Coprecipitation of heat shock proteins with a cell surface glycoprotein.

Abstract

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.

• Authors: E N Hughes, J T August
• Journal: Proceedings of the National Academy of Sciences of the United States of America (Proc Natl Acad Sci U S A) Vol. 79 Issue 7 Pg. 2305-9 (Apr 1982) ISSN: 0027-8424 [Print] United States
• PMID: 6954542 (Publication Type: Comparative Study, Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Antibodies, Monoclonal
• Glycoproteins
• Heat-Shock Proteins
• Membrane Proteins
• Proteins

Topics

• Animals
• Antibodies, Monoclonal
• Cell Line
• Chromatography, Gel
• Electrophoresis
• Glycoproteins (immunology)
• HeLa Cells (metabolism)
• Heat-Shock Proteins
• Humans
• Kidney
• Membrane Proteins (immunology)
• Mice
• Mice, Inbred BALB C
• Molecular Weight
• Proteins (analysis, isolation & purification)