Publication Date:
1982-05-21
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Twardzik, D R -- Todaro, G J -- Marquardt, H -- Reynolds, F H Jr -- Stephenson, J R -- New York, N.Y. -- Science. 1982 May 21;216(4548):894-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6177040" target="_blank"〉PubMed〈/a〉
Keywords:
Abelson murine leukemia virus
;
Animals
;
*Cell Transformation, Neoplastic
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*Cell Transformation, Viral
;
Molecular Weight
;
Peptides/*metabolism
;
Phosphotyrosine
;
Rats
;
Receptor, Epidermal Growth Factor
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Receptors, Cell Surface/metabolism
;
Transforming Growth Factors
;
Tyrosine/analogs & derivatives/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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