RGD Reference Report - Purification of the transforming growth factor-beta (TGF-beta) binding proteoglycan betaglycan. - Rat Genome Database

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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.
RGD ID: 2302518
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.


Gene Ontology Annotations    

Molecular Function

Objects Annotated

Genes (Rattus norvegicus)
Tgfbr3  (transforming growth factor beta receptor 3)

Additional Information