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.
Article| July 01 1986
A major collagen-binding protein of chick embryo fibroblasts is a novel heat shock protein.
K M Yamada
Online Issn: 1540-8140
Print Issn: 0021-9525
J Cell Biol (1986) 103 (1): 223–229.
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K Nagata, S Saga, K M Yamada; A major collagen-binding protein of chick embryo fibroblasts is a novel heat shock protein.. J Cell Biol 1 July 1986; 103 (1): 223–229. doi: https://doi.org/10.1083/jcb.103.1.223
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