Transforming growth factor-beta inhibition of epithelial cell proliferation linked to the expression of a 53-kDa membrane receptor.
Transforming growth factor-beta inhibition of epithelial cell proliferation linked to the expression of a 53-kDa membrane receptor.
复制标题
DOI：
--
复制
发表时间：
1989-02
期刊：
影响因子：
--
通讯作者：
Frederick T. Boyd;J. Massagué
中科院分区：
文献类型：
--
作者：
Frederick T. Boyd;J. Massagué
增殖被转化生长因子-β (TGF-β) 阻断的细胞表达三种不同的表面糖蛋白，分别为 53、73 和 300 kDa，它们以高亲和力结合 TGF-β，但其功能尚不清楚。我们分离出两类化学诱导的 Mv1Lu 上皮细胞突变体，它们对 TGF-β 的生长抑制具有抵抗力。 R 类突变体选择性丧失 53-kDa（I 型）TGF-β 结合蛋白的表达。它们还失去了响应 TGF-β 的能力，导致纤连蛋白表达升高和细胞扁平化。 S 类突变体正常结合，但不响应 TGF-β。 TGF-β 抗性突变体保留接触抑制、非转化表型。 S突变体的特性表明它们在TGF-β信号转导机制中存在缺陷，而R突变体的结果表明I型TGF-β结合蛋白是参与介导TGF-β对细胞粘附和增殖作用的受体。
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.