Proteins phosphorylated on tyrosine as markers of human tumor cell lines
- 15 April 1987
- journal article
- research article
- Published by Wiley in International Journal of Cancer
- Vol. 39 (4), 482-487
- https://doi.org/10.1002/ijc.2910390413
Abstract
Previous work has shown that proteins phosphorylated on tyrosine are selectively detectable by antibodies against phosphotyrosine (P‐Tyr) in cells transformed by retroviral class‐1 oncogene‐encoded kinases endowed with non‐regulated activity (Di Renzo et al., 1986). In this work P‐Tyr antibodies were used to investigate the existence of human tumors expressing abnormal levels of tyrosine phosphoproteins and tyrosine kinases. Among 18 cell lines examined, the antibodies identified a number of tumors with a detectable level of proteins phosphorylated on tyrosine. Among these were a major protein with an approximate Mr of 150,000 in a gastric carcinoma; 2 proteins, with Mr of 130,000 and 110,000 in a colon carcinoma; a major protein with Mr of 170,000, tyrosine phosphorylated in both a urinary bladder and an epidermoid carcinoma; a 100,000 Mr protein phosphorylated in lung and breast carcinomas. An 80,000 Mr tyrosine phosphorylated protein was found in a fibrosarcoma and in a rhabdomyosarcoma. Among the hemopoietic malignancies screened, in 2 Philadelphia‐positive chronic myelogenous leukemias P‐Tyr antibodies recognized the chimeric bcr‐abl 210,000 Mr protein and its substrates. Two tyrosine phosphorylated proteins, one of Mr 70,000 and one of Mr 60,000, were detected in a Burkitt lymphoma line. These phosphoproteins were not found in samples harvested from normal gastro‐intestinal or urinary bladder epithelium, nor in control fibroblasts and lymphocytes. Two of the above proteins have associated tyrosine kinase activity: the 170,000 Mr protein of bladder carcinoma cells was found to be a constitutively phosphorylated EGF receptor.This publication has 48 references indexed in Scilit:
- Immunological detection of proteins phosphorylated at tyrosine in cells stimulated by growth factors or transformed by retroviral-oncogene-coded tyrosine kinasesEuropean Journal of Biochemistry, 1986
- Protein phosphorylation at tyrosine residues INv-abl transformed mouse lymphocytes and fibroblastsInternational Journal of Cancer, 1986
- Expression of a translocated c-abl gene in hybrids of mouse fibroblasts and chronic myelogenous leukaemia cellsNature, 1986
- Transformation of cells by an inhibitor of phosphatases acting on phosphotyrosine in proteinsCell, 1985
- The c-fms proto-oncogene product is related to the receptor for the mononuclear phagocyte growth factor, CSF 1Cell, 1985
- Human squamous cell lung cancers express increased epidermal growth factor receptors.JCI Insight, 1984
- Structure and sequence of the cellular gene homologous to the RSV src gene and the mechanism for generating the transforming virusCell, 1983
- “Western Blotting”: Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein AAnalytical Biochemistry, 1981
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970