Linked Life Data

8116044

Source:http://linkedlifedata.com/resource/pubmed/id/8116044

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1994-3-29
pubmed:abstractText
There is evidence of two pathways of allorecognition, the direct pathway where T cells recognize intact allo-MHC molecules on the surface of target cells, and the indirect pathway where T cells recognize processed allo-MHC presented by self antigen-presenting cells. We used synthetic class II MHC allopeptides to study the cellular mechanisms of the indirect allorecognition pathway and its potential role in vascularized allograft rejection. LEW (RT1l) rat T cells--which are primed by immunization with a mixture of four 25 mer class II MHC allopeptides, representing the full length sequence of the beta chain of the hypervariable domain of the RT1.Du (WF), or by primary WF (RT1u) vascularized cardiac allografts--were capable of recognizing and proliferating to specific polymorphic class II MHC sequences when presented as peptides by responder APCs. T cells from naive LEW animals, WF animals immunized with syngeneic RT1.Du beta peptides, or LEW recipients of third-party BN (RT1n) vascularized cardiac allografts did not proliferate to the RT1.Du beta peptides, indicating the specificity of allopeptide recognition. In the strain combination used, immunogenicity of class II MHC allopeptides is determined by factors other than polymorphisms alone, since epitopic differences in 2 of the 4 RT1.Du beta allopeptides were not immunogenic. Responder T cells were CD4+, and were inhibited by monomorphic anticlass II monoclonal antibodies, and by specific anticlass II alloantibodies. These observations confirm the occurrence of self MHC-restricted recognition of processed allo-MHC in primary vascularized allograft rejection, and provide the rationale to develop novel and specific immunotherapies in organ transplantation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0041-1337
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
57
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
572-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Mechanisms of allo-recognition. Recognition by in vivo-primed T cells of specific major histocompatibility complex polymorphisms presented as peptides by responder antigen-presenting cells.
pubmed:affiliation
Department of Medicine, Brigham and Women's Hospital, Boston, Massachusetts 02115.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't