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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
1990-1-8
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pubmed:abstractText |
The T cell recognition of globular protein antigens requires the processing and presentation of the antigen by Ia-expressing APCs. Processing is believed to involve the uptake of antigen into an acidic compartment where proteolysis occurs. The resulting peptides containing the T cell antigenic determinant are associated with Ia and presented at the cell surface to the specific T cells. The mechanisms by which antigenic peptides become associated with Ia is not known. We previously described a peptide binding protein of 72/74 x 10(3) Mr (PBP72/74) that plays a role in antigen presentation as shown by the ability of an antiserum raised in rabbits to affinity-purified PBP72/74 to block presentation of cytochrome c to a cytochrome c-specific T cell hybrid. Here we show that PBP72/74 is recognized by mAbs specific for members of the HSP70 family of proteins. In Western blots PBP72/74 is bound by mAb 7.10, specific for an evolutionarily conserved epitope of HSP proteins and by mAb N27, specific for both the constitutively expressed and inducible 72/73 x 10(3) Mr HSP70 proteins. In addition, PBP72/74 shares a second common feature of the HSP proteins, that of binding to ATP. Indeed, ATP causes the release of PBP72/74 from binding to a peptide fragment of cytochrome c (Pc 81-104) and PBP72/74 can be eluted from ATP columns by Pc 81-104. Finally, a portion of PBP72/74 is shown to be present on B cell surfaces by immunofluorescence staining. Thus, it appears that characteristics of the heat shock proteins are shared by a protein playing a role in antigen presentation, suggesting some commonality in function.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-2424770,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-2443855,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-2524273,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-2538825,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-2903217,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-2937542,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-2944601,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-2994052,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-3031645,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-307029,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-3084497,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-3087629,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-3106556,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-3121636,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-3132709,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-3171482,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-3194755,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-3227811,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-3258651,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-3282178,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-3282179,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-3309677,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-3352747,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-3490919,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-3500065,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-3511530,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-3529095,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-3536957,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-3757030,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-3876513,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-4092680,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-6193218,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2584924-6980413
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0022-1007
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
170
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1799-809
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
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pubmed:year |
1989
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pubmed:articleTitle |
A peptide binding protein having a role in antigen presentation is a member of the HSP70 heat shock family.
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pubmed:affiliation |
Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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