Маркеры, характеризующие гликемический статус и развитие нейрональных нарушений у пациентов с сахарным диабетом 1-го типа (1091720), страница 22
Текст из файла (страница 22)
– 2009. - № 5. – С. 53-5675. Лебедева А.В. Гехт А.Б. Гусев Е.И. Аутоантитела к фактору роста нервов и белкаммаркерам нейроглии у больных, перенесших ишемический инсульт при осложненном инеосложненном течении заболевания // Журнал неврологии и психиатрии. - 2009.- N 11.- С. 6-1210576. Камчатнов П. Р, Чугунов А.
В.,. Рулева Н. Ю, Дугин С. Ф., Бурячковская Л. И.,Умарова Х. Я. Аутоантитела к глиальному фибриллярному кислому белку у больных сразличными формами цереброваскулярной патологи // Журнал неврологии и психиатрии им.С.С. Корсакова. - 2008. № 11. - С. 58-6177. Теплицкая Л.Е.
Ястребова Н.Е., Ветров Ю.Д., Ванеева Н.П. Иммунологическаяаутоагрессия у пациентов с диабетической ретинопатией при диабете 1-го типа //Микробиология. – 2006. № 7. - P. 59-6278. Hoeldtke R.D., Bryner K.D., Hobbs G.R. et al. Antibodies to glutamic acid decarboxylaseand peripheral nerve function in type 1 diabetes // J Clin Endocrinol Metab. – 2000.
– V. 85. - P.3297–330879. Milicevic Z., Newlon P.G., Pittenger G.L., Stansberry K.B., Vinik A.I. Anti-gangliosideGM1 antibody and distal symmetric "diabetic polyneuropathy" with dominant motor features //Diabetologia. – 1997. – V. 40(11). - P. 1364-136580. Vinik A.I., Pittenger G.L., Stansberry K.B. Powers A: Phospholipid and glutamic aciddecarboxylase autoantibodies in diabetic neuropathy // Diabetes Care.
– 1995. V. 18. - P. 1225–123281. Смирнов В.В., Петряйкина Е.Е., Макушева В.Г., Полетаев А.Б.. Содержаниеестественных аутоантитле различной специфичности у детей, больных сахарным диабетом //Педиатрия. - 2006. - № 4. - C. 15-1882.АфонинА.А.,МорозоваН.В.,ГалкинаГ.А.,КомковаМ.В..Клинико-диагностическое значение нейротропных факторов при диабетической периферическойполинейропатии у детей и подростков // Педиатрия. – 2008. - Том 87(5). – C. 21-2583.HovsepyanM.R., HaasM.J., Boyajyan A.S., GuevorkyanA.A., MamikonyanA.A., Myers S.E., Mooradian A.D.
Astrocytic and neuronal biochemical markers in the sera of subjectswith diabetes mellitus // Neurosci Lett. – 2004. – V. 369(3). - P. 224-22784. Anguizola J., Matsuda R., Barnaby O.S., Hoy K.S., Wa C., Bolt E., Koke M., Hage D. S.Review: Glycation of human serum albumin // Clinica Chimica Acta. – 2013. – V. 425. – P. 64–7685. Fasano. M., Curry S., Terreno E., et. al. The extraordinary ligand binding properties ofhuman serum albumin // IUBMB Life. – 2005. V. 57(12). – P. 787-79686. Oettl K., Stauber R.E..
Physiological and pathological changes in the redox state ofhuman serum albumin critically influence its binding properties // British Journal of Pharmacology. –2007. – V. 151. – P. 580–59087. Gutteridge J. M. , Halliwell B. The measurement and mechanism of lipid peroxidation inbiological systems // Trends Biochem Sci. – 1990. – V. 15(4). – P. 129-13588. Szapacs M.E., Riggins J.N., Zimmerman L.J., Liebler D.C. Covalent adduction of human106serum albumin by 4-hydroxy-2-nonenal: kinetic analysis of competing alkylation reactions //Biochemistry. – 2006.
- V. 45(35). – P. 10521-1052889. Hayashi T., Era S., Kawai K., Imai H., Nakamura K., Onda E., Yoh M. Observation forredox state of human serum and aqueous humor albumin from patients with senile cataract //Pathophysiology. - 2000. - V. 6. P. 237–243.90. Jourd’Heuil D., Halle ´n K., Feelisch M., Grisham M.B.
Dynamic state of S-nitrosothiolsin human plasma and whole blood // Free Radic Biol Med. – 2000. – V. 28. – P. 409–41791. Stamler J.S. S-nitrosothiols in the blood. Roles, amounts, and methods of analysis // CircRes. – 2004. – V. 94. – P. 414–41792. Zhang H., Means G.E. S-nitrosation of serum albumin: spectrophotometric determinationof its nitrosation by simple S-nitrosothiols // Anal.
Biochem. – 1996. - V. 237. – P. 141–14493. Marley R., Patel R.P., Orie N., et. al. Formation of nanomolar concentrations of Snitrosoalbumin in human plasma by nitric oxide // Free Radic Biol Med. – 2001. – V. 31. – P. 688–69694. Ogasawara Y., Mukai Y., Togawa T., Suziki T., Tanabe S., Ishij K. Determination ofplasma thiol bound to albumin using affinity chromatography and high-performance liquidchromatography with fluorescence detection: ratio of cysteinyl albumin as a possible biomarker ofoxidative stress // J Chromatogr B.
