Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases.

Kanner SB, Reynolds AB, Vines RR, Parsons JT
Proc Natl Acad Sci U S A. 1990 87 (9): 3328-32

PMID: 2110361 · PMCID: PMC53893 · DOI:10.1073/pnas.87.9.3328

Cellular transformation by oncogenic 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 chicken 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.

MeSH Terms (17)

Animals Antibodies, Monoclonal Antigen-Antibody Complex Cell Line Cells, Cultured Cell Transformation, Neoplastic Chick Embryo Enzyme-Linked Immunosorbent Assay Humans Immunoblotting Immunoglobulin G Immunoglobulin M Oncogene Protein pp60(v-src) Oncogenes Phosphoproteins Protein-Tyrosine Kinases Tyrosine

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