SHIPs ahoy

Citation
G. Krystal et al., SHIPs ahoy, INT J BIO C, 31(10), 1999, pp. 1007-1010
Citations number
11
Categorie Soggetti
Biochemistry & Biophysics
Journal title
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY
ISSN journal
13572725 → ACNP
Volume
31
Issue
10
Year of publication
1999
Pages
1007 - 1010
Database
ISI
SICI code
1357-2725(199910)31:10<1007:SA>2.0.ZU;2-7
Abstract
In 1996 three groups independently cloned a hemopoietic specific, are homol ogy 2-containing inositol 5'-phosphatase which, based on its structure, was called SHIP. More recently, a second more widely expressed SHIP-like prote in has been cloned and called SHIP2. Both specifically hydrolyze phosphatid ylinositol-3,4,5-trisphosphate and inositol 1,3,4,5-tetrakisphosphate in vi tro. Moreover, SHIP has been shown in vivo to be the primary enzyme respons ible for breaking down phosphatidylinositol-3,4,5-trisphosphate to phosphat idylinositol-3,4-bisphosphate in normal mast cells and, as a result, limits normal and prevents inappropriate mast cell degranulation. Because of thei r ability to break down phosphatidyrinositol-3,4,5-trisphosphate the SHIPs have the potential to regulate many, if not all, phosphatidylinositol-3-kin ase induced events including, proliferation, differentiation, apoptosis, en d cell activation, cell movement and adhesion and will thus likely be the s ubject of intensive research over the next few years. (C) 1999 Elsevier Sci ence Ltd. All rights reserved.