Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
|
pubmed:dateCreated |
1991-2-20
|
pubmed:abstractText |
The contribution of oligosaccharides to the biochemical composition and antigen heterogeneity of the phosphotyrosine phosphatase CD45 glycoproteins has been studied on the K-562 erythroleukemic cell line. Treatment of immunoprecipitated CD45 glycoproteins with distinct exo- and endoglycosidases revealed the presence of highly sialylated O- and N-linked complex carbohydrates in the composition of mature CD45 glycoproteins. Incubation of K-562 cells with the N-glycosylation inhibitor tunicamycin blocked carbohydrate processing during biosynthesis of CD45 proteins, generating unglycosylated polypeptides similar in size to those resulting from digestion of CD45 proteins with a mixture of both N- and O-glycanases. Epitopes defining the T cell maturation related CD45R0 and CD45RB antigen specificities were present on the mature 180- and 190-kDa K-562 CD45 proteins, respectively. However, the CD45R0 and CD45RB epitopes were not detected on the high mannose biosynthetic CD45 precursors. Furthermore, treatment of CD45 proteins with O-glycanase or neuraminidase resulted in the loss of both CD45R0 and CD45RB epitopes, although reactivity of the anti-CD45R0 and anti-CD45RB mAb was not affected by mAb preincubation with either sialic acids or sialyllactose in solution. From these results we conclude that the blockade of early steps of N-glycosylation during carbohydrate processing resulted in the inhibition of subsequent incorporation of O-linked sugars on CD45 polypeptides, thus preventing the late acquisition of the CD45R0 and CD45RB determinants on the 180- and 190-kDa CD45 polypeptides.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD45,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation...,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/Sialoglycoproteins
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0014-2980
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
20
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
2667-71
|
pubmed:dateRevised |
2007-11-15
|
pubmed:meshHeading |
pubmed-meshheading:1702721-Antibodies, Monoclonal,
pubmed-meshheading:1702721-Antigens, CD,
pubmed-meshheading:1702721-Antigens, CD45,
pubmed-meshheading:1702721-Antigens, Differentiation,
pubmed-meshheading:1702721-Antigens, Differentiation, T-Lymphocyte,
pubmed-meshheading:1702721-Epitopes,
pubmed-meshheading:1702721-Glycosylation,
pubmed-meshheading:1702721-Histocompatibility Antigens,
pubmed-meshheading:1702721-Humans,
pubmed-meshheading:1702721-Molecular Weight,
pubmed-meshheading:1702721-Precipitin Tests,
pubmed-meshheading:1702721-Protein Processing, Post-Translational,
pubmed-meshheading:1702721-Sialoglycoproteins,
pubmed-meshheading:1702721-T-Lymphocyte Subsets,
pubmed-meshheading:1702721-Thymus Gland
|
pubmed:year |
1990
|
pubmed:articleTitle |
Glycosylation of CD45: carbohydrate composition and its role in acquisition of CD45R0 and CD45RB T cell maturation-related antigen specificities during biosynthesis.
|
pubmed:affiliation |
Servicio de Immunología, Hospital de la Princesa, Universidad Autónoma de Madrid, Spain.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|