Linked Life Data

7523514

Source:http://linkedlifedata.com/resource/pubmed/id/7523514

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1994-11-23
pubmed:abstractText
CD8+ T cells recognize antigenic peptides in the context of MHC class I molecules that encompass two distinct polypeptide chains, the MHC-encoded alpha-chain and the non-MHC-encoded beta 2-microglobulin (beta 2-m). The beta 2-m is considered essential for the stability and function of the MHC class I peptide complex and, hence, for peptide presentation to CD8+ T cells. In this study, we describe peptide presentation by macrophages from beta 2-m-deficient mice to a CD8+ CTL clone tht cross-recognizes an H-2Db-restricted peptide of the mycobacterial heat shock protein 60 (hsp60) and a self-peptide presented by IFN-gamma-stressed macrophages. Specific lysis of stressed or hsp60 peptide-pulsed beta 2-m-/- macrophages was inhibited by the nucleoprotein peptide with high affinity to H-2Db. Brefeldin A, a known inhibitor of MHC class I processing, interfered with lysis of IFN-gamma-stressed, but not of hsp60 peptide-pulsed, beta 2-m-/- macrophages. The hsp60 peptide failed to stimulate surface expression of H-2Db in beta 2-m-/- macrophages, and slightly increased MHC class I expression in the transporter mutant cell line RMA-S, as detected by cytofluorometry. We concLude that presentation of endogenously processed cytosolic epitopes and exogenously added foreign peptides by the MHC class I alpha-chain can occur independent from beta 2-m. Presumably, H-2Db peptides, but not H-2Kb peptides, have the capacity to induce and/or stabilize surface expression of a small number of MHC class I alpha-chains, and this low density is sufficient for recognition by CD8+ CTL, although it need not be detected by serologic means.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
153
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4070-80
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:7523514-Amino Acid Sequence, pubmed-meshheading:7523514-Animals, pubmed-meshheading:7523514-Antigen Presentation, pubmed-meshheading:7523514-Autoantigens, pubmed-meshheading:7523514-Cells, Cultured, pubmed-meshheading:7523514-Chaperonin 60, pubmed-meshheading:7523514-Cross Reactions, pubmed-meshheading:7523514-Cytotoxicity Tests, Immunologic, pubmed-meshheading:7523514-Epitopes, pubmed-meshheading:7523514-Female, pubmed-meshheading:7523514-H-2 Antigens, pubmed-meshheading:7523514-Macrophages, pubmed-meshheading:7523514-Male, pubmed-meshheading:7523514-Mice, pubmed-meshheading:7523514-Mice, Inbred C57BL, pubmed-meshheading:7523514-Mice, Mutant Strains, pubmed-meshheading:7523514-Molecular Sequence Data, pubmed-meshheading:7523514-Peptides, pubmed-meshheading:7523514-T-Lymphocytes, Cytotoxic, pubmed-meshheading:7523514-Up-Regulation, pubmed-meshheading:7523514-beta 2-Microglobulin
pubmed:year
1994
pubmed:articleTitle
Beta 2-microglobulin independent presentation of exogenously added foreign peptide and endogenous self-epitope by MHC class I alpha-chain to a cross-reactive CD8+ CTL clone.
pubmed:affiliation
Department of Immunology, University of Ulm, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't