Dynamics of biophysical characteristics of albumin in patients on programmed hemodialysis

Background. One of the components of the metabolome that performs multifaceted functions in homeostasis is blood albumin. The albumin molecule has a pronounced hydrophilicity, due to which it plays an important role in maintaining oncotic blood pressure. Thus, the expansion of knowledge about the interrelationships of traditional biochemical information about the concentration of albumin and the biophysical properties of its derivatives complements the idea of the pharmacological effect of albumin transfusions. THE AIM: to study of the biophysical properties of albumin in patients with chronic kidney disease on programmed hemodialysis.

Patients and Methods. The study included 29 patients with chronic renal failure treated with programmed bicarbonate hemodialysis for an average of 110 months. To assess the condition of patients, a complex of laboratory studies was used, including hematological examination on Beckman Coulter analyzers; clinical assessment of nutritional status based on data from the analysis of medical histories; assessment of colloidal osmotic blood pressure by calculation, as well as by direct measurement on a BMT 923 oncometer; measurement of particle size in blood plasma by dynamic light scattering on a Photocor Compact spectrometer- Z. Statistical analysis of the material was performed using the Statistica for Windows v.6.0 software package. The null statistical hypothesis of the absence of differences and connections was rejected at p<0.05. RESULTS. The average correlation coefficient of oncotic pressure was 0.94 for total protein and 0.90 for albumin. Measurement of colloidal osmotic pressure showed a significant increase in pressure in each of the postdialysis samples. The hydrodynamic radius of the albumin peak for the predialysis sample is significantly higher, which may indicate a change in the sorption properties of the albumin surface. CONCLUSION. The calculation of oncotic pressure by the concentration of total protein, as a rule, provides clinical needs, however, with a significant concentration of toxins, clinical situations are possible in which a moderate decrease in the concentration of the "total protein" of the blood is detected, hence the main oncotic component – albumin is noted but there is a development pronounced edematous syndrome due to a significant decrease in oncotic pressure as a result of a conformational change in albumin molecules. In such situations, it is necessary to directly determine the oncotic pressure of the blood. Keywords: albumin, oncotic pressure, hydrodynamic radius, dialysis>˂0.05.

Results. The average correlation coefficient of oncotic pressure was 0.94 for total protein and 0.90 for albumin. Measurement of colloidal osmotic pressure showed a significant increase in pressure in each of the postdialysis samples. The hydrodynamic radius of the albumin peak for the predialysis sample is significantly higher, which may indicate a change in the sorption properties of the albumin surface.

Conclusion. The calculation of oncotic pressure by the concentration of total protein, as a rule, provides clinical needs, however, with a significant concentration of toxins, clinical situations are possible in which a moderate decrease in the concentration of the "total protein" of the blood is detected, hence the main oncotic component – albumin is noted but there is a development pronounced edematous syndrome due to a significant decrease in oncotic pressure as a result of a conformational change in albumin molecules. In such situations, it is necessary to directly determine the oncotic pressure of the blood.

1. Arosio P, Muller T, Rajah L, Yates EV, Aprile FA, Zhang Y, Knowles TP. Microfluidic diffusion analysis of the sizes and interactions of proteins under native solution conditions. ACS nano 2016; 10(1): 333–341. https://doi.org/10.1021/acsnano.5b04713

2. Jr TP. All About Albumin: Biochemistry, Genetics, and Medical Applications. Academic Press; 1995

3. Zubina IM, Tugusheva FA, Kulikova AI. The role of sulfhydryl groups of serum albumin in blood of patients with chronic glomerulonephritis in the maintenance of native conformation of protein. Nefrologiya 2002;6(2):39–46. (In Russ) https://doi.org/10.24884/1561-6274-2002-6-2-39-46

4. Kozhevnikov AD. The role of modified serum albumin in pathogenesis of renal diseases: some facts and hypotheses. Nefrologiya 1997;1(3):34–38. (In Russ) https://doi.org/10.24884/1561-6274-1997-1-3-34-38

5. Kulikova AI, Zubina IM, Tugusheva FA. The state of serum albumin in uraemic patients treated with chronic haemodialysis. Nefrologiya 2002;6(1):59–67. (In Russ) https://doi.org/10.24884/1561-6274-2002-6-1-59-67

6. Tugusheva FA, Zubina IM, Kulikova AI, Kozlov VV, Bondarenko IB. The use of the fluorescent method of determination of the total end the effective serum albumin concentration in patients with renal diseases. Nefrologiya 1998;2(4):37–42. (In Russ) https://doi.org/10.24884/1561-6274-1998-2-4-37-42

7. Vanholder R, Fouque D, Glorieux G et al. Clinical management of the uraemic syndrome in chronic kidney disease. Lancet Diabetes Endocrinol 2016;4:360–373. https://doi.org/10.1016/S2213-8587(16)00033-4

8. Viaene L, Annaert P, Loor de H, Poesen R, Evenepoel P, Meijers B. Albumin is the main plasma binding protein for indoxyl sulfate and p-cresyl sulfate. Biopharm Drug Dispos 2013;3 4:165–175. https://doi.org/10.1002/bdd.1834

9. Zubina IM. Physical and chemical properties of albumin and its functional usefulness in chronic glomerulonephritis: 14.00.46. SPb, 2001; 33–36. (In Russ)

10. Devine E, Krieter DH, Rüth M, Jankovski J, Lemke HD. Binding affinity and capacity for the uremic toxin indoxyl sulfate. Toxins 2014;6(2):416–429. https://doi.org/10.3390/toxins6020416

