Linked Life Data

2137074

Source:http://linkedlifedata.com/resource/pubmed/id/2137074

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1990-3-9
pubmed:abstractText
CR3 is probably the major adhesion molecule on monocytes and neutrophils. Its function as a phagocytic receptor for iC3b-coated particles has been well characterized. CR3 also has binding affinity for other ligands, including those that compete with iC3b such as fibrinogen, factor X, and beta-glucan, and those that do not such as bacterial LPS. CR3 binding to endothelial cells probably plays an important role in the extravascular migration of monocytes and neutrophils, but the ligand that it recognizes on endothelial cells has not been identified. Structurally CR3 belongs to the integrin family, and it shares a common subunit with p150,95 and LFA-1. The expression of these three membrane antigens appear to be limited to leukocytes, and they are sometimes referred to collectively as the leukocyte integrins. All three antigens have a common binding affinity for bacterial LPS. p150,95 also has affinity for iC3b, but p150,95/iC3b-dependent cellular responses has not been demonstrated. Its status as a complement receptor therefore awaits further experimental support.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0070-217X
pubmed:author
pubmed:issnType
Print
pubmed:volume
153
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
99-122
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
The leukocyte cell surface receptor(s) for the iC3b product of complement.
pubmed:affiliation
Sir William Dunn School of Pathology, University of Oxford, UK.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't