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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
24
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pubmed:dateCreated |
2000-1-6
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pubmed:abstractText |
Selectins are adhesion molecules that initiate tethering and rolling of leukocytes on the vessel wall. Rolling requires rapid formation and breakage of selectin-ligand bonds that must have mechanical strength to resist premature dissociation by the forces applied in shear flow. P- and L-selectin bind to the N-terminal region of P-selectin glycoprotein ligand-1 (PSGL-1), a mucin on leukocytes. To define determinants on PSGL-1 that contribute to the kinetic and mechanical properties of bonds with selectins, we compared rolling of transfected preB cells expressing P- or L-selectin on transfected cell monolayers expressing wild-type PSGL-1 or PSGL-1 constructs with substitutions in targeted N-terminal residues. Rolling through P- or L-selectin required a Thr or Ser at a specific position on PSGL-1, the attachment site for an essential O-glycan, but required only one of three nearby Tyr residues, which are sites for Tyr-SO(3) formation. The adhesive strengths and numbers of cells rolling through P- or L-selectin were similar on wild-type PSGL-1 and on each of the three PSGL-1 constructs containing only a single Tyr. However, the cells rolled more irregularly on the single-Tyr forms of PSGL-1. Analysis of the lifetimes of transient tethers on limiting densities of PSGL-1 revealed that L-selectin dissociated faster from single-Tyr than wild-type PSGL-1 at all shears examined. In sharp contrast, P-selectin dissociated faster from single-Tyr than wild-type PSGL-1 at higher shear but not at lower shear. Thus, tyrosine replacements in PSGL-1 affect distinct kinetic and mechanical properties of bonds with P- and L-selectin.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-10455156,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-1689464,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-1710173,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-2551036,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-347575,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-7505206,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-7532174,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-7535385,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-7538108,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-7553859,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-7559387,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-7585949,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-7585950,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-8207002,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-8538793,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-8621728,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-8626430,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-8662511,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-8787668,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-8896391,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-8896607,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-9239393,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-9281593,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-9507018,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-9582074,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-9618492,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-9751717,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10570148-9885254
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
96
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
13771-6
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:10570148-Amino Acid Sequence,
pubmed-meshheading:10570148-Animals,
pubmed-meshheading:10570148-B-Lymphocytes,
pubmed-meshheading:10570148-CHO Cells,
pubmed-meshheading:10570148-Cricetinae,
pubmed-meshheading:10570148-Gene Expression,
pubmed-meshheading:10570148-Genetic Engineering,
pubmed-meshheading:10570148-Hematopoietic Stem Cells,
pubmed-meshheading:10570148-Humans,
pubmed-meshheading:10570148-Kinetics,
pubmed-meshheading:10570148-L-Selectin,
pubmed-meshheading:10570148-Ligands,
pubmed-meshheading:10570148-Membrane Glycoproteins,
pubmed-meshheading:10570148-Molecular Sequence Data,
pubmed-meshheading:10570148-Mucins,
pubmed-meshheading:10570148-Mutagenesis, Site-Directed,
pubmed-meshheading:10570148-P-Selectin,
pubmed-meshheading:10570148-Sequence Homology, Amino Acid,
pubmed-meshheading:10570148-Tyrosine
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pubmed:year |
1999
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pubmed:articleTitle |
Tyrosine replacement in P-selectin glycoprotein ligand-1 affects distinct kinetic and mechanical properties of bonds with P- and L-selectin.
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pubmed:affiliation |
W. K. Warren Medical Research Institute, Department of Medicine, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, 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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