Characterization of a novel transformation-sensitive heat-shock protein (HSP47) that binds to collagen.
The synthesis of a major collagen-binding glycoprotein of molecular weight 47,000 was previously shown to be regulated by malignant transformation as well as by heat shock in chick embryo fibroblasts. The 47-kDa protein purified from chick embryos was characterized biochemically, and was found to exist as a monomer in native form. Its composition was enriched in basic amino acids and glycine, with fewer acidic residues and virtually no cysteine. N-terminal amino acid sequencing covering 36 residues revealed a single, novel sequence with an internal tandem repeat of Asp-Lys-Ala-Thr-Thr-Leu-Ala and Asp-Arg-Ser-Thr-Thr-Leu-Ala.
Nagata
K
K
Laboratory of Molecular Biology, National Cancer Institute, Bethesda, MD 20892.
Saga
S
S
Yamada
K M
KM
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002642:Chick Embryo; D003094:Collagen / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000378:metabolism*; D008970:Molecular Weight
D000596:Amino Acids; D006360:Heat-Shock Proteins; D003094:Collagen