Coprecipitation of heat shock proteins with a cell surface glycoprotein.
Monoclonal antibodies recognizing a mouse cell surface glycoprotein of Mr 90,000 were found to coprecipitate the Mr 70,000 and 72,000 heat shock-induced proteins of NIH/3T3 cells. These two smaller proteins were among the most abundant components of heat-treated NIH/3T3 cells. The Mr 70,000 component was not detected in normal cells whereas there was a low rate of incorporation of [35S]methionine into the Mr 72,000 polypeptide in the absence of heat shock. Tryptic peptide mapping and two-dimensional gel electrophoresis indicated that the coprecipitated and heat shock-induced polypeptides were identical and that the Mr 70,000 and 72,000 components contained homologous peptides. Also, the heat shock proteins had extensive structural homology with a cytoskeleton-associated protein of HeLa cells. The results suggest that the Mr 90,000 cell surface glycoprotein and the Mr 70,000 and 72,000 heat shock-inducible proteins mediate an association between the plasma membrane and the cell cytoskeleton.
D000818:Animals; D000911:Antibodies, Monoclonal; D002460:Cell Line; D002850:Chromatography, Gel; D004586:Electrophoresis; D006023:Glycoproteins / Q000276:immunology; D006367:HeLa Cells / Q000378:metabolism; D006360:Heat-Shock Proteins; D006801:Humans; D007668:Kidney; D008565:Membrane Proteins / Q000276:immunology; D051379:Mice; D008807:Mice, Inbred BALB C; D008970:Molecular Weight; D011506:Proteins / Q000032:analysis / Q000302:isolation & purification*
D000911:Antibodies, Monoclonal; D006023:Glycoproteins; D006360:Heat-Shock Proteins; D008565:Membrane Proteins; D011506:Proteins