| pubmed-article:9103236 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9103236 | lifeskim:mentions | umls-concept:C1155000 | lld:lifeskim |
| pubmed-article:9103236 | lifeskim:mentions | umls-concept:C0205148 | lld:lifeskim |
| pubmed-article:9103236 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:9103236 | lifeskim:mentions | umls-concept:C0249992 | lld:lifeskim |
| pubmed-article:9103236 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:9103236 | pubmed:dateCreated | 1997-5-2 | lld:pubmed |
| pubmed-article:9103236 | pubmed:abstractText | Binding of P-selectin on activated endothelium to P-selectin glycoprotein ligand-1 (PSGL-1) on neutrophils mediates the initial tethering and rolling of neutrophils on the vessel wall at inflammatory sites. Upon activation of rolling cells by locally expressed signaling molecules, integrin-dependent adhesion mechanisms are engaged and transendothelial migration proceeds. P-selectin binding sites are uniformly distributed on the surface of quiescent neutrophils, but are redistributed to the uropod of activated neutrophils. It is unclear whether this activation-induced change in the surface topography of P-selectin binding sites is due to surface redistribution of PSGL-1, shedding of PSGL-1 from the lamellapod, and/or movement of PSGL-1 from an intracellular compartment to the uropod of the polarized cell. With the use of immunogold electron microscopy we previously demonstrated that PSGL-1 was localized to the tips of microvilli on neutrophils. Here we document a similar localization for PSGL-1 on eosinophils, basophils, monocytes, and lymphocytes. On quiescent neutrophils, approximately 80% of the PSGL-1 label was on tips of microvilli, which are randomly distributed around the cell circumference. On activated, polarized neutrophils, the PSGL-1 label was restricted to a segment of approximately 42% of the cell circumference even though total labeling decreased by only approximately 26%. Latex microbeads coated with anti-PSGL-1 mAb bound preferentially to the uropod of activated neutrophils. Subcellular fractionation and immunogold analysis of frozen thin sections of neutrophils failed to detect PSGL-1 in any intracellular compartment. Taken together, these data indicate that the activation-induced change in the surface topography of PSGL-1 is due to surface redistribution of PSGL-1. This process may facilitate transendothelial migration by disrupting bonds between P-selectin and PSGL-1 at the leading edge of migrating cells. | lld:pubmed |
| pubmed-article:9103236 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9103236 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9103236 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9103236 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9103236 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9103236 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9103236 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9103236 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9103236 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9103236 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9103236 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:9103236 | pubmed:issn | 0741-5400 | lld:pubmed |
| pubmed-article:9103236 | pubmed:author | pubmed-author:BaintonD FDF | lld:pubmed |
| pubmed-article:9103236 | pubmed:author | pubmed-author:BorregaardNN | lld:pubmed |
| pubmed-article:9103236 | pubmed:author | pubmed-author:ZimmermanG... | lld:pubmed |
| pubmed-article:9103236 | pubmed:author | pubmed-author:MooreK LKL | lld:pubmed |
| pubmed-article:9103236 | pubmed:author | pubmed-author:McEverR PRP | lld:pubmed |
| pubmed-article:9103236 | pubmed:author | pubmed-author:LorantD EDE | lld:pubmed |
| pubmed-article:9103236 | pubmed:author | pubmed-author:BruehlR ERE | lld:pubmed |
| pubmed-article:9103236 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9103236 | pubmed:volume | 61 | lld:pubmed |
| pubmed-article:9103236 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9103236 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9103236 | pubmed:pagination | 489-99 | lld:pubmed |
| pubmed-article:9103236 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:9103236 | pubmed:meshHeading | pubmed-meshheading:9103236-... | lld:pubmed |
| pubmed-article:9103236 | pubmed:meshHeading | pubmed-meshheading:9103236-... | lld:pubmed |
| pubmed-article:9103236 | pubmed:meshHeading | pubmed-meshheading:9103236-... | lld:pubmed |
| pubmed-article:9103236 | pubmed:meshHeading | pubmed-meshheading:9103236-... | lld:pubmed |
| pubmed-article:9103236 | pubmed:meshHeading | pubmed-meshheading:9103236-... | lld:pubmed |
| pubmed-article:9103236 | pubmed:meshHeading | pubmed-meshheading:9103236-... | lld:pubmed |
| pubmed-article:9103236 | pubmed:meshHeading | pubmed-meshheading:9103236-... | lld:pubmed |
| pubmed-article:9103236 | pubmed:meshHeading | pubmed-meshheading:9103236-... | lld:pubmed |
| pubmed-article:9103236 | pubmed:meshHeading | pubmed-meshheading:9103236-... | lld:pubmed |
| pubmed-article:9103236 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9103236 | pubmed:articleTitle | Leukocyte activation induces surface redistribution of P-selectin glycoprotein ligand-1. | lld:pubmed |
| pubmed-article:9103236 | pubmed:affiliation | Department of Pathology, University of California, San Francisco 94143, USA. | lld:pubmed |
| pubmed-article:9103236 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9103236 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9103236 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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