Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4895
|
| pubmed:dateCreated |
1989-4-7
|
| pubmed:databankReference | |
| pubmed:abstractText |
Focal adhesion of leukocytes to the blood vessel lining is a key step in inflammation and certain vascular disease processes. Endothelial leukocyte adhesion molecule-1 (ELAM-1), a cell surface glycoprotein expressed by cytokine-activated endothelium, mediates the adhesion of blood neutrophils. A full-length complementary DNA (cDNA) for ELAM-1 has now been isolated by transient expression in COS cells. Cells transfected with the ELAM-1 clone express a surface structure recognized by two ELAM-1 specific monoclonal antibodies (H4/18 and H18/7) and support the adhesion of isolated human neutrophils and the promyelocytic cell line HL-60. Expression of ELAM-1 transcripts in cultured human endothelial cells is induced by cytokines, reaching a maximum at 2 to 4 hours and decaying by 24 hours; cell surface expression of ELAM-1 protein parallels that of the mRNA. The primary sequence of ELAM-1 predicts an amino-terminal lectin-like domain, an EGF domain, and six tandem repetitive motifs (about 60 amino acids each) related to those found in complement regulatory proteins. A similar domain structure is also found in the MEL-14 lymphocyte cell surface homing receptor, and in granule-membrane protein 140, a membrane glycoprotein of platelet and endothelial secretory granules that can be rapidly mobilized (less than 5 minutes) to the cell surface by thrombin and other stimuli. Thus, ELAM-1 may be a member of a nascent gene family of cell surface molecules involved in the regulation of inflammatory and immunological events at the interface of vessel wall and blood.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Mar
|
| pubmed:issn |
0036-8075
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
3
|
| pubmed:volume |
243
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1160-5
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:2466335-Amino Acid Sequence,
pubmed-meshheading:2466335-Base Sequence,
pubmed-meshheading:2466335-Cell Adhesion,
pubmed-meshheading:2466335-DNA,
pubmed-meshheading:2466335-E-Selectin,
pubmed-meshheading:2466335-Endothelium, Vascular,
pubmed-meshheading:2466335-Gene Expression Regulation,
pubmed-meshheading:2466335-Humans,
pubmed-meshheading:2466335-Immunoassay,
pubmed-meshheading:2466335-Interleukin-1,
pubmed-meshheading:2466335-Membrane Glycoproteins,
pubmed-meshheading:2466335-Molecular Sequence Data,
pubmed-meshheading:2466335-Neutrophils,
pubmed-meshheading:2466335-Nucleic Acid Hybridization,
pubmed-meshheading:2466335-Recombinant Proteins,
pubmed-meshheading:2466335-Sequence Homology, Nucleic Acid,
pubmed-meshheading:2466335-Transcription, Genetic,
pubmed-meshheading:2466335-Transfection,
pubmed-meshheading:2466335-Tumor Cells, Cultured,
pubmed-meshheading:2466335-Tumor Necrosis Factor-alpha
|
| pubmed:year |
1989
|
| pubmed:articleTitle |
Endothelial leukocyte adhesion molecule 1: an inducible receptor for neutrophils related to complement regulatory proteins and lectins.
|
| pubmed:affiliation |
Department of Pathology, Brigham and Women's Hospital, Boston, MA 02115.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|