Purification of the transforming growth factor-β (TGF-β) binding proteoglycan betaglycan Journal Article
| Authors: | Andres, J. L.; Rönnstrand, L.; Cheifetz, S.; Massagué, J. |
| Article Title: | Purification of the transforming growth factor-β (TGF-β) binding proteoglycan betaglycan |
| Abstract: | We report the purification of betaglycan, a low-abundance membrane proteoglycan with high affinity for transforming growth factor-β (TGF-β). Betaglycan solubilized from rat embryo membrane preparations was purified to near-homogeneity by sequential chromatography through DEAE-Trisacryl, wheat germ lectin-Sepharose, and TGF-β1-agarose. Purified betaglycan has properties similar to betaglycan affinity-labeled in intact cells: it binds TGF-β1 and TGF-β2 with K(D) ~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-β and associates with artificial liposomes, indicating that the core protein binds TGF-β and anchors to membranes independently of the GAG chains present on the native protein or of any ancillary protein. |
| Keywords: | unclassified drug; nonhuman; animal; animal tissue; transforming growth factor beta; embryo; membrane proteins; rat; cattle; rats; liposomes; binding, competitive; chromatography, affinity; purification; proteoglycans; binding kinetics; proteoglycan; chromatography, ion exchange; human; priority journal; article; support, non-u.s. gov't; support, u.s. gov't, p.h.s.; betaglycan |
| Journal Title: | Journal of Biological Chemistry |
| Volume: | 266 |
| Issue: | 34 |
| ISSN: | 0021-9258 |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Date Published: | 1991-12-05 |
| Start Page: | 23282 |
| End Page: | 23287 |
| Language: | English |
| PUBMED: | 1744125 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Article -- Export Date: 27 September 2019 -- Source: Scopus |
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