Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
|
| pubmed:dateCreated |
1989-5-9
|
| pubmed:databankReference | |
| pubmed:abstractText |
GMP-140 is an integral membrane glycoprotein found in secretory granules of platelets and endothelial cells. After cellular activation, it is rapidly redistributed to the plasma membrane. The cDNA-derived primary structure of GMP-140 predicts a cysteine-rich protein with multiple domains, including a "lectin" region, an "EGF" domain, nine tandem consensus repeats related to those in complement-binding proteins, a transmembrane domain, and a short cytoplasmic tail. Some cDNAs also predict a soluble protein with a deleted transmembrane segment. The domain organization of GMP-140 is similar to that of ELAM-1, a cytokine-inducible endothelial cell receptor that binds neutrophils. This similarity suggests that GMP-140 belongs to a new family of inducible receptors with related structure and function on vascular cells.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Mar
|
| pubmed:issn |
0092-8674
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
24
|
| pubmed:volume |
56
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1033-44
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:2466574-Amino Acid Sequence,
pubmed-meshheading:2466574-Base Sequence,
pubmed-meshheading:2466574-Blotting, Northern,
pubmed-meshheading:2466574-Blotting, Southern,
pubmed-meshheading:2466574-Cell Adhesion,
pubmed-meshheading:2466574-Cloning, Molecular,
pubmed-meshheading:2466574-Cytoplasmic Granules,
pubmed-meshheading:2466574-DNA,
pubmed-meshheading:2466574-Endothelium, Vascular,
pubmed-meshheading:2466574-Homeostasis,
pubmed-meshheading:2466574-Humans,
pubmed-meshheading:2466574-Inflammation,
pubmed-meshheading:2466574-Intracellular Membranes,
pubmed-meshheading:2466574-Megakaryocytes,
pubmed-meshheading:2466574-Membrane Proteins,
pubmed-meshheading:2466574-Molecular Sequence Data,
pubmed-meshheading:2466574-P-Selectin,
pubmed-meshheading:2466574-Platelet Membrane Glycoproteins,
pubmed-meshheading:2466574-Protein Biosynthesis
|
| pubmed:year |
1989
|
| pubmed:articleTitle |
Cloning of GMP-140, a granule membrane protein of platelets and endothelium: sequence similarity to proteins involved in cell adhesion and inflammation.
|
| pubmed:affiliation |
St. Francis Medical Research Institute, University of Oklahoma Health Sciences Center, Oklahoma City.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|