Selective inactivity of TGF-beta/decorin complexes.
Previous studies had shown that binding of TGF-beta to the small proteoglycan decorin results in its inactivation. Indeed, in osteosarcoma cells the addition of decorin prevented the TGF-beta 1-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-beta 1 was fully active in U937 monocytes with respect to the inhibition of cell proliferation. There was no inhibition of the TGF-beta-mediated stimulation of the retraction of fibroblast-populated collagen lattices. Thus, the formation of TGF-beta/decorin complexes leads to the neutralization of distinct effects only.
Institute of Physiological Chemistry and Pathobiochemistry, University of Münster, Germany.
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Hausser
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Gröning
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Hasilik
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Schönherr
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Kresse
D058578:Biglycan; D002455:Cell Division / Q000187:drug effects; D003094:Collagen; D058575:Decorin; D015536:Down-Regulation / Q000187:drug effects / Q000502:physiology; D016326:Extracellular Matrix Proteins; D006801:Humans; D009000:Monocytes / Q000166:cytology / Q000378:metabolism; D012516:Osteosarcoma / Q000378:metabolism; D011509:Proteoglycans / Q000096:biosynthesis / Q000378:metabolism* / Q000494:pharmacology; D016212:Transforming Growth Factor beta / Q000378:metabolism* / Q000494:pharmacology; D014407:Tumor Cells, Cultured
C546884:BGN protein, human; D058578:Biglycan; C546878:DCN protein, human; D058575:Decorin; D016326:Extracellular Matrix Proteins; D011509:Proteoglycans; D016212:Transforming Growth Factor beta; D003094:Collagen