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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6368
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pubmed:dateCreated |
1992-5-6
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pubmed:abstractText |
The mutant human cell line T2 is defective in antigen presentation in the context of class I major histocompatibility complex (MHC) molecules, and also in that transfected T2 cells show poor surface expression of exogenous human class I (HLA) alleles. Both defects are thought to lie in the transport of antigenic peptides derived from cytosolic proteins into the endoplasmic reticulum (ER), as peptide-deficient class I molecules might be expected to be either unstable or retained in the ER. The products of several mouse class I (H-2) genes, and the endogenous gene HLA-A2 do, however, reach the surface of T2 cells at reasonable levels although they are non-functional. We report here that, as expected, poorly surface-expressed HLA molecules do not significantly bind endogenous peptides. Surprisingly, H-2 molecules expressed in T2 also lack associated peptides, arguing that 'empty' complexes of mouse class I glycoproteins with human beta 2-microglobulin are neither retained in the ER nor unstable. HLA-A2 molecules, however, do bind high levels of a limited set of endogenous peptides. We have sequenced three of these peptides and find that two, a 9-mer and an 11-mer, are derived from a putative signal sequence (of IP-30, an interferon-gamma-inducible protein), whereas a third, a 13-mer, is of unknown origin. The unusual length of two of the peptides argues that the 9-mers normally associated with HLA-A2 molecules may be generated before their transport from the cytosol rather than in a pre-Golgi compartment. To our knowledge, this is the first report of the isolation of a fragment of a eukaryotic signal peptide generated in vivo.
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pubmed:commentsCorrections | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0028-0836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
356
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
443-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1557127-Alleles,
pubmed-meshheading:1557127-Amino Acid Sequence,
pubmed-meshheading:1557127-Cell Line,
pubmed-meshheading:1557127-Cell Membrane,
pubmed-meshheading:1557127-Genes, MHC Class I,
pubmed-meshheading:1557127-HLA Antigens,
pubmed-meshheading:1557127-HLA-A Antigens,
pubmed-meshheading:1557127-HLA-A2 Antigen,
pubmed-meshheading:1557127-HLA-B Antigens,
pubmed-meshheading:1557127-Humans,
pubmed-meshheading:1557127-Major Histocompatibility Complex,
pubmed-meshheading:1557127-Molecular Sequence Data,
pubmed-meshheading:1557127-Mutation,
pubmed-meshheading:1557127-Transfection
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pubmed:year |
1992
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pubmed:articleTitle |
HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides.
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pubmed:affiliation |
Department of Microbiology and Immunology, Duke University Medical Center, Durham, North Carolina 27710.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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