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

A new 55-kDa HDL/apolipoprotein binding protein was demonstrated in plasma membrane preparations of the human cell lines and primary cultured hepatocytes. Analysis of specific binding by ligand immunoblots of HDL, apoA-I, and apoA-II to a partially purified 55-kDa PA-I plasma membrane preparation demonstrated a K(d,HDL) = 50 nM (10 microg/ml), K(d,apoA-II) = 20 nM (0.4 microg/ml), and K(d, apoA-I) = 330 nM (10 microg/ml). Following preparative SDS-PAGE electrophoresis of a plasma membrane preparation isolated from human PA-I cells, fractions with apoA-II binding activity were collected, concentrated, and subjected to two-dimensional electrophoresis. Internal microprotein sequencing of the 55-kDa protein band revealed the binding protein as being heat shock protein 60 (hsp60). The hsp60 monoclonal antibody LK-1 blocked apoA-II binding to the 55-kDa HBP preparation. In summary, these results provide a potential mechanism to explain the known association between immunity developed against hsp60 and the development of atherosclerosis. Copyright 2000 Academic Press.