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rdf:type |
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lifeskim:mentions |
umls-concept:C0007004,
umls-concept:C0007634,
umls-concept:C0125090,
umls-concept:C0127400,
umls-concept:C0134835,
umls-concept:C0183683,
umls-concept:C0282651,
umls-concept:C0344211,
umls-concept:C0558295,
umls-concept:C0597538,
umls-concept:C0806140,
umls-concept:C1171411,
umls-concept:C1317973,
umls-concept:C1514873,
umls-concept:C1521721,
umls-concept:C1548789
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pubmed:issue |
36
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pubmed:dateCreated |
2002-9-2
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pubmed:abstractText |
l- and P-selectin are known to require sulfation in their ligand molecules. We investigated the significance of carbohydrate 6-sulfation and tyrosine sulfation in selectin-mediated cell adhesion. COS-7 cells were genetically engineered to express P-selectin glycoprotein ligand-1 (PSGL-1) or its mutant in various combinations with 6-O-sulfotransferase (6-Sul-T) and/or alpha1-->3fucosyltransferase VII (Fuc-T VII). The cells transfected with PSGL-1, 6-Sul-T, and Fuc-T VII cDNAs supported rolling mediated by all three selectins and provided the best experimental system so far to estimate kinetic parameters in selectin-mediated cell adhesion for all three selectins using the identical rolling substrate and to compare the ligand specificity of each selectin. L-selectin-mediated rolling was drastically impaired if the cells lacked carbohydrate 6-sulfation elaborated by 6-Sul-T, but not affected when PSGL-1 was replaced with a mutant lacking three tyrosine residues at its NH(2) terminus. L-selectin-mediated adhesion was also hardly affected by mocarhagin treatment of the cells, which cleaved a short peptide containing sulfated tyrosine residues from PSGL-1. In contrast, P-selectin-mediated rolling was abolished when PSGL-1 was either mutated or cleaved by mocarhagin at its NH(2) terminus, whereas the cells expressing PSGL-1 and Fuc-T VII but not 6-Sul-T showed only a modest decrease in P-selectin-mediated adhesion. These results indicate that L-selectin prefers carbohydrate 6-sulfation much more than tyrosine sulfation, whereas P-selectin favors tyrosine sulfation in the PSGL-1 molecule far more than carbohydrate 6-sulfation. E-selectin-mediated adhesion was sulfation-independent requiring only Fuc-T VII, and thus the three members of the selectin family have distinct requirements for ligand sulfation.
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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/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD34,
http://linkedlifedata.com/resource/pubmed/chemical/Cobra Venoms,
http://linkedlifedata.com/resource/pubmed/chemical/Fucosyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/L-Selectin,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/P-Selectin,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfotransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfur,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/galactoside 3-fucosyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/mocarhagin,
http://linkedlifedata.com/resource/pubmed/chemical/tyrosine O-sulfate
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
277
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
32578-86
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12068018-Animals,
pubmed-meshheading:12068018-Antibodies, Monoclonal,
pubmed-meshheading:12068018-Antigens, CD34,
pubmed-meshheading:12068018-COS Cells,
pubmed-meshheading:12068018-Carbohydrate Metabolism,
pubmed-meshheading:12068018-Cell Adhesion,
pubmed-meshheading:12068018-Cobra Venoms,
pubmed-meshheading:12068018-Flow Cytometry,
pubmed-meshheading:12068018-Fucosyltransferases,
pubmed-meshheading:12068018-Gene Deletion,
pubmed-meshheading:12068018-Genetic Vectors,
pubmed-meshheading:12068018-Humans,
pubmed-meshheading:12068018-L-Selectin,
pubmed-meshheading:12068018-Ligands,
pubmed-meshheading:12068018-Metalloendopeptidases,
pubmed-meshheading:12068018-P-Selectin,
pubmed-meshheading:12068018-Protein Structure, Tertiary,
pubmed-meshheading:12068018-Substrate Specificity,
pubmed-meshheading:12068018-Sulfotransferases,
pubmed-meshheading:12068018-Sulfur,
pubmed-meshheading:12068018-Transfection,
pubmed-meshheading:12068018-Tyrosine
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pubmed:year |
2002
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pubmed:articleTitle |
Distinct sulfation requirements of selectins disclosed using cells that support rolling mediated by all three selectins under shear flow. L-selectin prefers carbohydrate 6-sulfation totyrosine sulfation, whereas p-selectin does not.
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pubmed:affiliation |
Program of Molecular Pathology, Aichi Cancer Center, Research Institute, Nagoya 464-8681, Japan.
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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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