pubmed-article:7537557 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7537557 | lifeskim:mentions | umls-concept:C0242629 | lld:lifeskim |
pubmed-article:7537557 | lifeskim:mentions | umls-concept:C0018133 | lld:lifeskim |
pubmed-article:7537557 | lifeskim:mentions | umls-concept:C1332714 | lld:lifeskim |
pubmed-article:7537557 | lifeskim:mentions | umls-concept:C1420364 | lld:lifeskim |
pubmed-article:7537557 | lifeskim:mentions | umls-concept:C0443199 | lld:lifeskim |
pubmed-article:7537557 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:7537557 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:7537557 | pubmed:dateCreated | 1995-6-8 | lld:pubmed |
pubmed-article:7537557 | pubmed:abstractText | Two distinct T-cell glycoforms of CD43 result from differential glycosylation of a single gene product in vivo. The 115 kDa glycoform carries mainly tetrasaccharides and is a pan T-cell marker, whereas the 130 kDa glycoform carries mainly hexasaccharides and is associated with T-cell activation. CD43 has been shown to play a role both in enhancing and inhibiting cell adhesion; however, the function of the individual glycoforms is unknown. We have examined the distribution and regulation of the CD43 glycoforms in a murine model of acute graft-versus-host disease (GVHD) using monoclonal antibodies (mAbs) S7 and 1B11 specific for the 115 and 130 kDa CD43 glycoforms, respectively. An increase in T-lymphocyte CD43 130 kDa expression occurred during GVHD from day 4 onwards and coincided with splenomegaly and upregulation of the beta 1-6GlcNAc transferase (C2GnT), the key enzyme responsible for the addition of complex O-glycan branching to CD43. When T-lymphocyte subsets were examined for CD43 expression, we found that in GVHD, both CD43 glycoforms were upregulated on CD4+ T cells. However, in CD8+ T cells, CD43 115 kDa was downregulated while CD43 130 kDa was dramatically upregulated, such that two distinct CD8+1B11+ T-cell subsets were observed. These data demonstrate differential expression of the CD43 glycoforms in both resting and activated CD4+ and CD8+ T cells, and suggest that glycosylation differences between the CD43 glycoforms may reflect participation in the different functions of these T-cell subsets in immune disorders in vivo. | lld:pubmed |
pubmed-article:7537557 | pubmed:language | eng | lld:pubmed |
pubmed-article:7537557 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7537557 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7537557 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7537557 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7537557 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7537557 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7537557 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7537557 | pubmed:month | Dec | lld:pubmed |
pubmed-article:7537557 | pubmed:issn | 0959-6658 | lld:pubmed |
pubmed-article:7537557 | pubmed:author | pubmed-author:WilliamsM JMJ | lld:pubmed |
pubmed-article:7537557 | pubmed:author | pubmed-author:JonesA TAT | lld:pubmed |
pubmed-article:7537557 | pubmed:author | pubmed-author:ElliesL GLG | lld:pubmed |
pubmed-article:7537557 | pubmed:author | pubmed-author:ZiltenerH JHJ | lld:pubmed |
pubmed-article:7537557 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7537557 | pubmed:volume | 4 | lld:pubmed |
pubmed-article:7537557 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7537557 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7537557 | pubmed:pagination | 885-93 | lld:pubmed |
pubmed-article:7537557 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:7537557 | pubmed:year | 1994 | lld:pubmed |
pubmed-article:7537557 | pubmed:articleTitle | Differential regulation of CD43 glycoforms on CD4+ and CD8+ T lymphocytes in graft-versus-host disease. | lld:pubmed |
pubmed-article:7537557 | pubmed:affiliation | Biomedical Research Centre, University of British Columbia, Vancouver, Canada. | lld:pubmed |
pubmed-article:7537557 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7537557 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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