:lang="ru">Fonesca SG, Urano F, Burcin M, Gromada J. Stress hypERactivation in the β-cell. Islets 2010; 2 (1): 1-9</mixed-citation><mixed-citation xml:lang="en">Fonesca SG, Urano F, Burcin M, Gromada J. Stress hypERactivation in the β-cell. Islets 2010; 2 (1): 1-9</mixed-citation></citation-alternatives></ref><ref id="cit28"><label>28</label><citation-alternatives><mixed-citation xml:lang="ru">Pallet N, Beuvier N, Legendre C et al. Autophagy protects renal tubular cells against cyclosporine toxicity. Autophagy 2008; 4: 783-791</mixed-citation><mixed-citation xml:lang="en">Pallet N, Beuvier N, Legendre C et al. Autophagy protects renal tubular cells against cyclosporine toxicity. Autophagy 2008; 4: 783-791</mixed-citation></citation-alternatives></ref><ref id="cit29"><label>29</label><citation-alternatives><mixed-citation xml:lang="ru">Pallet N, Anglicheau D, Thervet E. Autophagy is an adaptive mechanism against endoplasmic reticulum stress. Nephrol Dial Transplant 2009; 24: 3891</mixed-citation><mixed-citation xml:lang="en">Pallet N, Anglicheau D, Thervet E. Autophagy is an adaptive mechanism against endoplasmic reticulum stress. Nephrol Dial Transplant 2009; 24: 3891</mixed-citation></citation-alternatives></ref><ref id="cit30"><label>30</label><citation-alternatives><mixed-citation xml:lang="ru">Kawakami T, Inagi R, Takano H et al. Endoplasmic reticulum stress induces autophagy in renal proximal tubular cells. Nephrol Dial Transplant 2009; 24: 2665-2672</mixed-citation><mixed-citation xml:lang="en">Kawakami T, Inagi R, Takano H et al. Endoplasmic reticulum stress induces autophagy in renal proximal tubular cells. Nephrol Dial Transplant 2009; 24: 2665-2672</mixed-citation></citation-alternatives></ref><ref id="cit31"><label>31</label><citation-alternatives><mixed-citation xml:lang="ru">Ogata M, Hino S, Saito A et al. Autophagy is activated for cell survival after endoplasmic reticulum stress. Mol Cell Biol 2006; 26: 9220-9231</mixed-citation><mixed-citation xml:lang="en">Ogata M, Hino S, Saito A et al. Autophagy is activated for cell survival after endoplasmic reticulum stress. Mol Cell Biol 2006; 26: 9220-9231</mixed-citation></citation-alternatives></ref><ref id="cit32"><label>32</label><citation-alternatives><mixed-citation xml:lang="ru">Yorimitsu T, Nair U, Yang Z, Klionsky DJ. Endoplasmic reticulum stress triggers autophagy. J Biol Chem 2006; 281: 30299-30304</mixed-citation><mixed-citation xml:lang="en">Yorimitsu T, Nair U, Yang Z, Klionsky DJ. Endoplasmic reticulum stress triggers autophagy. J Biol Chem 2006; 281: 30299-30304</mixed-citation></citation-alternatives></ref><ref id="cit33"><label>33</label><citation-alternatives><mixed-citation xml:lang="ru">Mizushima N, Levine B, Cuervo AM, Klionsky DJ. Autophagy fights disease through cellular self-digestion. Nature 2008; 451 (7182): 1069-1075</mixed-citation><mixed-citation xml:lang="en">Mizushima N, Levine B, Cuervo AM, Klionsky DJ. Autophagy fights disease through cellular self-digestion. Nature 2008; 451 (7182): 1069-1075</mixed-citation></citation-alternatives></ref><ref id="cit34"><label>34</label><citation-alternatives><mixed-citation xml:lang="ru">Periyasamy-Thandavan S, Jiang M, Wei Q et al. Autophagy is cytoprotective during cisplatin injury of renal proximal tubular cells. Kidney Int 2008; 74 (5): 631-640</mixed-citation><mixed-citation xml:lang="en">Periyasamy-Thandavan S, Jiang M, Wei Q et al. Autophagy is cytoprotective during cisplatin injury of renal proximal tubular cells. Kidney Int 2008; 74 (5): 631-640</mixed-citation></citation-alternatives></ref><ref id="cit35"><label>35</label><citation-alternatives><mixed-citation xml:lang="ru">Hartleben D, Gödel M, Meyer-Schwesinger C et al. Autophagy influences glomerular disease susceptibility and maintains podocyte homeostasis in aging mice. J Clin Invest 2010; 120 (4): 1084-1096</mixed-citation><mixed-citation xml:lang="en">Hartleben D, Gödel M, Meyer-Schwesinger C et al. Autophagy influences glomerular disease susceptibility and maintains podocyte homeostasis in aging mice. J Clin Invest 2010; 120 (4): 1084-1096</mixed-citation></citation-alternatives></ref><ref id="cit36"><label>36</label><citation-alternatives><mixed-citation xml:lang="ru">Ding WX, Ni HM, Gao W et al. Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability. Am J Pathol 2007; 171: 513-524</mixed-citation><mixed-citation xml:lang="en">Ding WX, Ni HM, Gao W et al. Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability. Am J Pathol 2007; 171: 513-524</mixed-citation></citation-alternatives></ref><ref id="cit37"><label>37</label><citation-alternatives><mixed-citation xml:lang="ru">Høyer-Hansen M, Jäättelä M. Connecting endoplasmic reticulum stress to autophagy by unfolded protein response and calcium. Cell Death Differ 2007; 14: 1576-1582</mixed-citation><mixed-citation xml:lang="en">Høyer-Hansen M, Jäättelä M. Connecting endoplasmic reticulum stress to autophagy by unfolded protein response and calcium. Cell Death Differ 2007; 14: 1576-1582</mixed-citation></citation-alternatives></ref><ref id="cit38"><label>38</label><citation-alternatives><mixed-citation xml:lang="ru">Harding HP, Zhang Y, Zeng H et al. An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol Cell 2003; 11 (3): 619-633</mixed-citation><mixed-citation xml:lang="en">Harding HP, Zhang Y, Zeng H et al. An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol Cell 2003; 11 (3): 619-633</mixed-citation></citation-alternatives></ref><ref id="cit39"><label>39</label><citation-alternatives><mixed-citation xml:lang="ru">McCullough KD, Martindale JL, Klotz LO et al. Gadd 153 sensitizes cells by downregulating Bcl2 and perturbing the cellular redox state. Mol Cell Biol 2001; 21: 1249-1259</mixed-citation><mixed-citation xml:lang="en">McCullough KD, Martindale JL, Klotz LO et al. Gadd 153 sensitizes cells by downregulating Bcl2 and perturbing the cellular redox state. Mol Cell Biol 2001; 21: 1249-1259</mixed-citation></citation-alternatives></ref><ref id="cit40"><label>40</label><citation-alternatives><mixed-citation xml:lang="ru">Anding AL, Chapman JS, Barnett DW et al. The unhydrolyzable fenretinide analogue 4-hydroxybenylretinone induces the proaptotic genes GADD 153 (CHOP) and Bcl-2-binding component 3 (PUMA) and apoptosis that is caspase-dependent and independent of the retinoic acid receptor. Cancer Res 2007; 67: 6270-6277</mixed-citation><mixed-citation xml:lang="en">Anding AL, Chapman JS, Barnett DW et al. The unhydrolyzable fenretinide analogue 4-hydroxybenylretinone induces the proaptotic genes GADD 153 (CHOP) and Bcl-2-binding component 3 (PUMA) and apoptosis that is caspase-dependent and independent of the retinoic acid receptor. Cancer Res 2007; 67: 6270-6277</mixed-citation></citation-alternatives></ref><ref id="cit41"><label>41</label><citation-alternatives><mixed-citation xml:lang="ru">Bhatt K, Feng L, Pabla N et al. Effects of targeted Bcl-2 expression in mitochondria or endoplasmic reticulum on renal tubular cell apoptosis. Am J Physiol Renal Physiol 2008; 94: F499-F507</mixed-citation><mixed-citation xml:lang="en">Bhatt K, Feng L, Pabla N et al. Effects of targeted Bcl-2 expression in mitochondria or endoplasmic reticulum on renal tubular cell apoptosis. Am J Physiol Renal Physiol 2008; 94: F499-F507</mixed-citation></citation-alternatives></ref><ref id="cit42"><label>42</label><citation-alternatives><mixed-citation xml:lang="ru">Zinszner H, Kuroda M, Wang X et al. CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum. Genes Dev 1998; 12: 982-995</mixed-citation><mixed-citation xml:lang="en">Zinszner H, Kuroda M, Wang X et al. CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum. Genes Dev 1998; 12: 982-995</mixed-citation></citation-alternatives></ref><ref id="cit43"><label>43</label><citation-alternatives><mixed-citation xml:lang="ru">Urano F, Wang X, Bertolotti A et al. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 2000; 287: 664-666</mixed-citation><mixed-citation xml:lang="en">Urano F, Wang X, Bertolotti A et al. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 2000; 287: 664-666</mixed-citation></citation-alternatives></ref><ref id="cit44"><label>44</label><citation-alternatives><mixed-citation xml:lang="ru">Nishitoh H, Matsuzawa A, Tobiume K et al. ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev 2002; 16: 1345-1355</mixed-citation><mixed-citation xml:lang="en">Nishitoh H, Matsuzawa A, Tobiume K et al. ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev 2002; 16: 1345-1355</mixed-citation></citation-alternatives></ref><ref id="cit45"><label>45</label><citation-alternatives><mixed-citation xml:lang="ru">Kim R, Emi M, Tanabe K, Murakami S. Role of the unfolded protein response in cell death. Apoptosis 2006; 11: 5-13</mixed-citation><mixed-citation xml:lang="en">Kim R, Emi M, Tanabe K, Murakami S. Role of the unfolded protein response in cell death. Apoptosis 2006; 11: 5-13</mixed-citation></citation-alternatives></ref><ref id="cit46"><label>46</label><citation-alternatives><mixed-citation xml:lang="ru">Davis RJ. Signal transduction by the JNK group of MAP kinases. Cell 2000; 103: 239-252</mixed-citation><mixed-citation xml:lang="en">Davis RJ. Signal transduction by the JNK group of MAP kinases. Cell 2000; 103: 239-252</mixed-citation></citation-alternatives></ref><ref id="cit47"><label>47</label><citation-alternatives><mixed-citation xml:lang="ru">Князькин ИВ, Цыган ВН. Апоптоз в урологии. Наука, СПб., 2007; 25-26</mixed-citation><mixed-citation xml:lang="en">Князькин ИВ, Цыган ВН. Апоптоз в урологии. Наука, СПб., 2007; 25-26</mixed-citation></citation-alternatives></ref><ref id="cit48"><label>48</label><citation-alternatives><mixed-citation xml:lang="ru">Yoneda T, Imaizumi K, Oono K et al. Activation of caspase-12, an endoplasmic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress. J Biol Chem 2001; 276: 13935-13940</mixed-citation><mixed-citation xml:lang="en">Yoneda T, Imaizumi K, Oono K et al. Activation of caspase-12, an endoplasmic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress. J Biol Chem 2001; 276: 13935-13940</mixed-citation></citation-alternatives></ref><ref id="cit49"><label>49</label><citation-alternatives><mixed-citation xml:lang="ru">Nakagawa T, Zhu H, Morishima N et al. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 2000; 403: 98-103</mixed-citation><mixed-citation xml:lang="en">Nakagawa T, Zhu H, Morishima N et al. