Heat shock protein 60 is a high-affinity high-density lipoprotein binding protein

Citation
Av. Bocharov et al., Heat shock protein 60 is a high-affinity high-density lipoprotein binding protein, BIOC BIOP R, 277(1), 2000, pp. 228-235
Citations number
52
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
ISSN journal
0006291X → ACNP
Volume
277
Issue
1
Year of publication
2000
Pages
228 - 235
Database
ISI
SICI code
0006-291X(20001014)277:1<228:HSP6IA>2.0.ZU;2-A
Abstract
A new 55-kDa HDL/apolipoprotein binding protein was demonstrated in plasma membrane preparations of the human cell lines and primary cultured hepatocy tes, Analysis of specific binding by ligand immunoblots of HDL, apoA-I, and apoA-II to a partially purified S5-kDa PA-I plasma membrane preparation de monstrated a K-d,K-HDL = 50 nM (10 mug/ml), K-d,K-apoA-II = 20 nM (0.4 mug/ ml), and K-d,K-apoA-I = 330 nM (10 mug/ml). Following preparative SDS-PAGF electrophoresis of a plasma membrane preparation isolated from human PA-I c ells, fractions with apoA-II binding activity were collected, concentrated, and subjected to two-dimensional electrophoresis. Internal microprotein se quencing of the 55-kDa protein band revealed the binding protein as being h eat shock protein 60 (hsp60), The hsp60 monoclonal antibody LK-1 blocked ap oA-II binding to the 55-kDa HBP preparation. In summary, these results prov ide a potential mechanism to explain the known association between immunity developed against hsp60 and the development of atherosclerosis, (C) 2000 A cademic Press.