PMID: 9175590May 2, 1997Paper

Enhanced binding of advanced glycation endproducts (AGE) by the ApoE4 isoform links the mechanism of plaque deposition in Alzheimer's disease

Neuroscience Letters
Y M Li, D W Dickson

Abstract

Alzheimer's disease (AD) brains contain high levels of advanced glycation endproducts (AGEs). Double immunostaining using anti-AGE and anti-apolipoprotein E (apoE) antibodies demonstrated that AGEs co-localized to a very high degree with apoE. We examined the binding of apoE to in vitro-prepared AGE-bovine serum albumin (AGE-BSA), using Western ligand blot analysis. ApoE exhibited AGE-specific binding activity in the presence of excess native BSA, with the dimeric form of apoE binding better than the monomeric form. Other apolipoproteins including apo A1, B, CI and CII, and serum beta2-microglobulin, did not bind AGE-BSA. ApoE4 exhibited a 3-fold greater AGE-binding activity than the apoE3 isoform. These results suggest that apoE may participate in aggregate formation in the AD brain by binding to AGE-modified plaque components. It is possible that enhanced binding of apoE4 might have pathogenic consequences in vivo.

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Citations

Jul 16, 1999·Mechanisms of Ageing and Development·X SongY M Li
Jun 24, 2000·European Journal of Biochemistry·C LoskeG Münch
May 6, 1999·Diabetic Medicine : a Journal of the British Diabetic Association·R Stewart, D Liolitsa
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Sep 28, 2010·Progress in Retinal and Eye Research·Chung-Jung Chiu, Allen Taylor

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