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 2000; 403: 98-103</mixed-citation></citation-alternatives></ref><ref id="cit50"><label>50</label><citation-alternatives><mixed-citation xml:lang="ru">Rao RV, Hermel E, Castro-Obregon S et al. Coupling endoplasmic reticulum stress to the cell death program. Mechanism of caspase activation. J Biol Chem 2001; 276: 33869-33874</mixed-citation><mixed-citation xml:lang="en">Rao RV, Hermel E, Castro-Obregon S et al. Coupling endoplasmic reticulum stress to the cell death program. Mechanism of caspase activation. J Biol Chem 2001; 276: 33869-33874</mixed-citation></citation-alternatives></ref><ref id="cit51"><label>51</label><citation-alternatives><mixed-citation xml:lang="ru">Morishima N, Nakanishi K, Takenouchi H et al. An endoplasmic reticulum stress-specific caspase cascade in apoptosis. Cytochrome c-independent activation of caspase-9 by caspase-12. J Biol Chem 2002; 277: 34287-34294</mixed-citation><mixed-citation xml:lang="en">Morishima N, Nakanishi K, Takenouchi H et al. An endoplasmic reticulum stress-specific caspase cascade in apoptosis. Cytochrome c-independent activation of caspase-9 by caspase-12. J Biol Chem 2002; 277: 34287-34294</mixed-citation></citation-alternatives></ref><ref id="cit52"><label>52</label><citation-alternatives><mixed-citation xml:lang="ru">Hitomi J, Katayama T, Eguchi Y et al. Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Abeta-induced cell death. J Cell Biol 2004; 165: 347-356</mixed-citation><mixed-citation xml:lang="en">Hitomi J, Katayama T, Eguchi Y et al. Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Abeta-induced cell death. J Cell Biol 2004; 165: 347-356</mixed-citation></citation-alternatives></ref><ref id="cit53"><label>53</label><citation-alternatives><mixed-citation xml:lang="ru">Scorrano L, Oakes SA, Opferman JT et al. BAX and BAK regulation of endoplasmic reticulum Ca2+: A control point for apoptosis. Science 2003; 300: 135-139</mixed-citation><mixed-citation xml:lang="en">Scorrano L, Oakes SA, Opferman JT et al. BAX and BAK regulation of endoplasmic reticulum Ca2+: A control point for apoptosis. Science 2003; 300: 135-139</mixed-citation></citation-alternatives></ref><ref id="cit54"><label>54</label><citation-alternatives><mixed-citation xml:lang="ru">Zong WX, Li C, Hatzivassiliou G et al. Bax and Bak can localize to the endoplasmic reticulum to initiate apoptosis. J Cell Biol 2003; 162: 59-69</mixed-citation><mixed-citation xml:lang="en">Zong WX, Li C, Hatzivassiliou G et al. Bax and Bak can localize to the endoplasmic reticulum to initiate apoptosis. J Cell Biol 2003; 162: 59-69</mixed-citation></citation-alternatives></ref><ref id="cit55"><label>55</label><citation-alternatives><mixed-citation xml:lang="ru">Nakagawa T, Yuan J. Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis. J Cell Biol 2000; 150: 887-894</mixed-citation><mixed-citation xml:lang="en">Nakagawa T, Yuan J. Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis. J Cell Biol 2000; 150: 887-894</mixed-citation></citation-alternatives></ref><ref id="cit56"><label>56</label><citation-alternatives><mixed-citation xml:lang="ru">Orrenius S, Zhivotovsky B, Nicotera P. Regulation of cell death: the calcium-apoptosis link. Nat Rev Mol Cell Biol 2003; 4: 552-565</mixed-citation><mixed-citation xml:lang="en">Orrenius S, Zhivotovsky B, Nicotera P. Regulation of cell death: the calcium-apoptosis link. Nat Rev Mol Cell Biol 2003; 4: 552-565</mixed-citation></citation-alternatives></ref><ref id="cit57"><label>57</label><citation-alternatives><mixed-citation xml:lang="ru">Ryan PM, Bedard K, Breining T, Cribb AE. Disruption of the endoplasmic reticulum by cytotoxins in LLC-PK1 cells. Toxicol Lett 2005; 159: 154-163</mixed-citation><mixed-citation xml:lang="en">Ryan PM, Bedard K, Breining T, Cribb AE. Disruption of the endoplasmic reticulum by cytotoxins in LLC-PK1 cells. Toxicol Lett 2005; 159: 154-163</mixed-citation></citation-alternatives></ref><ref id="cit58"><label>58</label><citation-alternatives><mixed-citation xml:lang="ru">Muruganandan S, Cribb AE. Calpain-induced endoplasmic reticulum stress and cell death following cytotoxic damage to renal cells. Toxicol Sci 2006; 94 (1): 118-128</mixed-citation><mixed-citation xml:lang="en">Muruganandan S, Cribb AE. Calpain-induced endoplasmic reticulum stress and cell death following cytotoxic damage to renal cells. Toxicol Sci 2006; 94 (1): 118-128</mixed-citation></citation-alternatives></ref><ref id="cit59"><label>59</label><citation-alternatives><mixed-citation xml:lang="ru">Tan Y, Dourdin N, Wu C et al. Ubiquitous calpains promote caspase-12 and JNK activation during endoplasmic reticulum stress-induced apoptosis. J Biol Chem 2006; 281: 16016-16024</mixed-citation><mixed-citation xml:lang="en">Tan Y, Dourdin N, Wu C et al. Ubiquitous calpains promote caspase-12 and JNK activation during endoplasmic reticulum stress-induced apoptosis. J Biol Chem 2006; 281: 16016-16024</mixed-citation></citation-alternatives></ref><ref id="cit60"><label>60</label><citation-alternatives><mixed-citation xml:lang="ru">Gallego-Sandin S, Alonso MT, Garcia-Sancho J. Calcium homeostasis modulator 1 (CALHM1) reduces the calcium content of the endoplasmic reticulum (ER) and triggers ER stress. Biochem J 2011; 437 (3): 469-475</mixed-citation><mixed-citation xml:lang="en">Gallego-Sandin S, Alonso MT, Garcia-Sancho J. Calcium homeostasis modulator 1 (CALHM1) reduces the calcium content of the endoplasmic reticulum (ER) and triggers ER stress. Biochem J 2011; 437 (3): 469-475</mixed-citation></citation-alternatives></ref><ref id="cit61"><label>61</label><citation-alternatives><mixed-citation xml:lang="ru">Lin JH, Li H, Yasumura D et al. IRE1 signaling affects cell fate during the unfolded protein response. Science 2007; 318: 944-949</mixed-citation><mixed-citation xml:lang="en">Lin JH, Li H, Yasumura D et al. IRE1 signaling affects cell fate during the unfolded protein response. Science 2007; 318: 944-949</mixed-citation></citation-alternatives></ref><ref id="cit62"><label>62</label><citation-alternatives><mixed-citation xml:lang="ru">Rurkowski DT, Arnold SM, Miller CN et al. Adaptation to ER stress is mediated by differential stabilities of pro-survival and proapoptotic mRNAs and proteins. PLoS Biol 2006; 4: e374</mixed-citation><mixed-citation xml:lang="en">Rurkowski DT, Arnold SM, Miller CN et al. Adaptation to ER stress is mediated by differential stabilities of pro-survival and proapoptotic mRNAs and proteins. PLoS Biol 2006; 4: e374</mixed-citation></citation-alternatives></ref><ref id="cit63"><label>63</label><citation-alternatives><mixed-citation xml:lang="ru">Nakanishi K, Sudo T, Morishima N. Endoplasmic reticulum stress signaling transmitted by ATF6 mediates apoptosis during muscle development. J Cell Biol 2005; 169: 555-560</mixed-citation><mixed-citation xml:lang="en">Nakanishi K, Sudo T, Morishima N. Endoplasmic reticulum stress signaling transmitted by ATF6 mediates apoptosis during muscle development. J Cell Biol 2005; 169: 555-560</mixed-citation></citation-alternatives></ref><ref id="cit64"><label>64</label><citation-alternatives><mixed-citation xml:lang="ru">Wu J, Kaufman RJ. From acute ER stress to physiological roles of the unfolded protein response. Cell Death Differ 2006; 13: 374-384</mixed-citation><mixed-citation xml:lang="en">Wu J, Kaufman RJ. From acute ER stress to physiological roles of the unfolded protein response. Cell Death Differ 2006; 13: 374-384</mixed-citation></citation-alternatives></ref><ref id="cit65"><label>65</label><citation-alternatives><mixed-citation xml:lang="ru">Rush JS, Sweitzer T, Kent C et al. Biogenesis of the endoplasmic reticulum in activated B lymphocytes: temporal relationships between the induction of protein N-glycosylation activity and the biosynthesis of membrane protein and phospholipid. Arch Biochem Biophys 1991; 84: 63-70</mixed-citation><mixed-citation xml:lang="en">Rush JS, Sweitzer T, Kent C et al. Biogenesis of the endoplasmic reticulum in activated B lymphocytes: temporal relationships between the induction of protein N-glycosylation activity and the biosynthesis of membrane protein and phospholipid. Arch Biochem Biophys 1991; 84: 63-70</mixed-citation></citation-alternatives></ref><ref id="cit66"><label>66</label><citation-alternatives><mixed-citation xml:lang="ru">Reimold AM, Iwakoshi NN, Manis J et al. Plasma cell differentiation requires the transcription factor XBP1. Nature 2001; 412: 300-307</mixed-citation><mixed-citation xml:lang="en">Reimold AM, Iwakoshi NN, Manis J et al. Plasma cell differentiation requires the transcription factor XBP1. Nature 2001; 412: 300-307</mixed-citation></citation-alternatives></ref><ref id="cit67"><label>67</label><citation-alternatives><mixed-citation xml:lang="ru">Zhang K, Wong HN, Song B et al. The unfolded protein response sensor IRE1α is required at 2 distinct steps in B cell lymphopoiesis. J Clin Invest 2005; 115: 268-281</mixed-citation><mixed-citation xml:lang="en">Zhang K, Wong HN, Song B et al. The unfolded protein response sensor IRE1α is required at 2 distinct steps in B cell lymphopoiesis. J Clin Invest 2005; 115: 268-281</mixed-citation></citation-alternatives></ref><ref id="cit68"><label>68</label><citation-alternatives><mixed-citation xml:lang="ru">Iwakoshi NN, Lee AH, Vallabhajosyula P et al. Plasma cell differentiation and the unfolded protein response intersect at the transcription factor XBP1. Nat Immun 2003; 4: 321-329</mixed-citation><mixed-citation xml:lang="en">Iwakoshi NN, Lee AH, Vallabhajosyula P et al. Plasma cell differentiation and the unfolded protein response intersect at the transcription factor XBP1. Nat Immun 2003; 4: 321-329</mixed-citation></citation-alternatives></ref><ref id="cit69"><label>69</label><citation-alternatives><mixed-citation xml:lang="ru">Drori A, Tirosh B. Regulation of immunoglobulin synthesis, modification, and trafficking by unfolded protein response a quantitative approach. Methods Enzymol 2011; 491: 309-325</mixed-citation><mixed-citation xml:lang="en">Drori A, Tirosh B. Regulation of immunoglobulin synthesis, modification, and trafficking by unfolded protein response a quantitative approach. Methods Enzymol 2011; 491: 309-325</mixed-citation></citation-alternatives></ref><ref id="cit70"><label>70</label><citation-alternatives><mixed-citation