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Yamao, Takuji; Noguchi, Tetsuya; Takeuchi, Osamu; Nishiyama, Uichi; Morita, Haruhiko; Hagiwara, Tetsuya; Akahori, Hironori; Kato, Takashi; Inagaki, Kenjiro; Okazawa, Hideki; Hayashi, Yoshitake; Matozaki, Takashi; Takeda, Kiyoshi; Akira, Shizuo; Kasuga, Masato
The Journal of biological chemistry, 10/2002, Letnik: 277, Številka: 42Journal Article
SHPS-1 is a receptor-type glycoprotein that binds and activates the protein-tyrosine phosphatases SHP-1 and SHP-2, and thereby negatively modulates intracellular signaling initiated by various cell surface receptors coupled to tyrosine kinases. SHPS-1 also regulates intercellular communication in the neural and immune systems through its association with CD47 (integrin-associated protein) on adjacent cells. Furthermore, recent studies with fibroblasts derived from mice expressing an SHPS-1 mutant that lacks most of the cytoplasmic region suggested that the intact protein contributes to cytoskeletal function. Mice homozygous for this SHPS-1 mutation have now been shown to manifest thrombocytopenia. These animals did not exhibit a defect in megakaryocytopoiesis or in platelet production. However, platelets were cleared from the bloodstream more rapidly in the mutant mice than in wild-type animals. Furthermore, peritoneal macrophages from the mutant mice phagocytosed red blood cells more effectively than did those from wild-type mice; in addition, they exhibited an increase both in the rate of cell spreading and in the formation of filopodia-like structures at the cell periphery. These results indicate that SHPS-1 both contributes to the survival of circulating platelets and down-regulates the macrophage phagocytic response.
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