Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1995-2-9
pubmed:abstractText
Cellular proteins undergo proteolysis to yield peptide/MHC class I complexes for display on the APC surface. During this process it is not clear whether MHC molecules bind to and stabilize independently generated peptides, or whether they are involved in the peptide cleavage events. In this study, we analyzed the role of MHC molecules in Ag processing by characterizing the naturally processed peptide analogues of OVA (OVA257-264, SL8) in APC. DNA constructs encoding SL8 precursors were transfected into cells that varied in their MHC expression. By HPLC fractionation of cell extracts and with sensitive T cell assays for both the processed SL8 and its minimal Met-SL8 (MSL8) precursor, we determined that expression of Kb MHC molecule was essential for detecting processed peptides in living cells. Curiously, although the translated MSL8 nonapeptide precursor itself could bind Kb as well as the SL8 octapeptide, and MSL8 was available to MHC, only the SL8 peptide was found in Kb cell extracts. The presence of naturally processed SL8, but not MSL8 peptide in Kb-expressing cells suggests that the precise identity of endogenously processed peptides is also strongly influenced by the MHC molecules.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
154
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
585-98
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
The role of MHC class I molecules in the generation of endogenous peptide/MHC complexes.
pubmed:affiliation
Department of Molecular and Cell Biology, University of California, Berkeley 94720.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't