xml:lang="ru">Delepine M, Nicolino M, Barrett T et al. EIFAK3, encoding translation initiation factor 2-α kinase 3, is mutated in patients with Wolcott-Rallison syndrome. Nat Genet 2000; 25: 406-409</mixed-citation><mixed-citation xml:lang="en">Delepine M, Nicolino M, Barrett T et al. EIFAK3, encoding translation initiation factor 2-α kinase 3, is mutated in patients with Wolcott-Rallison syndrome. Nat Genet 2000; 25: 406-409</mixed-citation></citation-alternatives></ref><ref id="cit71"><label>71</label><citation-alternatives><mixed-citation xml:lang="ru">Harding HP, Zeng H, Zhang Y et al. Diabetes mellitus and exocrine pancreatic dysfunction in perk -/- mice reveals a role for translational control in secretory cell survival. Mol Cell 2001; 7: 1153-1163</mixed-citation><mixed-citation xml:lang="en">Harding HP, Zeng H, Zhang Y et al. Diabetes mellitus and exocrine pancreatic dysfunction in perk -/- mice reveals a role for translational control in secretory cell survival. Mol Cell 2001; 7: 1153-1163</mixed-citation></citation-alternatives></ref><ref id="cit72"><label>72</label><citation-alternatives><mixed-citation xml:lang="ru">Reimold AM, Etkin A, Clauss I et al. An essential role in liver development for transcription factor XBP-1. Genes Dev 2000; 14: 152-157</mixed-citation><mixed-citation xml:lang="en">Reimold AM, Etkin A, Clauss I et al. An essential role in liver development for transcription factor XBP-1. Genes Dev 2000; 14: 152-157</mixed-citation></citation-alternatives></ref><ref id="cit73"><label>73</label><citation-alternatives><mixed-citation xml:lang="ru">Yang X, Matsuda K, Bialek P et al. ATF4 is a substrate of RSK2 and an essential regulator of osteoblast biology; implication for Coffin-Lowry syndrome. Cell 2004; 117: 387-398</mixed-citation><mixed-citation xml:lang="en">Yang X, Matsuda K, Bialek P et al. ATF4 is a substrate of RSK2 and an essential regulator of osteoblast biology; implication for Coffin-Lowry syndrome. Cell 2004; 117: 387-398</mixed-citation></citation-alternatives></ref><ref id="cit74"><label>74</label><citation-alternatives><mixed-citation xml:lang="ru">Zhang P, McGrath B, Li S et al. The PERK eukaryotic initiation factor 2α kinase is required for the development of skeletal system, postnatal growth, and the function and viability of the pancreas. Mol Cell Biol 2002; 22: 3864-3874</mixed-citation><mixed-citation xml:lang="en">Zhang P, McGrath B, Li S et al. The PERK eukaryotic initiation factor 2α kinase is required for the development of skeletal system, postnatal growth, and the function and viability of the pancreas. Mol Cell Biol 2002; 22: 3864-3874</mixed-citation></citation-alternatives></ref><ref id="cit75"><label>75</label><citation-alternatives><mixed-citation xml:lang="ru">Nakanishi K, Dohmae N, Morishima N. Endoplasmic reticulum stress increases myofiber formation in vitro. FASEB J 2007; 21: 2994-3003</mixed-citation><mixed-citation xml:lang="en">Nakanishi K, Dohmae N, Morishima N. Endoplasmic reticulum stress increases myofiber formation in vitro. FASEB J 2007; 21: 2994-3003</mixed-citation></citation-alternatives></ref><ref id="cit76"><label>76</label><citation-alternatives><mixed-citation xml:lang="ru">Ostergaard L, Simonsen U, Eskildsen-Helmond Y et al. Proteomics reveals lowering oxygen alters cytoskeletal and endoplasmic stress proteins in human endothelial cells. Proteomics 2009; 19: 4457-4467</mixed-citation><mixed-citation xml:lang="en">Ostergaard L, Simonsen U, Eskildsen-Helmond Y et al. Proteomics reveals lowering oxygen alters cytoskeletal and endoplasmic stress proteins in human endothelial cells. Proteomics 2009; 19: 4457-4467</mixed-citation></citation-alternatives></ref><ref id="cit77"><label>77</label><citation-alternatives><mixed-citation xml:lang="ru">Werno C, Zhou J, Brüne B. A 23187 ionomycin and thapsigargin upregulate mRNA of HIF-1 alpha via endoplasmic reticulum stress rather than a rise in intracellular calcium. J Cell Physiol 2008; 215: 798-714</mixed-citation><mixed-citation xml:lang="en">Werno C, Zhou J, Brüne B. A 23187 ionomycin and thapsigargin upregulate mRNA of HIF-1 alpha via endoplasmic reticulum stress rather than a rise in intracellular calcium. J Cell Physiol 2008; 215: 798-714</mixed-citation></citation-alternatives></ref><ref id="cit78"><label>78</label><citation-alternatives><mixed-citation xml:lang="ru">Gotoh T, Mori M. Nitric oxide and endoplasmic reticulum stress. Arterioscler Thromb Vasc Biol 2006; 26 (7): 1439-1446</mixed-citation><mixed-citation xml:lang="en">Gotoh T, Mori M. Nitric oxide and endoplasmic reticulum stress. Arterioscler Thromb Vasc Biol 2006; 26 (7): 1439-1446</mixed-citation></citation-alternatives></ref><ref id="cit79"><label>79</label><citation-alternatives><mixed-citation xml:lang="ru">Gotoh T, Oyadomari S, Mori K, Mori M. Nitric oxide-induced apoptosis in RAW 264.7 macrophages is mediated by endoplasmic reticulum stress pathway involving ATF6 and CHOP. J Biol Chem 2002; 277 (14): 12343-12350</mixed-citation><mixed-citation xml:lang="en">Gotoh T, Oyadomari S, Mori K, Mori M. Nitric oxide-induced apoptosis in RAW 264.7 macrophages is mediated by endoplasmic reticulum stress pathway involving ATF6 and CHOP. J Biol Chem 2002; 277 (14): 12343-12350</mixed-citation></citation-alternatives></ref><ref id="cit80"><label>80</label><citation-alternatives><mixed-citation xml:lang="ru">De Gracia DJ, Montie HL. Cerebral ischemia and the unfolded protein response. J Neurochem 2004; 91: 1-8</mixed-citation><mixed-citation xml:lang="en">De Gracia DJ, Montie HL. Cerebral ischemia and the unfolded protein response. J Neurochem 2004; 91: 1-8</mixed-citation></citation-alternatives></ref><ref id="cit81"><label>81</label><citation-alternatives><mixed-citation xml:lang="ru">Kohno K., Higuchi T, Ohta S et al. Neuroprotective nitric oxide synthase inhibitor reduces intracellular calcium accumulation following transient global ischemia in the gerbil. Neurosci Lett 1997; 224: 17-20</mixed-citation><mixed-citation xml:lang="en">Kohno K., Higuchi T, Ohta S et al. Neuroprotective nitric oxide synthase inhibitor reduces intracellular calcium accumulation following transient global ischemia in the gerbil. Neurosci Lett 1997; 224: 17-20</mixed-citation></citation-alternatives></ref><ref id="cit82"><label>82</label><citation-alternatives><mixed-citation xml:lang="ru">Xu KY, Huso DL, Dawson TM et al. Nitric oxide synthase in cardiac sarcoplasmic reticulum. Proc Sci USA 1999; 96: 657-662</mixed-citation><mixed-citation xml:lang="en">Xu KY, Huso DL, Dawson TM et al. Nitric oxide synthase in cardiac sarcoplasmic reticulum. Proc Sci USA 1999; 96: 657-662</mixed-citation></citation-alternatives></ref><ref id="cit83"><label>83</label><citation-alternatives><mixed-citation xml:lang="ru">Oyadomari S, Takeda K, Takiguchi M et al. Nitric oxideinduced apoptosis in pancreatic β cells is mediated by the endoplasmic reticulum stress pathway. Proc Natl Acad Sci USA 2001; 98 (19): 10845-10850</mixed-citation><mixed-citation xml:lang="en">Oyadomari S, Takeda K, Takiguchi M et al. Nitric oxideinduced apoptosis in pancreatic β cells is mediated by the endoplasmic reticulum stress pathway. Proc Natl Acad Sci USA 2001; 98 (19): 10845-10850</mixed-citation></citation-alternatives></ref><ref id="cit84"><label>84</label><citation-alternatives><mixed-citation xml:lang="ru">Inagi R. Endoplasmic reticulum stress as a progression factor for kidney injury. Curr Opin Pharmacol 2010; 10 (2): 156-165</mixed-citation><mixed-citation xml:lang="en">Inagi R. Endoplasmic reticulum stress as a progression factor for kidney injury. Curr Opin Pharmacol 2010; 10 (2): 156-165</mixed-citation></citation-alternatives></ref><ref id="cit85"><label>85</label><citation-alternatives><mixed-citation xml:lang="ru">Dickhout JG, Hossain GS, Pozza LM et al. Peroxynitrite causes endoplasmic reticulum stress and apoptosis in human vascular endothelium: implications in atherogenesis. Arterioscler Thromb Vasc Biol 2005; 25: 2623-2629</mixed-citation><mixed-citation xml:lang="en">Dickhout JG, Hossain GS, Pozza LM et al. Peroxynitrite causes endoplasmic reticulum stress and apoptosis in human vascular endothelium: implications in atherogenesis. Arterioscler Thromb Vasc Biol 2005; 25: 2623-2629</mixed-citation></citation-alternatives></ref><ref id="cit86"><label>86</label><citation-alternatives><mixed-citation xml:lang="ru">Malhotra JD, Miao H, Zhang K et al. Antioxidants reduce endoplasmic reticulum stress and improve protein secretion. Proc Natl Sci USA 2008; 105 (47): 18525-18530</mixed-citation><mixed-citation xml:lang="en">Malhotra JD, Miao H, Zhang K et al. Antioxidants reduce endoplasmic reticulum stress and improve protein secretion. Proc Natl Sci USA 2008; 105 (47): 18525-18530</mixed-citation></citation-alternatives></ref><ref id="cit87"><label>87</label><citation-alternatives><mixed-citation xml:lang="ru">Hayashi T, Saito A, Okuno S et al. Oxidative damage to the endoplasmic reticulum is implicated in ischemic neuronal death. J Cereb Blood Flow Metabol 2003; 23: 1117-1128</mixed-citation><mixed-citation xml:lang="en">Hayashi T, Saito A, Okuno S et al. Oxidative damage to the endoplasmic reticulum is implicated in ischemic neuronal death. J Cereb Blood Flow Metabol 2003; 23: 1117-1128</mixed-citation></citation-alternatives></ref><ref id="cit88"><label>88</label><citation-alternatives><mixed-citation xml:lang="ru">Yokouchi M, Hiramatsu N, Hayakawa K et al. Involvement of selective reactive oxygen species upstream of proapoptotic branches of unfolded protein response. J Biol Chem 2008; 283 (7): 4252-4260</mixed-citation><mixed-citation xml:lang="en">Yokouchi M, Hiramatsu N, Hayakawa K et al. Involvement of selective reactive oxygen species upstream of proapoptotic branches of unfolded protein response. J Biol Chem 2008; 283 (7): 4252-4260</mixed-citation></citation-alternatives></ref><ref id="cit89"><label>89</label><citation-alternatives><mixed-citation xml:lang="ru">Cullinan SB, Diehl JA. Coordination of ER and oxidative stress signaling: the PERK/Nrf2 signaling pathway. Int J Biochem Cell Biol 2006; 38 (3): 317-332</mixed-citation><mixed-citation xml:lang="en">Cullinan SB, Diehl JA. Coordination of ER and oxidative stress signaling: the PERK/Nrf2 signaling pathway. Int J Biochem Cell Biol 2006; 38 (3): 317-332</mixed-citation></citation-alternatives></ref><ref