Transforming growth factor-beta inhibition of epithelial cell proliferation linked to the expression of a 53-kDa membrane receptor.
作者： F T Boyd , J Massagué
DOI: 10.1016/S0021-9258(18)94172-4
关键词: Cell adhesion 、 Cell biology 、 Cell growth 、 Fibronectin 、 Transforming growth factor beta 、 Cell culture 、 Transforming growth factor 、 Signal transduction 、 Biology 、 Cell surface receptor
摘要: 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 function unknown. We have isolated two classes chemically-induced Mv1Lu epithelial cell mutants resistant to inhibition TGF-beta. Class R selectively lost expression the 53-kDa (type I) TGF-beta-binding protein. They also ability respond elevated fibronectin flattening. S normally do not TGF-beta-resistant retain a contact inhibited, nontransformed phenotype. The properties suggest they are defective in signal transduction mechanism, while results identify type I protein as receptor involved mediating actions on adhesion proliferation.
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