Chemical Modification Induced by Glycation Increased Lysine Binding Site Activity of Human Serum Lipoprotein (a)

AUTHORS

Manigeh Kadkhodaei Elyaderani 1 , * , M Hadadi 2

1 Department of Biochemistry, School of Medicine, Jundishapoor University of Medical Sciences, [email protected], Iran

2 Department of Biochemistry, School of Medicine, Jundishapoor University of Medical Sciences, Iran

How to Cite: Kadkhodaei Elyaderani M, Hadadi M. Chemical Modification Induced by Glycation Increased Lysine Binding Site Activity of Human Serum Lipoprotein (a), Int J Endocrinol Metab. Online ahead of Print ; 5(4):195-240.

ARTICLE INFORMATION

International Journal of Endocrinology and Metabolism: 5 (4); 195-240
Article Type: Original Article
Received: December 13, 2005
Accepted: November 20, 2005
READ FULL TEXT

Abstract

Lipoprotein (a) is a major and independent risk factor for cardiovascular disease. The pathogenicity of Lp(a) as a risk factor may depend upon its Lysine binding site(LBS) activity. It is suggested that non enzymatic glycation of Lp(a) resulting from high plasma glucose level found in diabetic patients may be one of the factors contributing to the severity of this disease. The purpose of this research was to study the effect of glycation on Lysine binding site activity of lipoprotein(a).

Materials & Methods: Lp(a) was glycated by incubation of 100 ml serum in vitro with 0.25 to 350 mmol of glucose for 10 days at 37oC. Glycated Lp(a) was separated by using m–aminobronate affinity column chromatography and Lysine binding site properties of the glycated Lp(a) were compared with native Lp(a) by using lysine sepharose affinity chromatography.

Results: Glucose uptake by Lp(a) was linear as a function of concentration and time up to 7 days for all given concentrations. Glycation increased the negative charge of Lp(a) as monitored by electrophoresis and increased the affinity of Lp(a) for Lysine sepharose affinity column chromatography.

Conclusion: Chemical modification induced by glycation of lp(a) affected its lysine binding site activity and increased LP(a) lysine positive subspecies.Therefore it is suggested that nonenzymatic glycation of Lp(a) may contribute to premature atherogenesis of patients with diabetes mellitus by increasing its LBS activity. and diverting lipoprotein catabolism from non-athero genic to atherogenic pathways.

Full Text

Full text is available in PDF

© 0, International Journal of Endocrinology and Metabolism. This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial 4.0 International License (http://creativecommons.org/licenses/by-nc/4.0/) which permits copy and redistribute the material just in noncommercial usages, provided the original work is properly cited.
COMMENTS

LEAVE A COMMENT HERE: