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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
15
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pubmed:dateCreated |
2003-4-7
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pubmed:abstractText |
A protein of unknown physiological function, called amyloid precursor-like protein 2 (APLP2), forms an association with the murine class I molecule K(d) that is up-regulated by the presence of the adenoviral protein E3/19K. We have extended these findings to show that APLP2 and E3/19K associate preferentially with folded K(d) and not with the open form. APLP2 was detectable at the cell surface, but its surface expression was not up-regulated by the concurrent expression of K(d). Experimental down-regulation of APLP2 expression caused a consistent increase in the surface expression of K(d), indicating that APLP2 normally reduces K(d) surface expression. These data suggest a role for APLP2 in controlling the maturation of major histocompatibility complex class I molecules.
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pubmed:grant |
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/APLP1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/APLP2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Adenovirus E3 Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid beta-Protein Precursor,
http://linkedlifedata.com/resource/pubmed/chemical/Aplp1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Aplp2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/H-2 Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/H-2K(K) antigen,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12618-23
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pubmed:dateRevised |
2011-8-4
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pubmed:meshHeading |
pubmed-meshheading:12506118-Adenovirus E3 Proteins,
pubmed-meshheading:12506118-Amino Acid Substitution,
pubmed-meshheading:12506118-Amyloid beta-Protein Precursor,
pubmed-meshheading:12506118-Animals,
pubmed-meshheading:12506118-Base Sequence,
pubmed-meshheading:12506118-Binding Sites,
pubmed-meshheading:12506118-DNA Primers,
pubmed-meshheading:12506118-Gene Expression Regulation,
pubmed-meshheading:12506118-H-2 Antigens,
pubmed-meshheading:12506118-HeLa Cells,
pubmed-meshheading:12506118-Humans,
pubmed-meshheading:12506118-Kinetics,
pubmed-meshheading:12506118-L Cells (Cell Line),
pubmed-meshheading:12506118-Mice,
pubmed-meshheading:12506118-Mutagenesis, Site-Directed,
pubmed-meshheading:12506118-Nerve Tissue Proteins,
pubmed-meshheading:12506118-Protein Binding,
pubmed-meshheading:12506118-Protein Conformation,
pubmed-meshheading:12506118-Protein Folding,
pubmed-meshheading:12506118-RNA, Small Interfering,
pubmed-meshheading:12506118-Reverse Transcriptase Polymerase Chain Reaction
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pubmed:year |
2003
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pubmed:articleTitle |
The amyloid precursor-like protein 2 and the adenoviral E3/19K protein both bind to a conformational site on H-2Kd and regulate H-2Kd expression.
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pubmed:affiliation |
Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska 68198, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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