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*
The Terry Fox Laboratory, British Columbia Cancer Agency, Vancouver, British Columbia, Canada;
Eli Lilly, Indianapolis, IN 46285; and
Department of Pathology and Laboratory Medicine, University of British Columbia, Vancouver, British Columbia, Canada
I-1,3,4,5-P4, inositol-1,3,4,5-tetraphosphate; PI-3,4-P2, phosphatidylinositol-3,4-biphosphate; I-1,3,4-P3, inositol-1,3,4-trisphosphate; I-1,4,5-P3, inositol-1,4,5-trisphosphate; CH-1, cytohesin-1; Epo, erythropoietin; PKC, protein kinase C; PI-3K, phosphatidylinositol-3 kinase; MAPK, mitogen activated protein kinase; HA, hemaglutinin; BCECF-AM, 2',7'-bis-(2-carboxyethyl)-(and-6)-carboxyfluo-rescein, acetoxymeyhyl ester; PH, pleckstrin homology.
The inside-out signaling involved in the activation of LFA-1-mediated cell adhesion is still poorly understood. Here we examined the role of the SH2-containing inositol phosphatase (SHIP), a major negative regulator of intracellular signaling, in this process. Wild-type SHIP and a phosphatase-deficient mutant SHIP were overexpressed in the murine myeloid cell line, DA-ER, and the effects on LFA-1-mediated cell adhesion to ICAM-1 (CD54) were tested. Overexpression of wild-type SHIP significantly enhanced cell adhesion to immobilized ICAM-1, and PMA, IL-3, or erythropoietin further augmented this adhesion. In contrast, phosphatase dead SHIP had no enhancing effects. Furthermore, PMA-induced activation of LFA-1 on DA-ER cells overexpressing wild-type SHIP was dependent on protein kinase C but independent of mitogen-activated protein kinase activation, whereas cytokine-induced activation was independent of protein kinase C and mitogen-activated protein kinase activation but required phosphatidylinositol-3 kinase activation. These results suggest that SHIP may regulate two distinct inside-out signaling pathways and that the phosphatase activity of SHIP is essential for both of them.
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