Selective inactivity of TGF-beta/decorin complexes

FEBS Lett. 1994 Oct 24;353(3):243-5. doi: 10.1016/0014-5793(94)01044-7.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biglycan
  • Cell Division / drug effects
  • Collagen
  • Decorin
  • Down-Regulation / drug effects
  • Down-Regulation / physiology
  • Extracellular Matrix Proteins
  • Humans
  • Monocytes / cytology
  • Monocytes / metabolism
  • Osteosarcoma / metabolism
  • Proteoglycans / biosynthesis
  • Proteoglycans / metabolism*
  • Proteoglycans / pharmacology
  • Transforming Growth Factor beta / metabolism*
  • Transforming Growth Factor beta / pharmacology
  • Tumor Cells, Cultured

Substances

  • BGN protein, human
  • Biglycan
  • DCN protein, human
  • Decorin
  • Extracellular Matrix Proteins
  • Proteoglycans
  • Transforming Growth Factor beta
  • Collagen