A major collagen-binding protein of chick embryo fibroblasts is a novel heat shock protein.
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| 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.
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| Authors | K Nagata, S Saga, K M Yamada |
| Journal | The Journal of cell biology (J Cell Biol) Vol. 103 Issue 1 Pg. 223-9 (Jul 1986) ISSN: 0021-9525 [Print] United States |
| PMID | 3722264 (Publication Type: Journal Article) |
| Chemical References |
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