| pubmed-article:8920857 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8920857 | lifeskim:mentions | umls-concept:C1332717 | lld:lifeskim |
| pubmed-article:8920857 | lifeskim:mentions | umls-concept:C1706438 | lld:lifeskim |
| pubmed-article:8920857 | lifeskim:mentions | umls-concept:C0085358 | lld:lifeskim |
| pubmed-article:8920857 | lifeskim:mentions | umls-concept:C0024518 | lld:lifeskim |
| pubmed-article:8920857 | lifeskim:mentions | umls-concept:C0001128 | lld:lifeskim |
| pubmed-article:8920857 | lifeskim:mentions | umls-concept:C0024337 | lld:lifeskim |
| pubmed-article:8920857 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:8920857 | lifeskim:mentions | umls-concept:C1413244 | lld:lifeskim |
| pubmed-article:8920857 | lifeskim:mentions | umls-concept:C2698600 | lld:lifeskim |
| pubmed-article:8920857 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:8920857 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:8920857 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
| pubmed-article:8920857 | lifeskim:mentions | umls-concept:C0456387 | lld:lifeskim |
| pubmed-article:8920857 | lifeskim:mentions | umls-concept:C1510996 | lld:lifeskim |
| pubmed-article:8920857 | lifeskim:mentions | umls-concept:C0205251 | lld:lifeskim |
| pubmed-article:8920857 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:8920857 | lifeskim:mentions | umls-concept:C1706204 | lld:lifeskim |
| pubmed-article:8920857 | lifeskim:mentions | umls-concept:C1555721 | lld:lifeskim |
| pubmed-article:8920857 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:8920857 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:8920857 | pubmed:dateCreated | 1996-12-30 | lld:pubmed |
| pubmed-article:8920857 | pubmed:abstractText | Cytotoxic T lymphocyte (CTL) activation requires specific T cell receptor (TCR)-class I major histocompatibility complex (MHC) antigen complex interactions as well as the participation of coreceptor or accessory molecules on the surface of CTL. CD8 can serve as a coreceptor in that it binds to the same MHC class I molecules as the TCR to facilitate efficient TCR signaling. In addition, CD8 can be "activated" by TCR stimulation to bind to class I molecules with high avidity, including class I not recognized by the TCR as antigenic complexes (non-antigen [Ag] class I), to augment CTL responses and thus serve an accessory molecule function. A Glu/Asp227-->Lys substitution in the class I alpha 3 domain acidic loop abrogates lysis of target cells expressing these mutant molecules by alloreactive CD8-dependent CTL. Lack of response is attributed to the destruction of the CD8 binding site in the alpha 3 domain which is likely to disrupt CD8 coreceptor function. The relative importance of the class I alpha 3 domain acidic loop Glu227 in coreceptor as opposed to accessory functions of CD8 is unclear. To address this issue, we examined CTL adhesion and degranulation in response to immobilized class I-peptide complexes formed in vitro from antigenic peptides and purified class I molecules containing wild-type or Glu227-->Lys substituted alpha 3 domains. The alpha 3 domain mutant class I-peptide complexes were bound by CTL and triggered degranulation, however to much lower levels than wild-type class I-peptide complexes. In further experiments, it is directly demonstrated that the alpha 3 domain mutant class I molecules, which lack the Glu227 CD8 binding site, still serve as TCR-activated, avidity-enhanced CD8 accessory ligands. However, mutant class I peptide Ag complexes failed to effectively serve as CD8 coreceptor ligands to initiate TCR-dependent signals required to induce avidity-enhanced CD8 binding to coimmobilized non-Ag class I molecules. Thus the Glu227-->Lys mutation effectively distinguishes CD8 coreceptor and avidity-enhanced CD8 accessory functions. | lld:pubmed |
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| pubmed-article:8920857 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8920857 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8920857 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8920857 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8920857 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8920857 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:8920857 | pubmed:issn | 0022-1007 | lld:pubmed |
| pubmed-article:8920857 | pubmed:author | pubmed-author:ShenLL | lld:pubmed |
| pubmed-article:8920857 | pubmed:author | pubmed-author:PotterT ATA | lld:pubmed |
| pubmed-article:8920857 | pubmed:author | pubmed-author:KaneK PKP | lld:pubmed |
| pubmed-article:8920857 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8920857 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:8920857 | pubmed:volume | 184 | lld:pubmed |
| pubmed-article:8920857 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8920857 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8920857 | pubmed:pagination | 1671-83 | lld:pubmed |
| pubmed-article:8920857 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:8920857 | pubmed:meshHeading | pubmed-meshheading:8920857-... | lld:pubmed |
| pubmed-article:8920857 | pubmed:meshHeading | pubmed-meshheading:8920857-... | lld:pubmed |
