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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
1988-9-26
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pubmed:abstractText |
Lymphocyte interactions with high endothelial venules (HEV) are important to the in vivo migration of normal and neoplastic lymphocyte populations. We have previously described an 85- to 95-kDa lymphocyte surface glycoprotein(s) defined by mAb Hermes-1, that is involved in the recognition of HEV by human lymphocytes: antibodies against distinct epitopes of the Hermes-1 Ag differentially inhibit lymphocyte binding to lymph node, mucosal, or synovial HEV. Here we characterize further the Hermes-1-defined glycoproteins. No well defined differences were observed between the Hermes-1 Ag immunoprecipitated from PBL and from mucosa- vs lymph HEV-specific cell lines. The Ag is an acidic (isoelectric point = 4.2) sulfated molecule bearing both O-linked and (3,4) N-linked oligosaccharide side chains. A subset of the Hermes-1-immunoprecipitated species is modified by covalent linkage to chondroitin sulfate, yielding a Mr of approximately 180 to 200 kDa. Pulse-chase labeling reveals a major precursor of 76 kDa that appears to be processed either to the 85- to 95-kDa form or, by addition of chondroitin sulfate, to a 180- to 200-kDa form. The potential role of these structural modifications, and particularly of chondroitin sulfate, in the function of the putative adhesion molecules is discussed.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Chondroitin Sulfates,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Mannosyl-Glycoprotein...,
http://linkedlifedata.com/resource/pubmed/chemical/Neuraminidase,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Lymphocyte Homing,
http://linkedlifedata.com/resource/pubmed/chemical/glycanase
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0022-1767
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
141
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1615-23
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:3137259-Animals,
pubmed-meshheading:3137259-Antibodies, Monoclonal,
pubmed-meshheading:3137259-Carbohydrate Conformation,
pubmed-meshheading:3137259-Chondroitin Sulfates,
pubmed-meshheading:3137259-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:3137259-Endothelium,
pubmed-meshheading:3137259-Endothelium, Lymphatic,
pubmed-meshheading:3137259-Glycoproteins,
pubmed-meshheading:3137259-Glycoside Hydrolases,
pubmed-meshheading:3137259-Glycosylation,
pubmed-meshheading:3137259-Humans,
pubmed-meshheading:3137259-Isoelectric Focusing,
pubmed-meshheading:3137259-Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase,
pubmed-meshheading:3137259-Mice,
pubmed-meshheading:3137259-Molecular Weight,
pubmed-meshheading:3137259-Neuraminidase,
pubmed-meshheading:3137259-Protein Precursors,
pubmed-meshheading:3137259-Rats,
pubmed-meshheading:3137259-Receptors, Immunologic,
pubmed-meshheading:3137259-Receptors, Lymphocyte Homing
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pubmed:year |
1988
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pubmed:articleTitle |
Biochemical properties of glycoproteins involved in lymphocyte recognition of high endothelial venules in man.
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pubmed:affiliation |
Department of Pathology, Stanford University Medical Center, CA 94305.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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