Document Detail

Early-glycation of apolipoprotein E: effect on its binding to LDL receptor, scavenger receptor A and heparan sulfates.
MedLine Citation:
PMID:  12069854     Owner:  NLM     Status:  MEDLINE    
Glycation is responsible for disruption of lipoprotein functions leading to the development of atherosclerosis in diabetes. The effects of apolipoprotein E (apoE) glycation were investigated with respect to its interaction with receptors. The interaction of apoE with the low density lipoprotein receptor (LDL-R) and scavenger receptor A (SR-A) was measured by competition experiments performed using, respectively, on a human fibroblast cell line 125I-LDL, and on a murine macrophage cell line (J774) 125I-acetylated LDL, and unlabeled apoE/phospholipid complexes. Glycated apoE binding to heparin and heparan sulfates (HS) was assessed by surface plasmon resonance (SPR) technology. Site-directed mutagenesis was then performed on Lys-75, the major glycation site of the protein. The prepared mutant protein proved to be useful as a tool to study the role of Lys-75 in apoE glycation. The findings showed that, although glycation has no effect on apoE binding either to the LDL-R or to SR-A, it impairs its binding to immobilized heparin and HS. The glycation of Lys-75 was found to be proceed rapidly and contributed significantly to total protein glycation. We propose that, in the case of diabetes, glycation may lead to the atherogenicity of apoE-containing lipoproteins disturbing their uptake via the HS proteoglycan pathway.
Isabelle Laffont; Vladimir V Shuvaev; Olivier Briand; Sophie Lestavel; Anne Barbier; Naoyuki Taniguchi; Jean-Charles Fruchart; Véronique Clavey; Gérard Siest
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1583     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  2002 Jun 
Date Detail:
Created Date:  2002-06-18     Completed Date:  2002-08-06     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  99-107     Citation Subset:  IM    
INSERM U525 (Equipe 4), Centre du Médicament, Université Henri Poincaré Nancy 1, 30, rue Lionnois, France.
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MeSH Terms
Apolipoproteins E / genetics,  metabolism*
Base Sequence
Cells, Cultured
DNA Primers
Glucose / metabolism*
Heparitin Sulfate / metabolism*
Membrane Proteins*
Mutagenesis, Site-Directed
Protein Binding
Receptors, Immunologic / metabolism*
Receptors, LDL / metabolism*
Receptors, Lipoprotein*
Receptors, Scavenger
Recombinant Proteins / metabolism
Scavenger Receptors, Class A
Scavenger Receptors, Class B
Reg. No./Substance:
0/Apolipoproteins E; 0/DNA Primers; 0/Membrane Proteins; 0/Receptors, Immunologic; 0/Receptors, LDL; 0/Receptors, Lipoprotein; 0/Receptors, Scavenger; 0/Recombinant Proteins; 0/Scarb1 protein, mouse; 0/Scavenger Receptors, Class A; 0/Scavenger Receptors, Class B; 50-99-7/Glucose; 9050-30-0/Heparitin Sulfate

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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