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(Received for publication, May 8, 1997, and in revised form, August 8, 1997)
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From The SH2 domain-containing inositol 5-phosphatase,
SHIP, known to dephosphorylate inositol 1,3,4,5-tetrakisphosphate and
phosphatidylinositol 3,4,5-trisphosphate has recently been shown to be
expressed in a variety of hemopoietic cells. This 145-kDa protein is
induced to associate with Shc by multiple cytokines and may play an
important role in the negative regulation of immunocompetent cells
mediated by Fc
INSERM Unité 326, Institut
Fédératif de Recherche 30, Hôpital Purpan, 31059 Toulouse, France, ¶ Interdisciplinary Research Institute (IRIBHN),
Université Libre de Bruxelles, Campus Erasme, 808 Route de
Lennik, 1070 Brussels, Belgium, and ** Protein Phosphorylation
Laboratory, Imperial Cancer Research Fund, 44 Lincoln's Inn Fields,
London WC2A 3PX, United Kingdom
RIIB receptor. We report here that SHIP is present in
human blood platelets and may be involved in platelet activation evoked by thrombin. Platelet SHIP was identified by Western blotting as a
single 145-kDa protein. Both phosphatidylinositol 3,4,5-trisphosphate and inositol 1,3,4,5-tetrakisphosphate 5-phosphatase activities could
be demonstrated in anti-SHIP immunoprecipitates of platelet lysate.
Thrombin stimulation induced a tyrosine phosphorylation of SHIP, this
effect being prevented if platelets were not shaken or if
RGD-containing peptides were present, indicating an
aggregation-dependent, integrin-mediated event. Moreover,
although the intrinsic phosphatase activity of SHIP did not appear to
be significantly increased, tyrosine-phosphorylated SHIP was relocated
to the actin cytoskeleton upon activation in an aggregation- and
integrin engagement-dependent manner. Finally, the striking correlation
observed between phosphatidylinositol 3,4-bisphosphate production and
the tyrosine phosphorylation of SHIP, as well as its relocation to the
cytoskeleton upon thrombin stimulation, suggest a role for SHIP in the
aggregation-dependent and GpIIb-IIIa-mediated accumulation
of this important phosphoinositide.
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