Selective inactivity of TGF-β/decorin complexes
Previous studies had shown that binding of TGF-β to the small proteoglycan decorin results in its inactivation. Indeed, in osteosarcoma cells the addition of decorin prevented the TGF-β1-mediated up-regulation of biglycan synthesis. However, the down-regulation of proteoglycan-100 remained unaltered...
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Veröffentlicht in: | FEBS letters 1994-10, Vol.353 (3), p.243-245 |
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creator | Hausser, Heinz Gröning, Arndt Hasilik, Andrej Schönherr, Elke Kresse, Hans |
description | Previous studies had shown that binding of TGF-β to the small proteoglycan decorin results in its inactivation. Indeed, in osteosarcoma cells the addition of decorin prevented the TGF-β1-mediated up-regulation of biglycan synthesis. However, the down-regulation of proteoglycan-100 remained unaltered. Even in the presence of a 100,000-fold molar excess of decorin, TGF-β1 was fully active in U937 monocytes with respect to the inhibition of cell proliferation. There was no inhibition of the TGF-β-mediated stimulation of the retraction of fibroblast-populated collagen lattices. Thus, the formation of TGF-β/decorin complexes leads to the neutralization of distinct effects only. |
doi_str_mv | 10.1016/0014-5793(94)01044-7 |
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subjects | Biglycan Cell Division - drug effects Collagen Collagen-gel retraction Decorin Down-Regulation - drug effects Down-Regulation - physiology Extracellular Matrix Proteins Humans Monocytes - cytology Monocytes - metabolism Osteosarcoma - metabolism Proteoglycan-100 Proteoglycans - biosynthesis Proteoglycans - metabolism Proteoglycans - pharmacology TGF-β Transforming Growth Factor beta - metabolism Transforming Growth Factor beta - pharmacology Tumor Cells, Cultured |
title | Selective inactivity of TGF-β/decorin complexes |
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