Mar 24, 1989

Cloning of GMP-140, a granule membrane protein of platelets and endothelium: sequence similarity to proteins involved in cell adhesion and inflammation

G I JohnstonR P McEver


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.

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Mentioned in this Paper

CSRP1 gene
Transmembrane Domain
Blood Vessel
Neutrophils as Percentage of Blood Leukocytes (Lab Test)
Platelet Membrane Glycoproteins
Integral to Membrane
Protein Biosynthesis
Southern Blot Result
Absolute Neutrophil Count

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