pubmed-article:10570148 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10570148 | lifeskim:mentions | umls-concept:C0125090 | lld:lifeskim |
pubmed-article:10570148 | lifeskim:mentions | umls-concept:C0041485 | lld:lifeskim |
pubmed-article:10570148 | lifeskim:mentions | umls-concept:C0001721 | lld:lifeskim |
pubmed-article:10570148 | lifeskim:mentions | umls-concept:C0443254 | lld:lifeskim |
pubmed-article:10570148 | lifeskim:mentions | umls-concept:C0559956 | lld:lifeskim |
pubmed-article:10570148 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
pubmed-article:10570148 | lifeskim:mentions | umls-concept:C0249992 | lld:lifeskim |
pubmed-article:10570148 | pubmed:issue | 24 | lld:pubmed |
pubmed-article:10570148 | pubmed:dateCreated | 2000-1-6 | lld:pubmed |
pubmed-article:10570148 | 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. | lld:pubmed |
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pubmed-article:10570148 | pubmed:language | eng | lld:pubmed |
pubmed-article:10570148 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10570148 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:10570148 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10570148 | pubmed:month | Nov | lld:pubmed |
pubmed-article:10570148 | pubmed:issn | 0027-8424 | lld:pubmed |
pubmed-article:10570148 | pubmed:author | pubmed-author:RamachandranV... | lld:pubmed |
pubmed-article:10570148 | pubmed:author | pubmed-author:CummingsR DRD | lld:pubmed |
pubmed-article:10570148 | pubmed:author | pubmed-author:ZhuCC | lld:pubmed |
pubmed-article:10570148 | pubmed:author | pubmed-author:LiuW JWJ | lld:pubmed |
pubmed-article:10570148 | pubmed:author | pubmed-author:QiuHH | lld:pubmed |
pubmed-article:10570148 | pubmed:author | pubmed-author:McEverR PRP | lld:pubmed |
pubmed-article:10570148 | pubmed:author | pubmed-author:NollertM UMU | lld:pubmed |
pubmed-article:10570148 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10570148 | pubmed:day | 23 | lld:pubmed |
pubmed-article:10570148 | pubmed:volume | 96 | lld:pubmed |
pubmed-article:10570148 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10570148 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10570148 | pubmed:pagination | 13771-6 | lld:pubmed |
pubmed-article:10570148 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:10570148 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10570148 | pubmed:articleTitle | Tyrosine replacement in P-selectin glycoprotein ligand-1 affects distinct kinetic and mechanical properties of bonds with P- and L-selectin. | lld:pubmed |
pubmed-article:10570148 | pubmed:affiliation | W. K. Warren Medical Research Institute, Department of Medicine, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA. | lld:pubmed |
pubmed-article:10570148 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10570148 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:10570148 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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