СИНТЕЗ И СЕКРЕЦИЯ ИНСУЛИНА: РОЛЬ КАТИОНОВ ЦИНКА

  • В. М. Шейбак УО «Гродненский государственный медицинский университет», Гродно
Ключевые слова: инсулин, цинк, синтез.

Аннотация

Представлены литературные данные о роли цинка в процессинге инсулина в панкреатических β-клетках островков Лангерганса. Показано, что в качестве кофактора Zn2+ не только принимает участие в синтезе и депонировании гранул инсулина в везикулах, но и, высвобождаясь во внеклеточное пространство, является сигнальной молекулой для α-клеток.

Литература

Becker, R. H. Clinical pharmacokinetics and pharmacodynamics of insulin glulisine / R. H. Becker, A. D. Frick // Clin Pharmacokinet. – 2008. – Vol.47. – P.7–20.

Bloom, C. R. Comparison of the allosteric properties of the Co(II) and Zn(II) substituted insulin hexamers / C. R. Bloom, N. Wu, A. Dunn // Biochem. – 1998. – Vol. 37. – P.10937– 10944.

Cadmium-113 nuclear magnetic resonance studies of bovine insulin: two-zinc insulin hexamer specifically binds calcium / J. L. Sudmeier [et al.] // Science – 2001. – Vol. 212. – P.560–562.

Calcium antagonists and islet function. I. Inhibition of insulin release by verapamil / G. Devis [et al.] // Diabetes – 1975. – Vol. 24. – P. 247–251.

β-Cell secretory products activate a-cell ATP-dependent potassium channels to inhibit glucagon release / I. Franklin [et al.] // Diabetes – 2005. – Vol. 54. – P. 1808–1815.

Chausmer, A. B. Zinc, insulin and diabetes / A.B. Chausmer // J. Am Coll Nutr. – 1998. – Vol. 17. – P. 109–115.

Chimienti, F. Zinc, pancreatic islet cell function and diabetes: new insights into an old story / F. Chimienti // Nutr Res Rev. – 2013. – Vol. 26, N 1. – P. 1-11.

Dodson, G. The role of assembly in insulin’s biosynthesis / G. Dodson, D. Steiner // Curr Opin Struct Biol – 2011. – Vol. 8. – P. 189–194.

Dunn, M. F. Zinc–ligand interactions modulate assembly and stability of the insulin hexamer – a review / M. F. Dunn // Biometals – 2005. - Vol.18. – P. 295–303.

Elemental composition of secretory granules in pancreatic islets of Langerhans / M. C. Foster [et al.] // Biophys J. – 1993. – Vol. 64. – P. 525–532.

Garg, V. K. Hypozincemia in diabetes mellitus / V. K. Garg, R. Gupta, R. K. Goyal // J Assoc Physicians India – 1994. – Vol. 42. – P. 720–721.

Gromada , J. α-Cells of theendocrine pancreas: 35 years of research but the enigmaremains/ J. Gromada, I. Franklin, C. B. Wollheim // Endocr Rev – 2007. – Vol. 28. – P. 84–116.

Henquin, J. C. Triggering and amplifying pathways of regulation of insulin secretion by glucose / J. C. Henquin // Diabetes – 2000. – Vol. 49. – P. 1751–1760.

Islet β-cell secretion determines glucagon release from neighbouring α-cells / H. Ishihara [et al.] // Nat Cell Biol. – 2003. – Vol. 5. – P. 330–335.

Kaarsholm, N. C. Comparison of solution structural flexibility and zinc binding domains for insulin, proinsulin and mini-proinsulin / N. C. Kaarsholm, H. C. Ko, M. F. Dunn // Biochem. – 1989. – Vol. 28. - P. 4427–4435.

Mechanisms of stabilization of the insulin hexamer through allosteric ligand interactions / W. Kadima [et al.] // J Biol Chem – 1992. – Vol. 267. – P. 8963–8970.

Mechanisms of stabilization of the insulin hexamer through allosteric ligand interactions / S. Rahuel-Clermont [et al.] // Biochem. – 1997. – Vol.36. – P.5837–5845.

Phenol stabilizes more helix in a new symmetrical zinc insulin hexamer / U. Derewenda [et al.] // Nature – 1989. – Vol. 338. – P. 594–596.

Planchart, A. Potentiation of insulin action by calciumand magnesium / A. Planchart // Diabetes. – 1969. – Vol..14. – P..430–431.

Ravier M.A. Glucose or insulin, but not zinc ions, inhibit glucagon secretion from mouse pancreatic α-cells / M. A. Ravier, G. A. Rutter // Diabetes. – 2005. – Vol. 54. – P. 1789–1797.

Regulation of glucagon secretion by zinc: lessons from the b cell-specific Znt8 knockout mouse model / A. B. Hardy [et al.] // Diabetes Obes Metab. – 2011. – Vol.13. – P. 112–117.

Robertson, R. P. A role for zinc in pancreatic islet β-cell cross-talk with the α-cell during hypoglycaemia / R. P. Robertson, H. Zhou, M. Slucca // Diabetes Obes Metab. – 2011. – V. 13. – P. 106–111.

Structure of rhombohedral 2 zinc insulin crystals / M. J. Adams [et al.] // Nature. – 1969. – Vol. 224. – P. 491–495.

Video image analysis of labile zinc in viable pancreatic islet cells using a specific fluorescent probe for zinc / P.D. Zalewski [et al.] //J Histochem Cytochem. – 1994. – Vol. 42. – P .877–884.

Wijesekara, N. Zinc, a regulator of islet function and glucose homeostasis/ N. Wijesekara, F. Chimienti, M. B. Wheeler // Diabetes Obes Metab. – 2009. – Vol. 11. – P. 202–214.

26X-ray crystallographic studies on hexameric insulins in the presence of helix-stabilizing agents, thiocyanate, methylparaben, and phenol / J. L. Whittingham [et al.] // Biochem. – 1995. – Vol. 34. – P. 15553–15563.

Zalewski, P. D. Correlation of apoptosis with change in intracellular labile Zn(II) using zinquin [(2-methyl-8-ptoluenesulphonamido-6-quinolyloxy)acetic acid], a new specific fluorescent probe for Zn(II) / P. D. Zalewski, I. J. Forbes, W. H. Betts // Biochem J. – 1993. – Vol. 296. – P. 403–408.

Zinc homeostasis in metabolic syndrome and diabetes / X. Miao [et al.] // Front. Med. – 2013. – Vol. 7. – P. 31-52.

Zinc in the physiology and pathology of the CNS / S. L. Sensi [et al.] // Nat Rev Neurosci. – 2009. – Vol. 10. – P. 780–791.




Загрузок PDF: 841
Опубликован
2015-05-21
Как цитировать
1.
Шейбак ВМ. СИНТЕЗ И СЕКРЕЦИЯ ИНСУЛИНА: РОЛЬ КАТИОНОВ ЦИНКА. Журнал ГрГМУ (Journal GrSMU) [Интернет]. 21 май 2015 г. [цитируется по 27 декабрь 2024 г.];(1(49):5-. доступно на: http://journal-grsmu.by/index.php/ojs/article/view/6