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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
1991-5-15
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pubmed:abstractText |
HLA-DR molecules are heterodimeric transmembrane glycoproteins that associate intracellularly with a polypeptide known as the invariant (I) chain. Shortly before expression of the HLA-DR alpha beta dimer on the cell surface, however, the I chain is removed from the intracellular alpha beta I complex by a mechanism thought to involve proteolysis. In this report, we show that treatment of purified alpha beta I with the cysteine proteinase cathepsin B results in the specific proteolysis of the HLA-DR-associated I chain in vitro. As a consequence of this, the I chain is removed and free alpha beta dimers are released from alpha beta I. Although alpha beta I fails to bind an immunogenic peptide, the released alpha beta dimers acquire the ability to bind the peptide after proteolysis of the I chain. These results suggest that the I chain inhibits immunogenic peptide binding to alpha beta I early during intracellular transport and demonstrate that proteolysis is likely to be the in vivo mechanism of I chain removal.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2014234-1967486,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2014234-2117634,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2014234-2156628,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2014234-2190094,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2014234-2234057,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2014234-2307844,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2014234-2388037,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2014234-2391366,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2014234-2402499,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2014234-2404209,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2014234-2478887,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2014234-2666863,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2014234-2925452,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2014234-2999796,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2014234-3020126,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2014234-3075592,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2014234-3282009,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2014234-3287381,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2014234-3489770,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2014234-3512715,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2014234-3930653,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2014234-6242349,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2014234-6811954,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2014234-6982931,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2014234-7043200,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2014234-7044372
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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 |
Apr
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
88
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3150-4
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2014234-Antigen-Presenting Cells,
pubmed-meshheading:2014234-Binding Sites,
pubmed-meshheading:2014234-Cathepsin B,
pubmed-meshheading:2014234-Chromatography, High Pressure Liquid,
pubmed-meshheading:2014234-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:2014234-HLA-DR Antigens,
pubmed-meshheading:2014234-Humans,
pubmed-meshheading:2014234-Hydrogen-Ion Concentration,
pubmed-meshheading:2014234-Peptides,
pubmed-meshheading:2014234-Structure-Activity Relationship
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pubmed:year |
1991
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pubmed:articleTitle |
Proteolysis of the class II-associated invariant chain generates a peptide binding site in intracellular HLA-DR molecules.
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pubmed:affiliation |
Department of Microbiology and Immunology, Duke University Medical Center, Durham, NC 27710.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.
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