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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5772
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pubmed:dateCreated |
1980-10-27
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pubmed:abstractText |
Malignant transformation by mammalian RNA sarcoma viruses has previously been shown to involve a reduction in receptor sites for a well characterized 6,000-molecular weight (MW) growth-promoting substance, designated epidermal growth factor (EGF). Although Abelson murine leukaemia virus (AbLV) resembles sarcoma viruses in its ability to transform embryo fibroblasts in cell culture, AbLV induces a rapid B-cell lymphoid leukaemia rather than fibrosarcomas in vivo. The major translational product of AbLV is a highly phosphorylated polyprotein of MW 120,000 which exhibits an associated tyrosine-specific protein kinase activity and probable transforming function. We show here that AbLV transformation resembles transformation by RNA sarcoma viruses with respect to the abolition of EGF-binding sites. EGF binding is restored to control levels following loss of polyprotein expression in morphological revertants of AbLV-transformed clones and remains uninfluenced in cell lines infected with transformation-defective (td) AbLV mutants encoding polyproteins deficient in protein kinase activity. These findings indicate that AbLV transformation involves a polyprotein-associated, tyrosine-specific protein kinase activity which mediates its effect through a mechanism resulting directly or indirectly in the abolition of EGF-binding sites.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0028-0836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
31
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pubmed:volume |
286
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
504-7
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:6250069-Abelson murine leukemia virus,
pubmed-meshheading:6250069-Animals,
pubmed-meshheading:6250069-Cell Line,
pubmed-meshheading:6250069-Cell Transformation, Neoplastic,
pubmed-meshheading:6250069-Cell Transformation, Viral,
pubmed-meshheading:6250069-Epidermal Growth Factor,
pubmed-meshheading:6250069-Leukemia Virus, Murine,
pubmed-meshheading:6250069-Mink,
pubmed-meshheading:6250069-Peptides,
pubmed-meshheading:6250069-Phosphoproteins,
pubmed-meshheading:6250069-Protein Kinases,
pubmed-meshheading:6250069-Rats,
pubmed-meshheading:6250069-Receptors, Cell Surface,
pubmed-meshheading:6250069-Tyrosine
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pubmed:year |
1980
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pubmed:articleTitle |
Abelson murine leukaemia virus transformation involves loss of epidermal growth factor-binding sites.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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