Linked Life Data

9103236

Source:http://linkedlifedata.com/resource/pubmed/id/9103236

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1997-5-2
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0741-5400
pubmed:author
pubmed:issnType
Print
pubmed:volume
61
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
489-99
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Leukocyte activation induces surface redistribution of P-selectin glycoprotein ligand-1.
pubmed:affiliation
Department of Pathology, University of California, San Francisco 94143, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't