Biochem Biophys Res Commun. 1988 May 16;152(3):1289-97.

Cloning, characterization, and expression of a human insulin-like growth factor binding protein.

Brewer MT, Stetler GL, Squires CH, Thompson RC, Busby WH, Clemmons DR.

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Synergen, Inc., Boulder, CO 80301.

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Biochem Biophys Res Commun 1988 Sep 30;155(3):1485.

Abstract

Insulin-like growth factors (IGFs) bind to specific proteins present in extracellular fluids. One of these binding proteins (IGF-BP) was purified from human amniotic fluid and was shown to potentiate the effects of IGF-I in vitro (10). In these studies, a polyclonal antibody to this protein was used to isolate a cDNA clone from a human decidua library. This clone encodes a polypeptide of 25,832 daltons that includes the sequences of 9 tryptic peptides that had been prepared from the purified IGF-BP. The protein has 15 cysteines that are clustered at the amino and carboxy ends of the molecule. The protein has an RGD sequence near its C-terminus, which may account for its ability to attach to cells and to potentiate the biological actions of IGF-I.

PMID:: 2454104; [PubMed - indexed for MEDLINE]

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GENBANK/M20841

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Cited by 13 PubMed Central articles

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