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Purification of the transforming growth factor-beta (TGF-beta) binding proteoglycan betaglycan.

Authors: Andres, JL  Ronnstrand, L  Cheifetz, S  Massague, J 
Citation: Andres JL, etal., J Biol Chem. 1991 Dec 5;266(34):23282-7.
Pubmed: (View Article at PubMed) PMID:1744125

We report the purification of betaglycan, a low-abundance membrane proteoglycan with high affinity for transforming growth factor-beta (TGF-beta). Betaglycan solubilized from rat embryo membrane preparations was purified to near-homogeneity by sequential chromatography through DEAE-Trisacryl, wheat germ lectin-Sepharose, and TGF-beta 1-agarose. Purified betaglycan has properties similar to betaglycan affinity-labeled in intact cells: it binds TGF-beta 1 and TGF-beta 2 with KD approximately 0.2 nM, contains heparan sulfate and chondroitin sulfate glycosaminoglycan (GAG) chains and N-linked glycans attached to a 110-kDa core protein, and can spontaneously associate with phosphatidylcholine liposomes. The betaglycan core obtained by enzymatic removal of the GAG chains has high affinity for TGF-beta and associates with artificial liposomes, indicating that the core protein binds TGF-beta and anchors to membranes independently of the GAG chains present on the native protein or of any ancillary protein.

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CRRD Object Information
CRRD ID: 2302518
Created: 2008-12-22
Species: All species
Last Modified: 2008-12-22
Status: ACTIVE



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