Abstract
TRANSFORMING growth factor-β (TGF-β) (reviewed in refs 1–3) is a family of molecules that are made up as disulphide-bonded dimers of at least three different types of homologous polypeptides4–8. The active molecules are cleaved from the C termini of precursors4,6–8. TGF-β1, like other forms of TGF-β, is synthesized and secreted in a latent high relative molecular mass form (L-TGF-β1) from which active TGF-β1 can be released by transient and probably unphysiological acidification9–12. The latent complex from human platelets contains one dimeric TGF-β1 molecule, which is noncovalently associated with a disulphide-bonded complex of one dimeric remnant of the precursor and a single molecule of the so-called TGF-β1 binding protein (TGF-01-BP)11,13. We report here that enzymatic removal in vitro of the carbohydrate structures in the remnant of the TGF-β1 precursor produces biologically active TGF-β1 from the latent complex, suggesting that carbohydrate structures are of importance in rendering TGF-β1 inactive in the complex in vivo.
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Miyazono, K., Heldin, CH. Role for carbohydrate structures inTGF-β1 latency. Nature 338, 158–160 (1989). https://doi.org/10.1038/338158a0
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DOI: https://doi.org/10.1038/338158a0
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