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

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Author

Summary, in English

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.

Publishing year

1991

Language

English

Pages

23282-23287

Publication/Series

Journal of Biological Chemistry

Volume

266

Issue

34

Document type

Journal article

Publisher

American Society for Biochemistry and Molecular Biology

Topic

  • Medicinal Chemistry

Keywords

  • Animals Binding
  • Affinity Chromatography
  • Ion Exchange Humans Liposomes/metabolism Membrane Proteins/*isolation & purification/metabolism Proteoglycans/*isolation & purification/metabolism Rats *Receptors
  • Competitive Cattle Chromatography
  • Transforming Growth Factor beta Transforming Growth Factor beta/*metabolism

Status

Published

ISBN/ISSN/Other

  • ISSN: 1083-351X