11. Jansen J, Jankowski J, Gajjala PR, Wetzels JFM, Masereeuw R.Disposition and clinical implications of protein-bound uremic toxins. Clin Sci Lond Engl 2017;131:1631–1647. https://doi.org/10.1042/CS20160191

12. Suchy-Dicey AM, Laha T, Hoofnagle A et al. Tubular secretion in CKD. J Am Soc Nephrol JASN 2016;27:2148–2155. https://doi.org/10.1681/ASN.2014121193

13. YAmpol'skij MA. Optimization of replacement therapy in patients with renal insufficiency: dis: 14.01.20. Rostov n/Donu, 2011: 68–70 (In Russ)

14. Koryachkin VA, Emanuel VL, Strashnov VI. Diagnostics in anesthesiology and intensive care. SpecLit, SPb., 2021; 416. (In Russ)

15. Emanuel' VL, Landa SB, Izmajlov M. Investigation of tammhorsfall protein oligomerous forms of a htalth persones and a urolithiasis patients by dynamic light scattering method. Aktual'nye voprosy biologicheskoj fiziki i himii 2016;1(2):189–194. (In Russ)

16. Onkometer bmt 923. URL: https://www.bmt-berlin.de/wp-content/uploads/923datasheet.pdf (Last access: 09. 11. 2022)

17. GOST R 53133.2-2008. Technologies laboratory clinical. Quality control of clinical laboratory research. Part 2. Rules for conducting intralaboratory quality control of quantitative methods of clinical laboratory research using control materials. National standard of the Russian Federation. Federal Agency for Technical Regulation. Ed. official. Standartinform, Moscow, 2009; 23. (In Russ.)

18. On the system of measures to improve the quality of clinical laboratory research in healthcare institutions of the Russian Federation. – Order of the Ministry of Health of the Russian Federation of February 7, 2000 N 45. Moscow, 2000:45. (In Russ.)

19. Al-Harthi S, Lachowicz JI, Nowakowski ME, Jaremko M, Jaremko Ł. Towards the functional high-resolution coordination chemistry of blood plasma human serum albumin. Journal of inorganic biochemistry 2019;198:110716. https://doi.org/10.1016/j.jinorgbio.2019.110716

20. Desirable biological variation database specifications. URL: https://www.westgard.com/biodatabase1.htm (Last access: 02. 11. 2022)

21. Weil MH, Henning RJ, Puri VK. Colloid oncotic pressure: clinical significance. Critical Care Medicine 1979;7(3):113–116

22. Technologies for improving the operating values of the analytical characteristics of analytical systems. URL: https://appliedmetrology.analytica.ru/lecture6/ (Last access: 02. 11. 2022)

23. Fraser CG. Reference change values. Clinical chemistry and laboratory medicine 2012;50(5):807–812. https://doi.org/10.1515/cclm.2011.733

24. Quinlan GJ, Martin GS, Evans TW. Albumin: Biochemical properties and therapeutic potential. Hepatology 2005;41(6):1211–1219. https://doi.org/10.1002/hep.20720

25. Lee E, Eom JE, Jeon KH, Kim TH, Kim E, Jhon GJ et al. Evaluation of albumin structural modifications through cobaltalbumin binding (CAB) assay. J Pharm Biomed Anal 2014;91:17– 23. https://doi.org/10.1016/j.jpba.2013.12.003

26. Fasano M, Curry S, Terreno E, Galliano M, Fanali G, Narciso P et al. The extraordinary ligand binding properties of human serum albumin. IUBMB Life 2005;57(12):787–796. https://doi.org/10.1080/15216540500404093

27. Kragh-Hansen U, Chuang VT, Otagiri M. Practical aspects of the ligand-binding and enzymatic properties of human serum albumin. Biol Pharm Bull 2002;25(6):695–704. https://doi.org/10.1248/bpb.25.695

28. Varshney A, Sen P, Ahmad E, Rehan M, Subbarao N, Khan RH. Ligand binding strategies of human serum albumin: How can the cargo be utilized? Chirality 2010;22(1):77–87. https://doi.org/10.1002/chir.20709

29. Gomella T, Cunningham M, Eyal F, Tuttle D. Neonatology: Management, Procedures, On-Call Problems, Diseases, and Drugs. 6 th ed. New York: McGraw-Hill Medical Publishers; 2009. Fig. 2: Methods for treatment of urolithiasis 35 Asian. J Pharm Clin Res 2017;10(10):32–35

30. Roche M, Rondeau P, Singh NR, Tarnus E, Bourdon E. The antioxidant properties of serum albumin. FEBS Lett 2008; 582(13):1783–1787. https://doi.org/10.1016/j.febslet.2008.04.057

31. Wei C, Nguyen SD, Kim MR, Sok DE. Rice albumin Nterminal (AspHis-His-Gln) prevents against copper ion-catalyzed oxidations. J Agric Food Chem 2007; 55(6):2149–2154. https://doi.org/10.1021/jf062387g

32. Halliwell B. Albumin – An important extracellular antioxidant? Biochem Pharmacol 1988;37(4):56971. https://doi.org/10.1016/0006-2952(88)90126-8

33. Hall J, Guyton A. Pocket Companion to Guyton and Hall Textbook of Medical Physiology. 11th ed. Philadelphia, PA: Elsevier Inc.; 2006

34. Skillman JJ. The role of albumin and oncotically active fluids in shock. Crit Care Med 1976;4(2):55–61. https://doi.org/10.1097/00003246-197603000-00003