Zinc inhibits glycation induced structural, functional modifications in albumin and protects erythrocytes from glycated albumin toxicity

TitleZinc inhibits glycation induced structural, functional modifications in albumin and protects erythrocytes from glycated albumin toxicity
Publication TypeJournal Article
Year of Publication2015
AuthorsTupe, R, Kulkarni, A, Adeshara, K, Sankhe, N, Shaikh, S, Dalai, S, Bhosale, SH, Gaikwad, SM
JournalInternational Journal of Biological Macromolecules
Volume79
Pagination601-610
Date PublishedAUG
ISSN0141-8130
KeywordsAlbumin, Erythrocytes, Glycation
Abstract

The present work aims to investigate the concentration and time dependant effect of zinc on the in vitro non enzymatic modifications of albumin by diabetic levels of glucose. Further, preventive and curative effect of zinc was studied by adding zinc before and after initiation of glycation respectively. Glycation of albumin was done at different concentrations of zinc (125, 250 and 500 mu M) at different time intervals (21,28 and 35 days) with appropriate controls. The antiglycation potential of zinc was assessed by estimating different markers of albumin glycation (fructosamines, carbonyls, bound sugar, AGEs), structural modifications (free amino, thiol group, beta amyloid, native PAGE, ANS binding, fluorescence lifetime decay and CD analysis) and functional properties (antioxidant activity, hemolysis). Zinc at highest concentration (500 mu M) significantly reduced modifications of albumin which was comparable to aminoguanidine and also protected secondary and tertiary structure of albumin after 28 days of incubation. Zinc exhibited significant protective effect on erythrocytes by inhibiting hemolysis. Thus the present study indicate preventive mode of albumin glycation inhibition by zinc. (C) 2015 Elsevier B.V. All rights reserved.

DOI10.1016/j.ijbiomac.2015.05.028
Type of Journal (Indian or Foreign)

Foreign

Impact Factor (IF)3.138
Divison category: 
Biochemical Sciences