id="cit90"><label>90</label><citation-alternatives><mixed-citation xml:lang="ru">Back SH, Scheuner D, Han J et al. Translation attenuation through eIF2alpha phosphorylation prevents oxidative stress and maintains the differentiated state in beta cells. Cell Metab 2009; 10: 13-26</mixed-citation><mixed-citation xml:lang="en">Back SH, Scheuner D, Han J et al. Translation attenuation through eIF2alpha phosphorylation prevents oxidative stress and maintains the differentiated state in beta cells. Cell Metab 2009; 10: 13-26</mixed-citation></citation-alternatives></ref><ref id="cit91"><label>91</label><citation-alternatives><mixed-citation xml:lang="ru">Viner RI, Hühmer AF, Bigelow DJ, Schöneich C. The oxidative inactivation of sarcoplasmic reticulum Ca2+-ATPase by peroxinitrite. Free Radic Res 1996; 24: 243-259</mixed-citation><mixed-citation xml:lang="en">Viner RI, Hühmer AF, Bigelow DJ, Schöneich C. The oxidative inactivation of sarcoplasmic reticulum Ca2+-ATPase by peroxinitrite. Free Radic Res 1996; 24: 243-259</mixed-citation></citation-alternatives></ref><ref id="cit92"><label>92</label><citation-alternatives><mixed-citation xml:lang="ru">Moreau VH, Castilho RF, Ferreira ST, Carvalho-Alves PC. Oxidative damage to sarcoplasmic reticulum Ca2+-ATPase at submicromolar iron concentrations: evidence for metal-catalyzed oxidation. Free Radic Biol Med 1998; 25: 554-560</mixed-citation><mixed-citation xml:lang="en">Moreau VH, Castilho RF, Ferreira ST, Carvalho-Alves PC. Oxidative damage to sarcoplasmic reticulum Ca2+-ATPase at submicromolar iron concentrations: evidence for metal-catalyzed oxidation. Free Radic Biol Med 1998; 25: 554-560</mixed-citation></citation-alternatives></ref><ref id="cit93"><label>93</label><citation-alternatives><mixed-citation xml:lang="ru">Kaplan P, Babusikova E, Lehotsky J, Dobrota D. Free radicalinduced protein modification and inhibition of Ca2+-ATPase of cardiac sarcoplasmic reticulum. Mol Cell Biochem 2003; 248: 41-47</mixed-citation><mixed-citation xml:lang="en">Kaplan P, Babusikova E, Lehotsky J, Dobrota D. Free radicalinduced protein modification and inhibition of Ca2+-ATPase of cardiac sarcoplasmic reticulum. Mol Cell Biochem 2003; 248: 41-47</mixed-citation></citation-alternatives></ref><ref id="cit94"><label>94</label><citation-alternatives><mixed-citation xml:lang="ru">Brunet S, Thibault L, Lepage G et al. Modulation of endoplasmic reticulum-bound cholesterol regulatory enzymes by iron/ ascorbate-mediated lipid peroxidation. Free Radic Biol Med 2000; 28: 46-54</mixed-citation><mixed-citation xml:lang="en">Brunet S, Thibault L, Lepage G et al. Modulation of endoplasmic reticulum-bound cholesterol regulatory enzymes by iron/ ascorbate-mediated lipid peroxidation. Free Radic Biol Med 2000; 28: 46-54</mixed-citation></citation-alternatives></ref><ref id="cit95"><label>95</label><citation-alternatives><mixed-citation xml:lang="ru">Hung CC, Ichimura T, Stevens JL, Bonventre JV. Protection of renal epithelial cells against oxidative injury by endoplasmic reticulum stress preconditioning is mediated by ERK ½ activation. J Biol Chem 2003; 278 (31): 29317-29326</mixed-citation><mixed-citation xml:lang="en">Hung CC, Ichimura T, Stevens JL, Bonventre JV. Protection of renal epithelial cells against oxidative injury by endoplasmic reticulum stress preconditioning is mediated by ERK ½ activation. J Biol Chem 2003; 278 (31): 29317-29326</mixed-citation></citation-alternatives></ref><ref id="cit96"><label>96</label><citation-alternatives><mixed-citation xml:lang="ru">Zhang K, Kaufman RJ. From endoplasmic-reticulum stress to the inflammatory response. Nature 2008; 454: 455-462</mixed-citation><mixed-citation xml:lang="en">Zhang K, Kaufman RJ. From endoplasmic-reticulum stress to the inflammatory response. Nature 2008; 454: 455-462</mixed-citation></citation-alternatives></ref><ref id="cit97"><label>97</label><citation-alternatives><mixed-citation xml:lang="ru">Lin W, Harding HP, Ron D, Popko B. Endoplasmic reticulum stress modulates the response of myelinating oligodendrocytes to the immune cytokine interferon-γ. J Cell Biol 2005; 169: 603-612</mixed-citation><mixed-citation xml:lang="en">Lin W, Harding HP, Ron D, Popko B. Endoplasmic reticulum stress modulates the response of myelinating oligodendrocytes to the immune cytokine interferon-γ. J Cell Biol 2005; 169: 603-612</mixed-citation></citation-alternatives></ref><ref id="cit98"><label>98</label><citation-alternatives><mixed-citation xml:lang="ru">Endo M, Mori M, Akira S, Gotoh T. C/EBR homologous protein (CHOP) is crucial for the induction of caspase-11 and the pathogenesis of lipopolysaccharide-induced inflammation. J Immunol 2006; 176: 6245-6253</mixed-citation><mixed-citation xml:lang="en">Endo M, Mori M, Akira S, Gotoh T. C/EBR homologous protein (CHOP) is crucial for the induction of caspase-11 and the pathogenesis of lipopolysaccharide-induced inflammation. J Immunol 2006; 176: 6245-6253</mixed-citation></citation-alternatives></ref><ref id="cit99"><label>99</label><citation-alternatives><mixed-citation xml:lang="ru">Hiramatsu N, Kasai A, Hayakawa K et al. Real-time detection and continuous monitoring of ER stress in vitro and in vivo by ES-TRAP: evidence for systemic transient ER stress during endotoxemia. Nucleic Acids Res 2006; 34: e93</mixed-citation><mixed-citation xml:lang="en">Hiramatsu N, Kasai A, Hayakawa K et al. Real-time detection and continuous monitoring of ER stress in vitro and in vivo by ES-TRAP: evidence for systemic transient ER stress during endotoxemia. Nucleic Acids Res 2006; 34: e93</mixed-citation></citation-alternatives></ref><ref id="cit100"><label>100</label><citation-alternatives><mixed-citation xml:lang="ru">Nagaraju K, Casciola-Rosen L, Lundberg I et al. Activation of the endoplasmic reticulum stress response in autoimmune myositis: potential role in muscle fiber damage and dysfunction. Arthritis Rheum 2005; 52: 1824-1835</mixed-citation><mixed-citation xml:lang="en">Nagaraju K, Casciola-Rosen L, Lundberg I et al. Activation of the endoplasmic reticulum stress response in autoimmune myositis: potential role in muscle fiber damage and dysfunction. Arthritis Rheum 2005; 52: 1824-1835</mixed-citation></citation-alternatives></ref><ref id="cit101"><label>101</label><citation-alternatives><mixed-citation xml:lang="ru">Yamasaki S, Yagishita N, Tsuchimochi K et al. Rheumatoid arthritis as a hyperendoplasmic-reticulum-associated degradation disease. Arthritis Res Ther 2005; 7: 181-186</mixed-citation><mixed-citation xml:lang="en">Yamasaki S, Yagishita N, Tsuchimochi K et al. Rheumatoid arthritis as a hyperendoplasmic-reticulum-associated degradation disease. Arthritis Res Ther 2005; 7: 181-186</mixed-citation></citation-alternatives></ref><ref id="cit102"><label>102</label><citation-alternatives><mixed-citation xml:lang="ru">Pahl HL, Baeuerle PA. A novel signal transduction pathway from the endoplasmic reticulum to the nucleus is mediated by transcription factor NF-κB. EMBO J 1995; 14: 2580-2588</mixed-citation><mixed-citation xml:lang="en">Pahl HL, Baeuerle PA. A novel signal transduction pathway from the endoplasmic reticulum to the nucleus is mediated by transcription factor NF-κB. EMBO J 1995; 14: 2580-2588</mixed-citation></citation-alternatives></ref><ref id="cit103"><label>103</label><citation-alternatives><mixed-citation xml:lang="ru">Jiang HY, Wek SA, McGrath BC et al. Phosphorylation of the α subunit of eukaryotic initiation factor 2 is required for activation of NF-κB in response to diverse cellular stresses. Mol Cell Biol 2003; 23: 5651-5663</mixed-citation><mixed-citation xml:lang="en">Jiang HY, Wek SA, McGrath BC et al. Phosphorylation of the α subunit of eukaryotic initiation factor 2 is required for activation of NF-κB in response to diverse cellular stresses. Mol Cell Biol 2003; 23: 5651-5663</mixed-citation></citation-alternatives></ref><ref id="cit104"><label>104</label><citation-alternatives><mixed-citation xml:lang="ru">Deng J, Lu PD, Zhang Y et al. Translational repression mediates activation of nuclear factor-κB by phosphorylated translation initiation factor 2. Mol Cell Biol 2004; 24: 10161-10168</mixed-citation><mixed-citation xml:lang="en">Deng J, Lu PD, Zhang Y et al. Translational repression mediates activation of nuclear factor-κB by phosphorylated translation initiation factor 2. Mol Cell Biol 2004; 24: 10161-10168</mixed-citation></citation-alternatives></ref><ref id="cit105"><label>105</label><citation-alternatives><mixed-citation xml:lang="ru">Xu C, Bailly-Maitre B, Reed JC. Endoplasmic reticulum stress: cell life and death decisions. J Clin Invest 2005; 115: 2656- 2664</mixed-citation><mixed-citation xml:lang="en">Xu C, Bailly-Maitre B, Reed JC. Endoplasmic reticulum stress: cell life and death decisions. J Clin Invest 2005; 115: 2656- 2664</mixed-citation></citation-alternatives></ref><ref id="cit106"><label>106</label><citation-alternatives><mixed-citation xml:lang="ru">Kaneko M, Niinuma Y, Nomura Y. Activation signal of nuclear factor-κB in response to endoplasmic reticulum stress is transduced via IRE1 and tumor necrosis factor receptor-associated factor 2. Biol Pharm Bull 2003; 26: 931-935</mixed-citation><mixed-citation xml:lang="en">Kaneko M, Niinuma Y, Nomura Y. Activation signal of nuclear factor-κB in response to endoplasmic reticulum stress is transduced via IRE1 and tumor necrosis factor receptor-associated factor 2. Biol Pharm Bull 2003; 26: 931-935</mixed-citation></citation-alternatives></ref><ref id="cit107"><label>107</label><citation-alternatives><mixed-citation xml:lang="ru">Hu P, Han Z, Couvillon AD et al. Autocrine tumor necrosis factor-α links endoplasmic reticulum stress to the membrane death receptor pathway through IRE1α-mediated NF-κB activation and downregulation of TRAF2 expression. Mol Cell Biol 2006; 26: 3071-3084</mixed-citation><mixed-citation xml:lang="en">Hu P, Han Z, Couvillon AD et al. Autocrine tumor necrosis factor-α links endoplasmic reticulum stress to the membrane death receptor pathway through IRE1α-mediated NF-κB activation and downregulation of TRAF2 expression. Mol Cell Biol 2006; 26: 3071-3084</mixed-citation></citation-alternatives></ref><ref id="cit108"><label>108</label><citation-alternatives><mixed-citation xml:lang="ru">Shkoda A, Ruiz PA, Daniel H et al. Interleukin-10 blocked endoplasmic reticulum stress in intestinal epithelial