A major collagen-binding protein of chick embryo fibroblasts is a novel heat shock protein

J Cell Biol. 1986 Jul;103(1):223-9. doi: 10.1083/jcb.103.1.223.

Abstract

Heat shock proteins of chick embryo fibroblasts were analyzed on SDS polyacrylamide gradient gels and were found to include not only three previously well-characterized proteins of 25,000, 73,000, and 89,000 D, but also a 47,000-D protein. Two-dimensional gel electrophoresis revealed that this protein was unusually basic (pI = 9.0) and corresponded to a recently characterized, major gelatin- and collagen-binding protein. The induction of synthesis of this 47,000-D membrane glycoprotein after heat stress of fibroblasts was particularly apparent in preparations isolated by gelatin-affinity chromatography. Regulation of this 47,000-D phosphoprotein was more sensitive than that of three major heat shock proteins in that a substantial stimulation of synthesis occurred at even 42 degrees C, as well as at higher temperature. Phosphorylation of the 47,000-D protein was not altered after heat shock. These studies establish this phosphorylated membrane glycoprotein as a member of the heat shock/stress protein family, and they add collagen binding to the unexpectedly diverse spectrum of biochemical activities induced by exposure of cells to stress.

MeSH terms

  • Animals
  • Arsenic / pharmacology
  • Arsenites*
  • Carrier Proteins / metabolism*
  • Cell Membrane / metabolism
  • Cells, Cultured
  • Chick Embryo
  • Collagen / metabolism*
  • Gene Expression Regulation
  • Glycoproteins / metabolism
  • Heat-Shock Proteins / metabolism*
  • In Vitro Techniques
  • Membrane Proteins / metabolism
  • Molecular Weight
  • Phosphoproteins / metabolism*
  • Time Factors

Substances

  • Arsenites
  • Carrier Proteins
  • Glycoproteins
  • Heat-Shock Proteins
  • Membrane Proteins
  • Phosphoproteins
  • Collagen
  • arsenite
  • Arsenic