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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
2001-7-5
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pubmed:databankReference |
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pubmed:abstractText |
L-selectin mediates lymphocyte homing by facilitating lymphocyte adhesion to addressins expressed in the high endothelial venules (HEV) of secondary lymphoid organs. Peripheral node addressin recognized by the MECA-79 antibody is apparently part of the L-selectin ligand, but its chemical nature has been undefined. We now identify a sulfated extended core1 mucin-type O-glycan, Gal beta 1-->4(sulfo-->6)GlcNAc beta 1-->3Gal beta 1-->3GalNAc, as the MECA-79 epitope. Molecular cloning of a HEV-expressed core1-beta 1,3-N-acetylglucosaminyltransferase (Core1-beta 3GlcNAcT) enabled the construction of the 6-sulfo sialyl Lewis x on extended core1 O-glycans, recapitulating the potent L-selectin-mediated, shear-dependent adhesion observed with novel L-selectin ligands derived from core2 beta1,6-N-acetylglucosaminyltransferase-I null mice. These results identify Core1-beta 3GlcNAcT and its cognate extended core1 O-glycans as essential participants in the expression of the MECA-79-positive, HEV-specific L-selectin ligands required for lymphocyte homing.
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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 |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/L-Selectin,
http://linkedlifedata.com/resource/pubmed/chemical/L-selectin counter-receptors,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/N-Acetylglucosaminyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Lymphocyte Homing,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfates
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
105
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
957-69
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11439191-Animals,
pubmed-meshheading:11439191-Antigens, Surface,
pubmed-meshheading:11439191-CHO Cells,
pubmed-meshheading:11439191-Carbohydrate Conformation,
pubmed-meshheading:11439191-Carbohydrate Sequence,
pubmed-meshheading:11439191-Cell Adhesion,
pubmed-meshheading:11439191-Cricetinae,
pubmed-meshheading:11439191-Epitopes,
pubmed-meshheading:11439191-Humans,
pubmed-meshheading:11439191-Immunoblotting,
pubmed-meshheading:11439191-In Situ Hybridization,
pubmed-meshheading:11439191-L-Selectin,
pubmed-meshheading:11439191-Ligands,
pubmed-meshheading:11439191-Lymphoid Tissue,
pubmed-meshheading:11439191-Membrane Proteins,
pubmed-meshheading:11439191-Mice,
pubmed-meshheading:11439191-Mice, Knockout,
pubmed-meshheading:11439191-Molecular Sequence Data,
pubmed-meshheading:11439191-N-Acetylglucosaminyltransferases,
pubmed-meshheading:11439191-Polysaccharides,
pubmed-meshheading:11439191-Receptors, Lymphocyte Homing,
pubmed-meshheading:11439191-Sulfates,
pubmed-meshheading:11439191-Transfection,
pubmed-meshheading:11439191-Venules
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pubmed:year |
2001
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pubmed:articleTitle |
Novel sulfated lymphocyte homing receptors and their control by a Core1 extension beta 1,3-N-acetylglucosaminyltransferase.
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pubmed:affiliation |
Glycobiology Program, Cancer Research Center, The Burnham Institute, La Jolla, CA 92037, USA.
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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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