cells: impact on chronic inflammation. Gastroenterology 2007; 132: 190-207</mixed-citation><mixed-citation xml:lang="en">Shkoda A, Ruiz PA, Daniel H et al. Interleukin-10 blocked endoplasmic reticulum stress in intestinal epithelial cells: impact on chronic inflammation. Gastroenterology 2007; 132: 190-207</mixed-citation></citation-alternatives></ref><ref id="cit109"><label>109</label><citation-alternatives><mixed-citation xml:lang="ru">Maguire JA, Mulugeta S, Beers MF. Endoplasmic reticulum stress induced by surfactant protein C BRICHOS mutants promotes proinflammatory signaling by epithelial cells. Am J Respir Cell Mol Biol 2011; 44 (3): 404-414</mixed-citation><mixed-citation xml:lang="en">Maguire JA, Mulugeta S, Beers MF. Endoplasmic reticulum stress induced by surfactant protein C BRICHOS mutants promotes proinflammatory signaling by epithelial cells. Am J Respir Cell Mol Biol 2011; 44 (3): 404-414</mixed-citation></citation-alternatives></ref><ref id="cit110"><label>110</label><citation-alternatives><mixed-citation xml:lang="ru">Fougeray S, Bouvier N, Beaune P et al. Metabolic stress promotes renal tubular inflammation by triggering the unfolded protein response. Cell Death Dis 2011; 2: e143</mixed-citation><mixed-citation xml:lang="en">Fougeray S, Bouvier N, Beaune P et al. Metabolic stress promotes renal tubular inflammation by triggering the unfolded protein response. Cell Death Dis 2011; 2: e143</mixed-citation></citation-alternatives></ref><ref id="cit111"><label>111</label><citation-alternatives><mixed-citation xml:lang="ru">Takano Y, Hiramatsu N, Okamura M et al. Suppression of cytokine response by GATA inhibitor K-7174 via unfolded protein response. Biochem Biophys Res Commun 2007; 360: 470-475</mixed-citation><mixed-citation xml:lang="en">Takano Y, Hiramatsu N, Okamura M et al. Suppression of cytokine response by GATA inhibitor K-7174 via unfolded protein response. Biochem Biophys Res Commun 2007; 360: 470-475</mixed-citation></citation-alternatives></ref><ref id="cit112"><label>112</label><citation-alternatives><mixed-citation xml:lang="ru">Hayakawa K, Hiramatsu N, Okamura M et al. Blunted activation of NF-κB and NF-κB-dependent gene expression by geranylgeranylacetone: involvement of unfolded protein response. Biochem Biophys Res Commun 2008; 365: 47-53</mixed-citation><mixed-citation xml:lang="en">Hayakawa K, Hiramatsu N, Okamura M et al. Blunted activation of NF-κB and NF-κB-dependent gene expression by geranylgeranylacetone: involvement of unfolded protein response. Biochem Biophys Res Commun 2008; 365: 47-53</mixed-citation></citation-alternatives></ref><ref id="cit113"><label>113</label><citation-alternatives><mixed-citation xml:lang="ru">Hayakawa K, Hiramatsu N, Okamura M et al. Acquisition of energy to proinflammatory cytokines in nonimmune cells through endoplasmic reticulum stress response: a mechanism for subsidence of inflammation. J Immunol 2009; 182 (2): 1182-1191</mixed-citation><mixed-citation xml:lang="en">Hayakawa K, Hiramatsu N, Okamura M et al. Acquisition of energy to proinflammatory cytokines in nonimmune cells through endoplasmic reticulum stress response: a mechanism for subsidence of inflammation. J Immunol 2009; 182 (2): 1182-1191</mixed-citation></citation-alternatives></ref><ref id="cit114"><label>114</label><citation-alternatives><mixed-citation xml:lang="ru">Forman MS, Lee VM, Trojanowski JQ. “Unfolding” pathways is neurodegenerative disease. Trends Neurosci 2003; 26: 407-410</mixed-citation><mixed-citation xml:lang="en">Forman MS, Lee VM, Trojanowski JQ. “Unfolding” pathways is neurodegenerative disease. Trends Neurosci 2003; 26: 407-410</mixed-citation></citation-alternatives></ref><ref id="cit115"><label>115</label><citation-alternatives><mixed-citation xml:lang="ru">Onuki R, Bando Y, Suyama E et al. An RNA-dependent protein kinase is involved in tunicamycin-induced apoptosis and Alzheimer’s disease. EMBO J 2004; 23: 959-968</mixed-citation><mixed-citation xml:lang="en">Onuki R, Bando Y, Suyama E et al. An RNA-dependent protein kinase is involved in tunicamycin-induced apoptosis and Alzheimer’s disease. EMBO J 2004; 23: 959-968</mixed-citation></citation-alternatives></ref><ref id="cit116"><label>116</label><citation-alternatives><mixed-citation xml:lang="ru">Hoozemans JJ, Veerhuis R, Van Haastert ES et al. The unfolded protein response is activated in Alzheimer’s disease. Acta Neuropathol (Berl) 2005; 110: 165-172</mixed-citation><mixed-citation xml:lang="en">Hoozemans JJ, Veerhuis R, Van Haastert ES et al. The unfolded protein response is activated in Alzheimer’s disease. Acta Neuropathol (Berl) 2005; 110: 165-172</mixed-citation></citation-alternatives></ref><ref id="cit117"><label>117</label><citation-alternatives><mixed-citation xml:lang="ru">Conn KJ, Gao W, McKee A et al. Identification of the protein disulfide isomerase family member PDlp in experimental Parkinson’s disease and Lewy body pathology. Brain Res 2004; 1022 (1-2): 164-172</mixed-citation><mixed-citation xml:lang="en">Conn KJ, Gao W, McKee A et al. Identification of the protein disulfide isomerase family member PDlp in experimental Parkinson’s disease and Lewy body pathology. Brain Res 2004; 1022 (1-2): 164-172</mixed-citation></citation-alternatives></ref><ref id="cit118"><label>118</label><citation-alternatives><mixed-citation xml:lang="ru">Holtz WA, O’Malley KL. Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons. J Biol Chem 2003; 278 (21): 19367-19377</mixed-citation><mixed-citation xml:lang="en">Holtz WA, O’Malley KL. Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons. J Biol Chem 2003; 278 (21): 19367-19377</mixed-citation></citation-alternatives></ref><ref id="cit119"><label>119</label><citation-alternatives><mixed-citation xml:lang="ru">Yoshida H. ER stress and diseases. FEBS J 2007; 274: 630-658</mixed-citation><mixed-citation xml:lang="en">Yoshida H. ER stress and diseases. FEBS J 2007; 274: 630-658</mixed-citation></citation-alternatives></ref><ref id="cit120"><label>120</label><citation-alternatives><mixed-citation xml:lang="ru">Kharroubi I, Ladrière L, Cardozo AK et al. Free fatty acids and cytokines induce pancreatic beta-cell apoptosis by different mechanisms: role of nuclear factor-kappa B and endoplasmic reticulum stress. Endocrinology 2004; 145: 5087-5096</mixed-citation><mixed-citation xml:lang="en">Kharroubi I, Ladrière L, Cardozo AK et al. Free fatty acids and cytokines induce pancreatic beta-cell apoptosis by different mechanisms: role of nuclear factor-kappa B and endoplasmic reticulum stress. Endocrinology 2004; 145: 5087-5096</mixed-citation></citation-alternatives></ref><ref id="cit121"><label>121</label><citation-alternatives><mixed-citation xml:lang="ru">Karaskov E, Scott C, Zhang L et al. Chronic palmitate but not oleate exposure induces endoplasmic reticulum stress, which may contribute to INS-1 pancreatic beta-cell apoptosis. Endocrinology 2006; 147: 3398-3407</mixed-citation><mixed-citation xml:lang="en">Karaskov E, Scott C, Zhang L et al. Chronic palmitate but not oleate exposure induces endoplasmic reticulum stress, which may contribute to INS-1 pancreatic beta-cell apoptosis. Endocrinology 2006; 147: 3398-3407</mixed-citation></citation-alternatives></ref><ref id="cit122"><label>122</label><citation-alternatives><mixed-citation xml:lang="ru">Cnop M, Ladrière L, Hekerman P et al. Selective inhibition of eukaryotic translation initiation factor 2alpha dephosphorylation potentiates fatty acid-induced endoplasmic reticulum stress and causes pancreatic beta-cell dysfunction and apoptosis. J Biol Chem 2007; 282: 3989-3997</mixed-citation><mixed-citation xml:lang="en">Cnop M, Ladrière L, Hekerman P et al. Selective inhibition of eukaryotic translation initiation factor 2alpha dephosphorylation potentiates fatty acid-induced endoplasmic reticulum stress and causes pancreatic beta-cell dysfunction and apoptosis. J Biol Chem 2007; 282: 3989-3997</mixed-citation></citation-alternatives></ref><ref id="cit123"><label>123</label><citation-alternatives><mixed-citation xml:lang="ru">Bach JF. Insulin-dependent diabetes mellitus as an autoimmune disease. Endocr Rev 1994; 15: 516-542</mixed-citation><mixed-citation xml:lang="en">Bach JF. Insulin-dependent diabetes mellitus as an autoimmune disease. Endocr Rev 1994; 15: 516-542</mixed-citation></citation-alternatives></ref><ref id="cit124"><label>124</label><citation-alternatives><mixed-citation xml:lang="ru">Delovitch TL, Singh B. The nonobese diabetic mouse as a model of autoimmune diabetes: immune dysregulation gets the NOD. Immunity 1997; 7: 727-738</mixed-citation><mixed-citation xml:lang="en">Delovitch TL, Singh B. The nonobese diabetic mouse as a model of autoimmune diabetes: immune dysregulation gets the NOD. Immunity 1997; 7: 727-738</mixed-citation></citation-alternatives></ref><ref id="cit125"><label>125</label><citation-alternatives><mixed-citation xml:lang="ru">Nozaki J, Kubota H, Yoshida H et al. The endoplasmic reticulum stress response is stimulated through the continuous activation of transcription factors ATF6 and XBP1 in Ins2+/Akita pancreatic β cells. Genes Cells 2004; 9: 261-270</mixed-citation><mixed-citation xml:lang="en">Nozaki J, Kubota H, Yoshida H et al. The endoplasmic reticulum stress response is stimulated through the continuous activation of transcription factors ATF6 and XBP1 in Ins2+/Akita pancreatic β cells. Genes Cells 2004; 9: 261-270</mixed-citation></citation-alternatives></ref><ref id="cit126"><label>126</label><citation-alternatives><mixed-citation xml:lang="ru">Scheuner D, Mierde DV, Song B et al. Control of mRNA translation preserves endoplasmic reticulum function in beta cells and maintains glucose homeostasis. Nat Med 2005; 11: 757-764</mixed-citation><mixed-citation xml:lang="en">Scheuner D, Mierde DV, Song B et al. Control of mRNA translation preserves endoplasmic reticulum function in beta cells and maintains glucose homeostasis. Nat Med 2005; 11: 757-764</mixed-citation></citation-alternatives></ref><ref id="cit127"><label>127</label><citation-alternatives><mixed-citation xml:lang="ru">Oyadomari S, Koizumi A, Takeda K et al. Targeted disruption of the Chop gene delays endoplasmic reticulum stress-induced diabetes. J Clin Invest 2002; 109: 525-532</mixed-citation><mixed-citation xml:lang="en">Oyadomari S, Koizumi A, Takeda K et al. Targeted disruption of the Chop gene