Coprecipitation of heat shock proteins with a cell surface glycoprotein.

Abstract

Monoclonal antibodies recognizing a mouse cell surface glycoprotein of MW 90,000 were found to coprecipitate the MW 70,000 and 72,000 heat shock-induced proteins of NIH/3T3 [neoplastic embryo fibroblasts] cells. These 2 smaller proteins were among the most abundant components of heat-treated NIH/3T3 cells. The MW 70,000 component was not detected in normal cells whereas there was a low rate of incorporation of [35S]methionine into the MW 72,000 polypeptide in the absence of heat shock. Tryptic peptide mapping and 2-dimensional gel electrophoresis indicated that the coprecipitated and heat shock-induced polypeptides were identical and that the MW 70,000 and 72,000 components contained homologous peptides. Also, the heat shock proteins had extensive structural homology with a cytoskeleton-associated protein of [human cervical carcinoma] HeLa cells. The MW 90,000 cell surface glycoprotein and the MW 70,000 and 72,000 heat shock-inducible proteins may mediate an association between the plasma membrane and the cell cytoskeleton.