nefrНефрологияNephrology (Saint-Petersburg)1561-62742541-9439Pavlov First Saint-Petersburg State Medical Universitynefr-201Research ArticleПЕРЕДОВАЯ СТАТЬЯLEADING ARTICLEЛаминины в структуре гломерулярной базальной мембраныLaminines in the structure of glomerular basement membraneБатюшинМ. М.BatiushinM. M.batjushin-m@ramb1er.ruПасечникД. Г.PasechnicD. G.pathanob2@rambler.ruГосударственное бюджетное образовательное учреждение высшего профессионального образования «Ростовский государственный медицинский университет» Министерства здравоохранения Российской ФедерацииРоссияRostov State Medical UniversityRussian Federation201601092016205915Copyright © Батюшин М.М., Пасечник Д.Г., 20162016Батюшин М.М., Пасечник Д.Г.Batiushin M.M., Pasechnic D.G.Данная работа распространяется под лицензией Creative Commons Attribution 4.0.This work is licensed under a Creative Commons Attribution 4.0 License.https://journal.nephrolog.ru/jour/article/view/201

Ламинины - семейство крупных гликозилированных протеинов, связывающихся друг с другом и формирующих по меньшей мере 15 гетеротримерных макромолекул. Ламинин-521 является одним из основных молекул в гломерулярной базальной мембране и синтезируется подоцитами и эндотелиоцитами. Большинство ламининов формируют крестообразную структуру, короткие глобулярные отростки которой (LN-домены) отвечают за межламининовое взаимодействие во внеклеточной среде. Такое взаимодействие приводит к полимеризации ламинина, лежащей в основе формирования пространства базальной мембраны. Полимеризация ламининов формирует сетчатую структуру, напоминающую кристаллическую. Причем, в естественных условиях этот процесс не происходит в жидкостях, для него необходима связь ламининов с клеточными рецепторами. Домены LG1-3 ламининов связываются преимущественно с интегринами, а LG4-5 - с а-дистрогликаном (a-DG), гепарансульфатом и сульфатированными гликолипидами (сульфатиды). Исследование мутации ламинина в лабораторных условиях позволяет детально изучить его вероятную роль в развитии гломерулопатий и ремоделировании гломерулярной мембраны при патологических процессах.

Laminines are high weighted glycosylated proteins that communicate with each other and forming at least 15 heterotrimeric macromolecules. Laminin-521 is one of the key molecules in the glomerular basal membrane and is synthesized by podocytes and endothelial cells. The majority of laminins form a cruciform structure, short globular processes of which (LN-domains) are responsible for laminin interaction in the extracellular environment. This interaction leads to polymerization of laminin, underlying the formation of the basal membrane. Polymerization of laminins forms a mesh crystalloid structure. Moreover, the polymerization of laminins in vivo does not occur in liquids, this process requires the connection of laminins with cellular receptors. Domains LG1-3 laminine are associated primarily with integrins, and LG4-5 - with α-dystroglycan (a-DG), heparan sulfate and sulfated glycolipids (sulfatide). The research of laminin mutations in the laboratory allows to study in details its probable role in the development of glomerulopathy and glomerular membrane remodeling in pathological processes.

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The authors declare that there are no conflicts of interest present.