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GMP\u2010140, along with ELAM\u20101 and the peripheral lymph node homing receptor, defines the selectin family of structurally related molecules that regulate interactions of leukocytes with the blood vessel wall. Each of these molecules contains an N\u2010terminal lectin\u2010like domain, followed by an EGF\u2010like region, a series of consensus repeats related to those in complement\u2010binding proteins, a transmembrane domain, and a short cytoplasmic tail. The genomic structures of the selectins suggest that they arose by duplication and modification of exons encoding specific structural domains. GMP\u2010140 is a receptor for neutrophils and monocytes when it is expressed on activated platelets and endothelium. This property facilitates rapid adhesion of leukocytes to endothelium at regions of tissue injury as well as platelet\u2010leukocyte interactions at sites of inflammation and hemorrhage. Like other leukocyte adhesion molecules, GMP\u2010140 may also participate in pathologic inflammation, thrombosis, and tumor metastasis. Confirmation of such pathologic roles may lead to design of new drugs that block adhesive receptor function in human disease.<\/jats:p>","DOI":"10.1002\/jcb.240450206","type":"journal-article","created":{"date-parts":[[2005,5,28]],"date-time":"2005-05-28T20:36:59Z","timestamp":1117312619000},"page":"156-161","source":"Crossref","is-referenced-by-count":156,"title":["GMP\u2010140: A receptor for neutrophils and monocytes on activated platelets and endothelium"],"prefix":"10.1002","volume":"45","author":[{"given":"Rodger 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