Transforming growth factor-beta inhibition of epithelial cell proliferation linked to the expression of a 53-kDa membrane receptor

UMMS Affiliation

Department of Biochemistry

Publication Date


Document Type



Animals; Cell Adhesion; Cell Division; Cell Line; DNA Replication; Epithelial Cells; Epithelium; Fibronectins; *Mutation; Receptors, Cell Surface; Receptors, Transforming Growth Factor beta; Transforming Growth Factors


Life Sciences | Medicine and Health Sciences


Cells whose proliferation is blocked by transforming growth factor-beta (TGF-beta) express three distinct surface glycoproteins of 53, 73, and 300 kDa that bind TGF-beta with high affinity, but whose function is unknown. We have isolated two classes of chemically-induced Mv1Lu epithelial cell mutants resistant to growth inhibition by TGF-beta. Class R mutants have selectively lost expression of the 53-kDa (type I) TGF-beta-binding protein. They have also lost the ability to respond to TGF-beta with elevated fibronectin expression and cell flattening. Class S mutants bind normally but do not respond to TGF-beta. TGF-beta-resistant mutants retain a contact inhibited, nontransformed phenotype. The properties of S mutants suggest that they are defective in the TGF-beta signal transduction mechanism, while the results with R mutants identify the type I TGF-beta-binding protein as the receptor involved in mediating TGF-beta actions on cell adhesion and proliferation.


J Biol Chem. 1989 Feb 5;264(4):2272-8.

Journal/Book/Conference Title

The Journal of biological chemistry

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PubMed ID