delays endoplasmic reticulum stress-induced diabetes. J Clin Invest 2002; 109: 525-532</mixed-citation></citation-alternatives></ref><ref id="cit128"><label>128</label><citation-alternatives><mixed-citation xml:lang="ru">Cnop M, Welsh N, Jonas JC et al. Mechanisms of pancreatic beta-cell death in type 1 and type 2 diabetes: many differences, few similarities. Diabetes 2005; 54: 97-107</mixed-citation><mixed-citation xml:lang="en">Cnop M, Welsh N, Jonas JC et al. Mechanisms of pancreatic beta-cell death in type 1 and type 2 diabetes: many differences, few similarities. Diabetes 2005; 54: 97-107</mixed-citation></citation-alternatives></ref><ref id="cit129"><label>129</label><citation-alternatives><mixed-citation xml:lang="ru">Bradshaw E, Raddassi K, Elyaman W et al. Monocytes from patients with type 1 diabetes spontaneously secrete pro-inflammatory cytokines inducing Th17. J immunol 2009; 183 (7): 4432-4439</mixed-citation><mixed-citation xml:lang="en">Bradshaw E, Raddassi K, Elyaman W et al. Monocytes from patients with type 1 diabetes spontaneously secrete pro-inflammatory cytokines inducing Th17. J immunol 2009; 183 (7): 4432-4439</mixed-citation></citation-alternatives></ref><ref id="cit130"><label>130</label><citation-alternatives><mixed-citation xml:lang="ru">Araki E, Oyadomari S, Mori M. Impact of endoplasmic reticulum stress pathway on pancreatic beta-cells and diabetes mellitus. Exp Biol Med 2003; 228: 1213-1217</mixed-citation><mixed-citation xml:lang="en">Araki E, Oyadomari S, Mori M. Impact of endoplasmic reticulum stress pathway on pancreatic beta-cells and diabetes mellitus. Exp Biol Med 2003; 228: 1213-1217</mixed-citation></citation-alternatives></ref><ref id="cit131"><label>131</label><citation-alternatives><mixed-citation xml:lang="ru">Cardozo AK, Ortis F, Storling J et al. Cytokines downregulate the sarcoendoplasmic reticulum pump Ca2+-ATPase 2b and deplete endoplasmic reticulum Ca2+, leading to induction of endoplasmic reticulum stress in pancreatic beta-cells. Diabetes 2005; 54: 452-461</mixed-citation><mixed-citation xml:lang="en">Cardozo AK, Ortis F, Storling J et al. Cytokines downregulate the sarcoendoplasmic reticulum pump Ca2+-ATPase 2b and deplete endoplasmic reticulum Ca2+, leading to induction of endoplasmic reticulum stress in pancreatic beta-cells. Diabetes 2005; 54: 452-461</mixed-citation></citation-alternatives></ref><ref id="cit132"><label>132</label><citation-alternatives><mixed-citation xml:lang="ru">Eizirik DL, Flodström M, Karlsen AE, Welsh N. The harmony of spheres: inducible nitric oxide synthase and related genes in pancreatic beta cells. Diabetologia 1996; 39: 875-890</mixed-citation><mixed-citation xml:lang="en">Eizirik DL, Flodström M, Karlsen AE, Welsh N. The harmony of spheres: inducible nitric oxide synthase and related genes in pancreatic beta cells. Diabetologia 1996; 39: 875-890</mixed-citation></citation-alternatives></ref><ref id="cit133"><label>133</label><citation-alternatives><mixed-citation xml:lang="ru">Cardozo AK, Heimberg H, Heremans Y et al. A comprehensive analysis of cytokine-induced and nuclear factor-kappa Bdependent genes in primary rat pancreatic beta-cells. J Biol Chem 2001; 276: 48879-48886</mixed-citation><mixed-citation xml:lang="en">Cardozo AK, Heimberg H, Heremans Y et al. A comprehensive analysis of cytokine-induced and nuclear factor-kappa Bdependent genes in primary rat pancreatic beta-cells. J Biol Chem 2001; 276: 48879-48886</mixed-citation></citation-alternatives></ref><ref id="cit134"><label>134</label><citation-alternatives><mixed-citation xml:lang="ru">Casciola-Rosen LA, Anhalt GJ, Rosen A. DNA-dependent protein kinase is one of a subset of autoantigens specifically cleaved early during apoptosis. J Exp Med 1995; 182: 1625-1634</mixed-citation><mixed-citation xml:lang="en">Casciola-Rosen LA, Anhalt GJ, Rosen A. DNA-dependent protein kinase is one of a subset of autoantigens specifically cleaved early during apoptosis. J Exp Med 1995; 182: 1625-1634</mixed-citation></citation-alternatives></ref><ref id="cit135"><label>135</label><citation-alternatives><mixed-citation xml:lang="ru">Butler AE, Janson J, Bonner-Weir S et al. Beta-cell deficit and increased beta-cell apoptosis in humans with type 2 diabetes. Diabetes 2003; 52: 102-110</mixed-citation><mixed-citation xml:lang="en">Butler AE, Janson J, Bonner-Weir S et al. Beta-cell deficit and increased beta-cell apoptosis in humans with type 2 diabetes. Diabetes 2003; 52: 102-110</mixed-citation></citation-alternatives></ref><ref id="cit136"><label>136</label><citation-alternatives><mixed-citation xml:lang="ru">Marchetti P, Bulgiani M, Lupi R et al. The endoplasmic reticulum in pancreatic beta cells of type 2 diabetes patients. Diabetologia 2007; 50 (12): 2486-2494</mixed-citation><mixed-citation xml:lang="en">Marchetti P, Bulgiani M, Lupi R et al. The endoplasmic reticulum in pancreatic beta cells of type 2 diabetes patients. Diabetologia 2007; 50 (12): 2486-2494</mixed-citation></citation-alternatives></ref><ref id="cit137"><label>137</label><citation-alternatives><mixed-citation xml:lang="ru">Nakatani Y, Kaneto H, Kawamori D et al. Involvement of endoplasmic reticulum stress in insulin resistance and diabetes. J Biol Chem 2005; 280 (1): 847-851</mixed-citation><mixed-citation xml:lang="en">Nakatani Y, Kaneto H, Kawamori D et al. Involvement of endoplasmic reticulum stress in insulin resistance and diabetes. J Biol Chem 2005; 280 (1): 847-851</mixed-citation></citation-alternatives></ref><ref id="cit138"><label>138</label><citation-alternatives><mixed-citation xml:lang="ru">Ozcan U, Cao Q, Yilmaz E et al. Endoplasmic reticulum stress links obesity, insulin action, and type 2 diabetes. Science 2004; 206: 457-461</mixed-citation><mixed-citation xml:lang="en">Ozcan U, Cao Q, Yilmaz E et al. Endoplasmic reticulum stress links obesity, insulin action, and type 2 diabetes. Science 2004; 206: 457-461</mixed-citation></citation-alternatives></ref><ref id="cit139"><label>139</label><citation-alternatives><mixed-citation xml:lang="ru">Ozcan U, Yilmaz E, Ozcan L et al. Chemical chaperones reduce ER stress and restore glucose homeostasis in a mouse model of type 2 diabetes. Science 2006; 313: 1137-1140</mixed-citation><mixed-citation xml:lang="en">Ozcan U, Yilmaz E, Ozcan L et al. Chemical chaperones reduce ER stress and restore glucose homeostasis in a mouse model of type 2 diabetes. Science 2006; 313: 1137-1140</mixed-citation></citation-alternatives></ref><ref id="cit140"><label>140</label><citation-alternatives><mixed-citation xml:lang="ru">Toth A, Nickson P, Mandl A et al. Endoplasmic reticulum stress as a novel therapeutic target in heart diseases. Cardiovasc Hematol Disord Drug Targets 2007; 7 (3): 205-218</mixed-citation><mixed-citation xml:lang="en">Toth A, Nickson P, Mandl A et al. Endoplasmic reticulum stress as a novel therapeutic target in heart diseases. Cardiovasc Hematol Disord Drug Targets 2007; 7 (3): 205-218</mixed-citation></citation-alternatives></ref><ref id="cit141"><label>141</label><citation-alternatives><mixed-citation xml:lang="ru">Groenendyk J, Sreenivasaiah PK, Kim do H et al. Biology of endoplasmic reticulum stress in the heart. Cir Res 2010; 107 (10): 1185-1197</mixed-citation><mixed-citation xml:lang="en">Groenendyk J, Sreenivasaiah PK, Kim do H et al. Biology of endoplasmic reticulum stress in the heart. Cir Res 2010; 107 (10): 1185-1197</mixed-citation></citation-alternatives></ref><ref id="cit142"><label>142</label><citation-alternatives><mixed-citation xml:lang="ru">Minamino T, Kitakaze M. ER stress in cardiovascular disease. J Mol Cell Cardiol 2010; 48 (6): 1105-1110</mixed-citation><mixed-citation xml:lang="en">Minamino T, Kitakaze M. ER stress in cardiovascular disease. J Mol Cell Cardiol 2010; 48 (6): 1105-1110</mixed-citation></citation-alternatives></ref><ref id="cit143"><label>143</label><citation-alternatives><mixed-citation xml:lang="ru">Aleshin AN, Sawa Y, Kitagawa-Sakakida S et al. 150-kDa oxygen-regulated protein attenuates myocardial ischemia-reperfusion injury in rat heart. J Mol Cell Cardiol 2005; 38: 517-525</mixed-citation><mixed-citation xml:lang="en">Aleshin AN, Sawa Y, Kitagawa-Sakakida S et al. 150-kDa oxygen-regulated protein attenuates myocardial ischemia-reperfusion injury in rat heart. J Mol Cell Cardiol 2005; 38: 517-525</mixed-citation></citation-alternatives></ref><ref id="cit144"><label>144</label><citation-alternatives><mixed-citation xml:lang="ru">Azfer A, Niu J, Rogers LM et al. Activation of endoplasmic reticulum stress response during the development of ischemic heart disease. Am J Physiol Heart Circ Physiol 2006; 291: H1411-H1420</mixed-citation><mixed-citation xml:lang="en">Azfer A, Niu J, Rogers LM et al. Activation of endoplasmic reticulum stress response during the development of ischemic heart disease. Am J Physiol Heart Circ Physiol 2006; 291: H1411-H1420</mixed-citation></citation-alternatives></ref><ref id="cit145"><label>145</label><citation-alternatives><mixed-citation xml:lang="ru">Thuerauf DJ, Marcinko M, Gude N et al. Activation of the unfolded protein response in infracted mouse heart and hypoxic cultured cardiac myocytes. Circ Res 2006; 99 (3): 275-282</mixed-citation><mixed-citation xml:lang="en">Thuerauf DJ, Marcinko M, Gude N et al. Activation of the unfolded protein response in infracted mouse heart and hypoxic cultured cardiac myocytes. Circ Res 2006; 99 (3): 275-282</mixed-citation></citation-alternatives></ref><ref id="cit146"><label>146</label><citation-alternatives><mixed-citation xml:lang="ru">Martindale JJ, Fernandez R, Thuerauf D et al. Endoplasmic reticulum stress gene induction and protection from ischemia/ reperfusion injury in the hearts of transgenic mice with a tamoxifenregulated form of ATF6. Circ Res 2006; 98 (9): 1186-1193</mixed-citation><mixed-citation xml:lang="en">Martindale JJ, Fernandez R, Thuerauf D et al. Endoplasmic reticulum stress gene induction and protection from ischemia/ reperfusion injury in the hearts of transgenic mice with a tamoxifenregulated form of ATF6. Circ Res 2006; 98 (9): 1186-1193</mixed-citation></citation-alternatives></ref><ref id="cit147"><label>147</label><citation-alternatives><mixed-citation xml:lang="ru">Miyazaki Y, Kaikita K, Endo M et al. C/EBP homologous protein deficiency attenuates myocardial reperfusion injury by inhibiting myocardial apoptosis and