Low HLA-C expression at cell surfaces correlates with increased turnover of heavy chain mRNA.
HLA-A
DOI:
10.1084/jem.181.6.2085
Publication Date:
2004-06-24T07:56:10Z
AUTHORS (5)
ABSTRACT
In comparison with HLA-A and -B, the protein products of HLA-C locus are poorly characterized, in part because their low level expression at cell surface. Here, we examine how protein-protein interactions during assembly regulation mRNA affect surface HLA-C. We find that intrinsic properties heavy chain proteins do not correlate expression: chains associate dissociate beta 2-microglobulin (beta 2m) rates comparable to those found for increased competition 2m does alter From studies chimeric genes spliced from HLA-B7 -Cw3 genes, containing B7 peptide-binding groove can have expression, suggesting inefficiency binding peptides is cause The levels HLA-A, or -C cells transfected cDNA be similar, implicating noncoding regions expression. expressed lower than HLA-B this difference results faster degradation message. Experiments examining B7/Cw3 B7/Cw6 suggest a region determining between 3' end exon 3 site untranslated region, approximately 600 bases downstream translation stop codon.
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