title: Zinc inhibits glycation induced structural, functional modifications in albumin and protects erythrocytes from glycated albumin toxicity.
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 μM) 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, β amyloid, native PAGE, ANS binding, fluorescence lifetime decay and CD analysis) and functional properties (antioxidant activity, hemolysis). Zinc at highest concentration (500 μM) 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.
authors.affiliation: Biochemical Sciences Division, Rajiv Gandhi Institute of IT and Biotechnology, Bharati Vidyapeeth University, Katraj, Pune 411046, India. Electronic address: rashmitupe@gmail.com.
authors.forename: Rashmi
authors.initials: R
authors.lastname: Tupe
authors.affiliation: Biochemical Sciences Division, Rajiv Gandhi Institute of IT and Biotechnology, Bharati Vidyapeeth University, Katraj, Pune 411046, India.
authors.forename: Amruta
authors.initials: A
authors.lastname: Kulkarni
authors.affiliation: Biochemical Sciences Division, Rajiv Gandhi Institute of IT and Biotechnology, Bharati Vidyapeeth University, Katraj, Pune 411046, India.
authors.forename: Krishna
authors.initials: K
authors.lastname: Adeshara
authors.affiliation: Biochemical Sciences Division, Rajiv Gandhi Institute of IT and Biotechnology, Bharati Vidyapeeth University, Katraj, Pune 411046, India.
authors.forename: Neena
authors.initials: N
authors.lastname: Sankhe
authors.affiliation: Biochemical Sciences Division, Rajiv Gandhi Institute of IT and Biotechnology, Bharati Vidyapeeth University, Katraj, Pune 411046, India.
authors.forename: Shamim
authors.initials: S
authors.lastname: Shaikh
authors.affiliation: Biochemical Sciences Division, CSIR-National Chemical Laboratory, Pune 411008, India.
authors.forename: Sayli
authors.initials: S
authors.lastname: Dalal
authors.affiliation: Biochemical Sciences Division, CSIR-National Chemical Laboratory, Pune 411008, India.
authors.forename: Siddharth
authors.initials: S
authors.lastname: Bhosale
authors.affiliation: Biochemical Sciences Division, CSIR-National Chemical Laboratory, Pune 411008, India.
authors.forename: Sushama
authors.initials: S
authors.lastname: Gaikwad
mesh_terms: D019610:Cytoprotection; D004353:Drug Evaluation, Preclinical; D004912:Erythrocytes / Q000187:drug effects / Q000502:physiology*; D006031:Glycosylation; D006801:Humans; D011499:Protein Processing, Post-Translational; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D015032:Zinc / Q000494:pharmacology*
chemical_list: D012710:Serum Albumin, Bovine; D015032:Zinc
keywords: Albumin; Erythrocytes; Glycation