Open AccessTransforming growth factor beta increases mRNA for matrix proteins both in the presence and in the absence of changes in mRNA stability.
Author(s) -
Risto Penttinen,
Satoko Kobayashi,
Paul Börnstein
Publication year - 1988
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.85.4.1105
Subject(s) - fibronectin , cycloheximide , messenger rna , extracellular matrix , biology , northern blot , transforming growth factor beta , beta (programming language) , growth factor , transforming growth factor , microbiology and biotechnology , tgf alpha , endocrinology , medicine , protein biosynthesis , biochemistry , receptor , gene , computer science , programming language
Transforming growth factor-beta (TGF-beta) has been shown to stimulate synthesis of extracellular matrix proteins, both in animals and in cell culture. We found that mRNAs for alpha 1(I) collagen, fibronectin, and thrombospondin were markedly increased in TGF-beta-treated 3T3 (mouse) cells. For collagen and fibronectin this increase was 10-to 20-fold, as measured by quantitative blot hybridization analysis. A maximal value was reached at 16-24 hr, with a subsequent gradual decline. Concomitant treatment with cycloheximide prevented the stimulation observed with TGF-beta. Under conditions of confluent growth a clear increase in alpha 1(I) collagen mRNA stability was observed, whereas in subconfluent cells no change in mRNA half-life was found, despite an equally large increase in mRNA levels. We suggest that the mode of action of TGF-beta varies with the target cell and depends on the interplay of a number of complex cellular factors.