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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1991-1-29
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pubmed:abstractText |
Immunological evidence was provided that in subclone 7 cell line, which is derived from SV40 transformed cells, 115-kDa super T antigen, a transformation-competent, elongated form of large T antigen was physically complexed with hsp70 proteins. This conclusion was first based on the coimmunoprecipitation from unstressed or heat shocked subclone 7 cells of both super T antigen and hsp70 proteins. This was observed with any one of a set of anti-T monoclonal antibodies reacting to determinants located either in the C-terminal region or in the N terminal region. Reciprocally coimmunoprecipitation of both hsp70 and super T was also observed in the anti-hsp70 peptide serum-immunoprecipitate. The formation of complexes between hsp70 proteins and super T antigen in subclone 7 cells was also confirmed by Western blot experiments. Moreover, when expressed in cell lines originating from human (Hela cells) or monkey (CV1P cells) species following transfection with the relevant plasmid, super T antigen again displayed the ability to associate with hsp70 proteins. Considering that super T antigen was obtained in laboratory experiments as a stable evolutionary variant of SV40 large T antigen, it is suggested that the marked ability of super T antigen to associate with heat shock protein could be selectively advantageous under certain conditions.
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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/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Polyomavirus Transforming,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0042-6822
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
180
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
285-93
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1701947-Animals,
pubmed-meshheading:1701947-Antibodies, Monoclonal,
pubmed-meshheading:1701947-Antibodies, Viral,
pubmed-meshheading:1701947-Antigens, Polyomavirus Transforming,
pubmed-meshheading:1701947-Blotting, Western,
pubmed-meshheading:1701947-Cell Line, Transformed,
pubmed-meshheading:1701947-Cells, Cultured,
pubmed-meshheading:1701947-Centrifugation, Density Gradient,
pubmed-meshheading:1701947-Cercopithecus aethiops,
pubmed-meshheading:1701947-Epitopes,
pubmed-meshheading:1701947-HeLa Cells,
pubmed-meshheading:1701947-Heat-Shock Proteins,
pubmed-meshheading:1701947-Humans,
pubmed-meshheading:1701947-Plasmids,
pubmed-meshheading:1701947-Rats,
pubmed-meshheading:1701947-Simian virus 40,
pubmed-meshheading:1701947-Transfection
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pubmed:year |
1991
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pubmed:articleTitle |
Immunological evidence for the association between simian virus 40 115-kDa super T antigen and hsp70 proteins in rat, monkey, and human cells.
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pubmed:affiliation |
Laboratoire d'Oncologie Moléculaire-I.R.S.C., C.N.R.S., Villejuif, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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