TRANSFORMING GROWTH FACTOR-BETA INHIBITION OF EPITHELIAL-CELL PROLIFERATION LINKED TO THE EXPRESSION OF A 53-KDA MEMBRANE-RECEPTOR

Google Scholar
  • 5 February 1989
    • journal article
    • research article
    • Vol. 264  (4) , 2272-2278
Abstract
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.

This publication has 28 references indexed in Scilit: