阿贝尔逊鼠白血病病毒诱导的转化涉及一种多肽生长因子的产生。

Transformation induced by Abelson murine leukemia virus involves production of a polypeptide growth factor.

作者信息

Twardzik D R, Todaro G J, Marquardt H, Reynolds F H, Stephenson J R

出版信息

Science. 1982 May 21;216(4548):894-7. doi: 10.1126/science.6177040.

Abstract

Rat embryo fibroblasts transformed by Abelson murine leukemia virus (MuLV) produce and release a transforming growth factor (TGF). Production of this factor is correlated with a tyrosine-specific protein kinase that is functionally active and is associated with the major Abelson MuLV gene product, P120. Transformation-defective mutants of Abelson MuLV do not transform cells, do not have their virus coded transforming gene product phosphorylated in tyrosine, and do not induce TGF production. Abelson MuLV-induced TGF morphologically transforms cells in culture, competes with 125I-labeled epidermal growth factor (EGF) for binding to cell receptors, and induces phosphorylation of tyrosine acceptor sites in the 160,000-dalton EGF membrane receptor. After purification to homogeneity, Abelson virus-induced TGF migrates as a single polypeptide with an apparent size of 7400 daltons as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.

摘要

由阿贝尔森鼠白血病病毒（MuLV）转化的大鼠胚胎成纤维细胞产生并释放一种转化生长因子（TGF）。该因子的产生与一种酪氨酸特异性蛋白激酶相关，这种激酶具有功能活性且与主要的阿贝尔森MuLV基因产物P120相关联。阿贝尔森MuLV的转化缺陷型突变体不能转化细胞，其病毒编码的转化基因产物酪氨酸不发生磷酸化，也不诱导TGF产生。阿贝尔森MuLV诱导的TGF在培养中使细胞发生形态转化，与125I标记的表皮生长因子（EGF）竞争结合细胞受体，并诱导160,000道尔顿EGF膜受体中酪氨酸受体位点的磷酸化。经纯化至同质后，阿贝尔森病毒诱导的TGF在十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳中作为一条表观大小为7400道尔顿的单一多肽迁移。