inflammation. Arterioscler Thromb Vasc Biol 2011; 31 (5): 1124-1132</mixed-citation><mixed-citation xml:lang="en">Miyazaki Y, Kaikita K, Endo M et al. C/EBP homologous protein deficiency attenuates myocardial reperfusion injury by inhibiting myocardial apoptosis and inflammation. Arterioscler Thromb Vasc Biol 2011; 31 (5): 1124-1132</mixed-citation></citation-alternatives></ref><ref id="cit148"><label>148</label><citation-alternatives><mixed-citation xml:lang="ru">Xin W, Lu X, Li X et al. Attenuation of endoplasmic reticulum stress-related myocardial apoptosis by SERCA2a gene delivery in ischemic heart disease. Mol Med 2011; 17 (3-4): 201-210</mixed-citation><mixed-citation xml:lang="en">Xin W, Lu X, Li X et al. Attenuation of endoplasmic reticulum stress-related myocardial apoptosis by SERCA2a gene delivery in ischemic heart disease. Mol Med 2011; 17 (3-4): 201-210</mixed-citation></citation-alternatives></ref><ref id="cit149"><label>149</label><citation-alternatives><mixed-citation xml:lang="ru">Lu F, Tian Z, Zhang W et al. Calcium-sensing receptors induce apoptosis in rat cardiomyocytes via the endo(sarco)plasmic reticulum pathway during hypoxia/reoxygenation. Basic Clin Pharmacol Toxicol 2010; 106 (5): 396-405</mixed-citation><mixed-citation xml:lang="en">Lu F, Tian Z, Zhang W et al. Calcium-sensing receptors induce apoptosis in rat cardiomyocytes via the endo(sarco)plasmic reticulum pathway during hypoxia/reoxygenation. Basic Clin Pharmacol Toxicol 2010; 106 (5): 396-405</mixed-citation></citation-alternatives></ref><ref id="cit150"><label>150</label><citation-alternatives><mixed-citation xml:lang="ru">Yeh C-H, Chen T-P, Wang Y-C et al. AMP-activated protein kinase activation during cardioplegia-induced hypoxia/reoxygenation injury attenuates cardiomyocytic apoptosis via regulation of endoplasmic reticulum stress. Mediators Inflamm 2010; 2010: 130636</mixed-citation><mixed-citation xml:lang="en">Yeh C-H, Chen T-P, Wang Y-C et al. AMP-activated protein kinase activation during cardioplegia-induced hypoxia/reoxygenation injury attenuates cardiomyocytic apoptosis via regulation of endoplasmic reticulum stress. Mediators Inflamm 2010; 2010: 130636</mixed-citation></citation-alternatives></ref><ref id="cit151"><label>151</label><citation-alternatives><mixed-citation xml:lang="ru">Belmont PJ, Chen WJ, San Pedro MN et al. Roles for endoplasmic reticulum-associated degradation and the novel endoplasmic reticulum stress response gene derlin-3 in the ischemic heart. Circ Res 2010; 106: 307-316</mixed-citation><mixed-citation xml:lang="en">Belmont PJ, Chen WJ, San Pedro MN et al. Roles for endoplasmic reticulum-associated degradation and the novel endoplasmic reticulum stress response gene derlin-3 in the ischemic heart. Circ Res 2010; 106: 307-316</mixed-citation></citation-alternatives></ref><ref id="cit152"><label>152</label><citation-alternatives><mixed-citation xml:lang="ru">Toko H, Takahashi H, Kayama Y et al. ANF6 is important under both pathological and physiological states in the heart. J Mol Cell Cardiol 2010; 49 (1): 113-120</mixed-citation><mixed-citation xml:lang="en">Toko H, Takahashi H, Kayama Y et al. ANF6 is important under both pathological and physiological states in the heart. J Mol Cell Cardiol 2010; 49 (1): 113-120</mixed-citation></citation-alternatives></ref><ref id="cit153"><label>153</label><citation-alternatives><mixed-citation xml:lang="ru">Toldo S, Severino A, Abbate A, Baldi A. The role of PDI as a survival factor in cardiomyocyte ischemia. Methods Enzymol 2011; 489: 47-65</mixed-citation><mixed-citation xml:lang="en">Toldo S, Severino A, Abbate A, Baldi A. The role of PDI as a survival factor in cardiomyocyte ischemia. Methods Enzymol 2011; 489: 47-65</mixed-citation></citation-alternatives></ref><ref id="cit154"><label>154</label><citation-alternatives><mixed-citation xml:lang="ru">Karki P, Fliegel L. Overexpression of the NHE1 isoform of the Na(+)/H(+) exchanger causes elevated apoptosis in isolated cardiomyocytes after hypoxia/reoxygenation challenge. Mol Cell Biochem 2010; 338 (1-2): 47-57</mixed-citation><mixed-citation xml:lang="en">Karki P, Fliegel L. Overexpression of the NHE1 isoform of the Na(+)/H(+) exchanger causes elevated apoptosis in isolated cardiomyocytes after hypoxia/reoxygenation challenge. Mol Cell Biochem 2010; 338 (1-2): 47-57</mixed-citation></citation-alternatives></ref><ref id="cit155"><label>155</label><citation-alternatives><mixed-citation xml:lang="ru">Зверев ЯФ, Брюханов ВМ. Ингибирование Na+/H+ обмена как новый подход к защите миокарда от ишемического и реперфузионного повреждения. Обзоры клин фармакол и лек терап 2003; 2 (3): 16-34</mixed-citation><mixed-citation xml:lang="en">Зверев ЯФ, Брюханов ВМ. Ингибирование Na+/H+ обмена как новый подход к защите миокарда от ишемического и реперфузионного повреждения. Обзоры клин фармакол и лек терап 2003; 2 (3): 16-34</mixed-citation></citation-alternatives></ref><ref id="cit156"><label>156</label><citation-alternatives><mixed-citation xml:lang="ru">Zhang Z-Y, Liu X-H, Hu W-C et al. The calcineurin-myocyte enhancer factor 2c pathway mediates cardiac hypertrophy induced by endoplasmic reticulum stress in neonatal cardiomyocytes. Am J Physiol Heart Circulat Physiol 2010; 298 (5): H1499-H1509</mixed-citation><mixed-citation xml:lang="en">Zhang Z-Y, Liu X-H, Hu W-C et al. The calcineurin-myocyte enhancer factor 2c pathway mediates cardiac hypertrophy induced by endoplasmic reticulum stress in neonatal cardiomyocytes. Am J Physiol Heart Circulat Physiol 2010; 298 (5): H1499-H1509</mixed-citation></citation-alternatives></ref><ref id="cit157"><label>157</label><citation-alternatives><mixed-citation xml:lang="ru">Dickhout JG, Carlisle RE, Austin RC. Interrelationship between cardiac hypertrophy, heart failure, and chronic kidney disease. Endoplasmic reticulum stress as a mediator of pathogenesis. Circ Res 2011; 108: 629-642</mixed-citation><mixed-citation xml:lang="en">Dickhout JG, Carlisle RE, Austin RC. Interrelationship between cardiac hypertrophy, heart failure, and chronic kidney disease. Endoplasmic reticulum stress as a mediator of pathogenesis. Circ Res 2011; 108: 629-642</mixed-citation></citation-alternatives></ref><ref id="cit158"><label>158</label><citation-alternatives><mixed-citation xml:lang="ru">Okada K, Minamino T, Tsukamoto Y et al. Prolonged endoplasmic reticulum stress in hypertrophic and failing heart after aortic constriction: possible contribution of endoplasmic reticulum stress to cardiac myocyte apoptosis. Circulation 2004; 110 (6): 705-712</mixed-citation><mixed-citation xml:lang="en">Okada K, Minamino T, Tsukamoto Y et al. Prolonged endoplasmic reticulum stress in hypertrophic and failing heart after aortic constriction: possible contribution of endoplasmic reticulum stress to cardiac myocyte apoptosis. Circulation 2004; 110 (6): 705-712</mixed-citation></citation-alternatives></ref><ref id="cit159"><label>159</label><citation-alternatives><mixed-citation xml:lang="ru">Wu T, Dong Z, Geng J et al. Valsartan protects against ER stress-induced myocardial apoptosis via CHOP/Puma signaling pathway in streptozotocin-induced diabetic rats. Eur J Pharm Sci 2011; 42 (5): 496-502</mixed-citation><mixed-citation xml:lang="en">Wu T, Dong Z, Geng J et al. Valsartan protects against ER stress-induced myocardial apoptosis via CHOP/Puma signaling pathway in streptozotocin-induced diabetic rats. Eur J Pharm Sci 2011; 42 (5): 496-502</mixed-citation></citation-alternatives></ref><ref id="cit160"><label>160</label><citation-alternatives><mixed-citation xml:lang="ru">Hamid T, Guo SZ, Kingery JR et al. Cardiomyocyte NF- B p65 promotes adverse remodeling, apoptosis, and endoplasmic reticulum stress in heart failure. Cardiovasc Res 2011; 89 (1): 129-138</mixed-citation><mixed-citation xml:lang="en">Hamid T, Guo SZ, Kingery JR et al. Cardiomyocyte NF- B p65 promotes adverse remodeling, apoptosis, and endoplasmic reticulum stress in heart failure. Cardiovasc Res 2011; 89 (1): 129-138</mixed-citation></citation-alternatives></ref><ref id="cit161"><label>161</label><citation-alternatives><mixed-citation xml:lang="ru">Sun Y, Liu G, Song T et al. Upregulation of GRP78 and caspase-12 in diastolic failing heart. Acta Biochim Pol 2008; 55 (3): 511-516</mixed-citation><mixed-citation xml:lang="en">Sun Y, Liu G, Song T et al. Upregulation of GRP78 and caspase-12 in diastolic failing heart. Acta Biochim Pol 2008; 55 (3): 511-516</mixed-citation></citation-alternatives></ref><ref id="cit162"><label>162</label><citation-alternatives><mixed-citation xml:lang="ru">Avery J, Etzion S, DeBosch BJ et al. TRB3 function in cardiac endoplasmic reticulum stress. Cir Res 2010;106 (9): 1516-1523</mixed-citation><mixed-citation xml:lang="en">Avery J, Etzion S, DeBosch BJ et al. TRB3 function in cardiac endoplasmic reticulum stress. Cir Res 2010;106 (9): 1516-1523</mixed-citation></citation-alternatives></ref><ref id="cit163"><label>163</label><citation-alternatives><mixed-citation xml:lang="ru">Isodono K, Takahashi T, Imoto H et al. PARM-1 is an endoplasmic reticulum molecule involved in endoplasmic reticulum stress-induced apoptosis in rat cardiac myocytes. PLoS One 2010; 5 (3): e9746</mixed-citation><mixed-citation xml:lang="en">Isodono K, Takahashi T, Imoto H et al. PARM-1 is an endoplasmic reticulum molecule involved in endoplasmic reticulum stress-induced apoptosis in rat cardiac myocytes. PLoS One 2010; 5 (3): e9746</mixed-citation></citation-alternatives></ref><ref id="cit164"><label>164</label><citation-alternatives><mixed-citation xml:lang="ru">Hamada H, Suzuki M, Yuasa S et al. Dilated cardiomyopathy caused by aberrant endoplasmic reticulum quality control in mutant KDEL receptor transgenic mice. Mol Cell Biol 2004; 24 (18): 8007-8017</mixed-citation><mixed-citation xml:lang="en">Hamada H, Suzuki M, Yuasa S et al. Dilated cardiomyopathy caused by aberrant endoplasmic reticulum quality control in mutant KDEL receptor transgenic mice. Mol Cell Biol 2004; 24 (18): 8007-8017</mixed-citation></citation-alternatives></ref><ref id="cit165"><label>165</label><citation-alternatives><mixed-citation xml:lang="ru">Mao W, Fukuoka S, Iwai C et al. Cardiomyocyte apoptosis in autoimmune cardiomiopathy: mediated via endoplasmic reticulum stress and exaggerated by norepinephrine. Am J Physiol Heart Circ Physiol 2007; 293 (3): H1636-H1645</mixed-citation><mixed-citation