| SV40 T-antigen as a dual oncogene: structure and function of the plasma membrane-associated population. | |
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MedLine Citation:
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PMID: 2552888 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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SV40 T-antigen (T-ag) is localized in both the nucleus (nT-ag) and plasma membrane (pmT-ag) of cells and provides multiple functions necessary for cell transformation. The pmT-ag population is structurally very similar to the nT-ag. Transport to the cell surface is by an unknown mechanism that does not involve the secretory pathway. The disposition of T-ag in the membrane exposes both the amino and the carboxyl terminus on the exterior of the cell. Nuclear-transport-defective mutants of T-ag can transform established cells in culture, but not primary cells, suggesting that non-nuclear forms of T-ag may mediate some transformation-related process(es). A non-cytolytic protein extraction technique utilizing 1-butanol solubilized from SV40-transformed cells a multimeric complex composed of pmT-ag and at least five cellular proteins ranging in size from 35,000 (35K) to 60K M. Both amino- and carboxylterminal T-ag-specific monoclonal antibodies co-precipitated T-ag and the 35-60K Mr proteins, but antibodies against the internal portion of T-ag precipitated only uncomplexed T-ag. The growth state of the cells markedly influenced the expression of the T-ag-containing surface complexes; more complexes were recovered from actively dividing cells than from confluent cell cultures, and suspension cells yielded more complexes than cells on a substratum. The complex exhibited a highly dynamic association with the cell membrane, as demonstrated by pulse-chase analysis. The characteristics of growth-dependent expression and rapid turnover rate suggest a functional role for the membrane complex. The identities of the cellular proteins in the complex with pmT-ag are unknown, although one member (56K) is recognized by p53-specific monoclonal antibodies. |
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Authors:
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J S Butel; D L Jarvis; S A Maxwell |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S.; Review |
Journal Detail:
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Title: Annals of the New York Academy of Sciences Volume: 567 ISSN: 0077-8923 ISO Abbreviation: Ann. N. Y. Acad. Sci. Publication Date: 1989 |
Date Detail:
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Created Date: 1989-11-08 Completed Date: 1989-11-08 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 7506858 Medline TA: Ann N Y Acad Sci Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 104-21 Citation Subset: IM |
Affiliation:
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Division of Molecular Virology, Baylor College of Medicine, Houston, Texas 77030. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Antigens, Polyomavirus Transforming / genetics* Cell Membrane / immunology Cell Transformation, Neoplastic Humans Oncogenes* Simian virus 40 / genetics*, immunology |
| Grant Support | |
ID/Acronym/Agency:
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CA09197/CA/NCI NIH HHS; CA22555/CA/NCI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Antigens, Polyomavirus Transforming |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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