– 2007. - V. 845. – P. 157–16395. Soejima A., Matsuzawa N., Hayashi T., Kimura R., Ootsuka T., Fukuoka K. et al. (2004).Alteration of redox state of human albumin before and after hemodialysis // Blood Purif. – 2004. – V.22. – P. 525–52996. Sogami M., Era S., Nagaoka Sm Kuwata K., Kida K., Shigami J., Miura K. et al. Highperformance liquid chromatographic studies on non-mercapt - mercapt conversion of human serumalbumin II // J Chromatogr. – 1985. – V. 332. - P. 19–2797.
Kadota K., Yui Y., Hattori R., Murohara Y., Kawai C. Decreased sulfhydryl groups ofserum albumin in coronary artery disease // Jpn Circ J. – 1991. – V. 55. – P. 937–94198. Suzuki E., Yasuda K., Takeda N., Sakata S., Era S., Kuwata K. et al. Increased oxidizedform of human serum albumin in patients with diabetes mellitus // Diabetes Res Clin Pract. - 1992. –V. 18. – P. 153–15899. Era S., Kuwata K., Imai H., Nakamura K., Hayashi T., Sogami M.
Age-related change inredox state of human serum albumin // Biochim Biophys Acta. – 1995. – V. 1247. – P. 12–16100. Imai H., Hayashi T., Negawa T., Nakamura K., Tomida M., Koda K. et al.Strenousexercise-induced change in redox state of human serum albumin during intensive kendo training // Jpn107J Physiol. - 2002. - V. 52. – P. 135–140101. Levine R. Carbonyl modified proteins in cellular regulation, aging, and disease // FreeRadic Biol Med. – 2002. - V. 32. - P. 790–796102.
Bourdon E., Loreau N., Blache D., Glucose and free radicals impair the antioxidantproperties of serum albumin // FASEB J. – 1999. V. 13 – P. 233-244103. Guedes S., Vitorino R., Domingues R., Amado F., Domingues P. Oxidation of bovineserum albumin: identification of oxidation products and structural modifications // Rapid CommunMass Spectrom. – 2009. – V. 23(15). – P. 2307-2315104.
Shaklai N., Garlick R.L., Bunn H.F. Nonenzymatic glycosylation of human serumalbumin alters its conformation and function // J Biol Chem. – 1984. – V. 259(6). - P. 3812-3817.105. Vlassopoulos A., Lean M.E., Combet E. Role of oxidative stress in physiologicalalbumin glycation: a neglected interaction // Free Radic Biol Med. – 2013. - V. 60. – P. 318-324.106. Roohk H.V., Zaidi AR. A review of glycated albumin as an intermediate glycation indexfor controlling diabetes // J Diabetes Sci Technol. – 2008. - V.
2. – P. 1114–1121107. Mendez D.L., Jensen R.A., McElroy L.A., Pena J.M., Esquerra R.M. The effect of nonenzymatic glycation on the unfolding of human serum albumin // Arch. Biochem. Biophys. – 2005. –V. 444. – P. 92–99108. Arif B, Jalaluddin M., Moinuddin A., Ahmad J., Arif Z., Alam K. Structural andimmuno-logical characterization of Amadori-rich human serum albumin: role in diabetes mellitus //Arch Biochem Biophys. – 2012. - V.
522. - P. 17–25109. Singh V.P., Bali A., Singh N., Jaggi A.S. Advanced glycation end products and diabeticcomplications // Korean J. Physiol. Pharmacol. – 2014. – V. 18(1). – P. 1-14110. Cohen M.P. Intervention strategies to prevent pathogenetic effects of glycated albumin.Arch Biochem Biophys // 2003. - V. 419(1). - P. 25-30111. Ahmad S., Moinuddin, Ali A. Immunological studies on glycated human IgG // LifeSci.2012. – V. 90.
– P. 980-987112.ScheijenJ.L., vandeWaarenburgM.P., StehouwerMeasurement of pentosidine in human plasma protein byC.D., SchalkwijkC.G.a single-column high-performance liquidchromatography method with fluorescence detection // J Chromatogr B AnalytTechnol Biomed Life Sci. – 2009. - V. 1;877(7). - P. 610-614.113. Fu M., Requena J., Jenkins A., et al. The advanced glycation end-product, NƐ(carboxymethyl)lysine, is a product ofboth lipid peroxidation and glycoxidation reactions // J B iolChem.
– 1996. - V. 271 . - P. 9982–9986114. Wa Ch., Cerny R.L., Clarke W.A., Hage D.S.. Characterization of glycation adducts on108human serum albumin by matrix assisted laser desorption/ionization time-of-flight mass spectrometry// Clin Chim Acta. – 2007. – V.385(1-2). - P. 48–60115. Barzilay J.I., Jablonski K.A., Fonseca V., et al. The impact of salsalate treatment onserum levels of advanced glycation end products in type 2 diabetes // Diabetes Care. – V.
37(4). - P.1083-1091116.HanssenN.M., EngelenL., FerreiraI.at.al.Plasma levels of advanced glycation endproducts Nε-(carboxymethyl)lysine, Nε-(carboxyethyl)lysine,andpentosidine are not independently associated with cardiovascular disease in individuals with orwithout type 2 diabetes: the Hoorn and CODAM studies // J Clin Endocrinol Metab. – 2013.
![](https://s.studizba.com/z.php?f=/templates/si/i/noavatar.png&w=100&h=100&t=1"){kind=avatar}