xml:lang="en">Mao W, Fukuoka S, Iwai C et al. Cardiomyocyte apoptosis in autoimmune cardiomiopathy: mediated via endoplasmic reticulum stress and exaggerated by norepinephrine. Am J Physiol Heart Circ Physiol 2007; 293 (3): H1636-H1645</mixed-citation></citation-alternatives></ref><ref id="cit166"><label>166</label><citation-alternatives><mixed-citation xml:lang="ru">Mao W, Iwai C, Liu J et al. Darbepoetin alpha exerts cardioprotective effect in autoimmune cardiomyopathy via reduction of ER stress and activation of the PI3K/Akt and STAT3 pathways. J Mol Cell Cardiol 2008; 45 (2): 250-260</mixed-citation><mixed-citation xml:lang="en">Mao W, Iwai C, Liu J et al. Darbepoetin alpha exerts cardioprotective effect in autoimmune cardiomyopathy via reduction of ER stress and activation of the PI3K/Akt and STAT3 pathways. J Mol Cell Cardiol 2008; 45 (2): 250-260</mixed-citation></citation-alternatives></ref><ref id="cit167"><label>167</label><citation-alternatives><mixed-citation xml:lang="ru">Shimazaki H, Watanabe K, Veeraveedu PT et al. The antioxidant edaravone attenuates ER-stress-mediated cardiac apoptosis and dysfunction in rats with autoimmune myocarditis. Free Radic Res 2010; 44 (9): 1082-1090</mixed-citation><mixed-citation xml:lang="en">Shimazaki H, Watanabe K, Veeraveedu PT et al. The antioxidant edaravone attenuates ER-stress-mediated cardiac apoptosis and dysfunction in rats with autoimmune myocarditis. Free Radic Res 2010; 44 (9): 1082-1090</mixed-citation></citation-alternatives></ref><ref id="cit168"><label>168</label><citation-alternatives><mixed-citation xml:lang="ru">Sukumaran V, Watanabe K, Veeraveedu PT et al. Olmesartan, an AT1 antagonist, attenuates oxidative stress, endoplasmic reticulum stress and cardiac inflammatory mediators in rats with heart failure induced by experimental autoimmune myocarditis. Int J Biol Sci 2011; 7 (2): 154-167</mixed-citation><mixed-citation xml:lang="en">Sukumaran V, Watanabe K, Veeraveedu PT et al. Olmesartan, an AT1 antagonist, attenuates oxidative stress, endoplasmic reticulum stress and cardiac inflammatory mediators in rats with heart failure induced by experimental autoimmune myocarditis. Int J Biol Sci 2011; 7 (2): 154-167</mixed-citation></citation-alternatives></ref><ref id="cit169"><label>169</label><citation-alternatives><mixed-citation xml:lang="ru">Werstuck GH, Lentz SR, Dayal S et al. Homocysteineinduced endoplasmic reticulum stress causes dysregulation of the cholesterol and triglyceride biosynthetic pathways. J Clin Invest 2001; 107: 1263-1273</mixed-citation><mixed-citation xml:lang="en">Werstuck GH, Lentz SR, Dayal S et al. Homocysteineinduced endoplasmic reticulum stress causes dysregulation of the cholesterol and triglyceride biosynthetic pathways. J Clin Invest 2001; 107: 1263-1273</mixed-citation></citation-alternatives></ref><ref id="cit170"><label>170</label><citation-alternatives><mixed-citation xml:lang="ru">Myoishi M, Hao H, Minamino T et al. Increased endoplasmic reticulum stress in atherosclerotic plaques associated with acute coronary syndrome. Circulation 2007; 116 (11): 1226-1233</mixed-citation><mixed-citation xml:lang="en">Myoishi M, Hao H, Minamino T et al. Increased endoplasmic reticulum stress in atherosclerotic plaques associated with acute coronary syndrome. Circulation 2007; 116 (11): 1226-1233</mixed-citation></citation-alternatives></ref><ref id="cit171"><label>171</label><citation-alternatives><mixed-citation xml:lang="ru">Tsukano H, Gotoh T, Endo M et al. The endoplasmic reticulum stress-C/EBP homologous protein pathway-mediated apoptosis in macrophages contributes to the instability of atherosclerotic plaques. Arterioscler Thromb Vasc Biol 2010; 30 (10): 1925-1932</mixed-citation><mixed-citation xml:lang="en">Tsukano H, Gotoh T, Endo M et al. The endoplasmic reticulum stress-C/EBP homologous protein pathway-mediated apoptosis in macrophages contributes to the instability of atherosclerotic plaques. Arterioscler Thromb Vasc Biol 2010; 30 (10): 1925-1932</mixed-citation></citation-alternatives></ref><ref id="cit172"><label>172</label><citation-alternatives><mixed-citation xml:lang="ru">Feldman DE, Chauhan V, Koong AC. The unfolded protein response: a novel component of the hypoxic stress response in tumors. Mol Cancer Res 2005; 3: 597-605</mixed-citation><mixed-citation xml:lang="en">Feldman DE, Chauhan V, Koong AC. The unfolded protein response: a novel component of the hypoxic stress response in tumors. Mol Cancer Res 2005; 3: 597-605</mixed-citation></citation-alternatives></ref><ref id="cit173"><label>173</label><citation-alternatives><mixed-citation xml:lang="ru">Ledoux S, Yang R, Friedlander G, Laouari D. Glucose depletion enhances P-glycoprotein expression in hepatoma cells: role of endoplasmic reticulum stress response. Cancer Res 2003; 63: 7284-7290</mixed-citation><mixed-citation xml:lang="en">Ledoux S, Yang R, Friedlander G, Laouari D. Glucose depletion enhances P-glycoprotein expression in hepatoma cells: role of endoplasmic reticulum stress response. Cancer Res 2003; 63: 7284-7290</mixed-citation></citation-alternatives></ref><ref id="cit174"><label>174</label><citation-alternatives><mixed-citation xml:lang="ru">Ozawa K, Tsukamoto Y, Hori O et al. Regulation of tumor angiogenesis by oxygen-regulated protein 150, an inducible endoplasmic reticulum chaperone. Cancer Res 2001; 61: 4206-4213</mixed-citation><mixed-citation xml:lang="en">Ozawa K, Tsukamoto Y, Hori O et al. Regulation of tumor angiogenesis by oxygen-regulated protein 150, an inducible endoplasmic reticulum chaperone. Cancer Res 2001; 61: 4206-4213</mixed-citation></citation-alternatives></ref><ref id="cit175"><label>175</label><citation-alternatives><mixed-citation xml:lang="ru">Abcouwer SF, Marjon PL, Loper RK, Vander Jagt DL. Response of VEGF expression to amino acid deprivation and inducers of endoplasmic reticulum stress. Invest Ophthalmol Vis Sci 2002; 43: 2791-2798</mixed-citation><mixed-citation xml:lang="en">Abcouwer SF, Marjon PL, Loper RK, Vander Jagt DL. Response of VEGF expression to amino acid deprivation and inducers of endoplasmic reticulum stress. Invest Ophthalmol Vis Sci 2002; 43: 2791-2798</mixed-citation></citation-alternatives></ref><ref id="cit176"><label>176</label><citation-alternatives><mixed-citation xml:lang="ru">Ozawa K, Kuwabara K, Tamatani M et al. 150-kDa oxygenregulated protein (ORP150) suppresses hypoxia-induced apoptotic cell death. J Biol Chem 1999; 274: 6397-6404</mixed-citation><mixed-citation xml:lang="en">Ozawa K, Kuwabara K, Tamatani M et al. 150-kDa oxygenregulated protein (ORP150) suppresses hypoxia-induced apoptotic cell death. J Biol Chem 1999; 274: 6397-6404</mixed-citation></citation-alternatives></ref><ref id="cit177"><label>177</label><citation-alternatives><mixed-citation xml:lang="ru">Kaufman RJ. Orchestrating the unfolded protein response in health and disease. J Clin Invest 2002; 110: 1389-1398</mixed-citation><mixed-citation xml:lang="en">Kaufman RJ. Orchestrating the unfolded protein response in health and disease. J Clin Invest 2002; 110: 1389-1398</mixed-citation></citation-alternatives></ref><ref id="cit178"><label>178</label><citation-alternatives><mixed-citation xml:lang="ru">Kakiuchi C, Iwamoto K, Ishiwata M et al. Impaired feedback regulation of XBP1 as a genetic risk factor for bipolar disorder. Nat Genet 2003; 35: 171-175</mixed-citation><mixed-citation xml:lang="en">Kakiuchi C, Iwamoto K, Ishiwata M et al. Impaired feedback regulation of XBP1 as a genetic risk factor for bipolar disorder. Nat Genet 2003; 35: 171-175</mixed-citation></citation-alternatives></ref><ref id="cit179"><label>179</label><citation-alternatives><mixed-citation xml:lang="ru">Kakiuchi C, Ishiwata M, Nanko S et al. Functional polymorphisms of HSPA5: possible association with bipolar disorder. Biochem Biophys Res Commun 2005; 336: 1136-1143</mixed-citation><mixed-citation xml:lang="en">Kakiuchi C, Ishiwata M, Nanko S et al. Functional polymorphisms of HSPA5: possible association with bipolar disorder. Biochem Biophys Res Commun 2005; 336: 1136-1143</mixed-citation></citation-alternatives></ref><ref id="cit180"><label>180</label><citation-alternatives><mixed-citation xml:lang="ru">Shao L, Sun X, Xu L et al. Mood stabilizing drug lithium increases expression of endoplasmic reticulum stress proteins in primary cultured rat cerebral cortical cells. Life Sci 2006; 78: 1317-1323</mixed-citation><mixed-citation xml:lang="en">Shao L, Sun X, Xu L et al. Mood stabilizing drug lithium increases expression of endoplasmic reticulum stress proteins in primary cultured rat cerebral cortical cells. Life Sci 2006; 78: 1317-1323</mixed-citation></citation-alternatives></ref><ref id="cit181"><label>181</label><citation-alternatives><mixed-citation xml:lang="ru">Tamtani M, Matsuyama T, Yamaguchi A. ORP 150 protects against hypoxia/ischemia-induced neuronal death. Nat Med 2001; 7: 317-323</mixed-citation><mixed-citation xml:lang="en">Tamtani M, Matsuyama T, Yamaguchi A. ORP 150 protects against hypoxia/ischemia-induced neuronal death. Nat Med 2001; 7: 317-323</mixed-citation></citation-alternatives></ref><ref id="cit182"><label>182</label><citation-alternatives><mixed-citation xml:lang="ru">Tajiri S, Oyadomari S, Yano S et al. Ischemia-induced neuronal cell death is mediated by the endoplasmic reticulum stress pathway involving CHOP. Cell Death Differ 2004; 11: 403-415</mixed-citation><mixed-citation xml:lang="en">Tajiri S, Oyadomari S, Yano S et al. Ischemia-induced neuronal cell death is mediated by the endoplasmic reticulum stress pathway involving CHOP. Cell Death Differ 2004; 11: 403-415</mixed-citation></citation-alternatives></ref><ref id="cit183"><label>183</label><citation-alternatives><mixed-citation xml:lang="ru">Rissanen A, Sivenius J, Jolkkonen J. Prolonged bihemispheric alterations in unfolded protein response related gene expression after experimental stroke. Brain Res 2006; 1087: 60-66</mixed-citation><mixed-citation xml:lang="en">Rissanen A, Sivenius J, Jolkkonen J. Prolonged bihemispheric alterations in unfolded protein response related gene expression after experimental stroke. Brain Res 2006; 1087: 60-66</mixed-citation></citation-alternatives></ref></ref-list><fn-group><fn fn-type="conflict"><p>The authors declare that there are no conflicts of interest present.</p></fn></fn-group></back></article>
