MONOCLONAL-ANTIBODIES TO INDIVIDUAL TYROSINE-PHOSPHORYLATED PROTEIN SUBSTRATES OF ONCOGENE-ENCODED TYROSINE KINASES
MONOCLONAL-ANTIBODIES TO INDIVIDUAL TYROSINE-PHOSPHORYLATED PROTEIN SUBSTRATES OF ONCOGENE-ENCODED TYROSINE KINASES
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DOI：
10.1073/pnas.87.9.3328
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发表时间：
1990-05-01
影响因子：
11.1
通讯作者：
PARSONS, JT
中科院分区：
文献类型：
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作者：
KANNER, SB;REYNOLDS, AB;PARSONS, JT
Cellular transformation by onocogenic retroviruses encoding protein tyrosine kinases coincides with the tyrosine-specific phosphorylation of multiple protein substrates. Previous studies have shown that tyrosine phosphorylation of a protein of 120 kDa, p120, correlated with src transformation in chicken embryo fibroblasts. Additionally, we previously identified two phosphotyrosine-containing cellular proteins, p130 and p110, that formed stable complexes with activated variants of pp60src, the src-encoded tyrosine kinase. To study transformation-relevant tyrosine kinase substrates, we have generated monoclonal antibodies to individual tyrosine phosphoproteins, including p130, P120, P110, and five additional phosphoproteins (p210, p125, p118, p85, and p185/p64). These antibodies detected several of the same tyrosine phosphoproteins in chickens embryo fibroblasts transformed by avian retroviruses Y73 and CT10, encoding the yes and crk oncogenes, respectively. Protein substrates in mouse, rat, hamster, and human cells overexpressing activated variants of chicken pp60src were also detected by several of the monoclonal antibodies.
