| Literature DB >> 10582334 |
G Krystal1, J E Damen, C D Helgason, M Huber, M R Hughes, J Kalesnikoff, V Lam, P Rosten, M D Ware, S Yew, R K Humphries.
Abstract
In 1996 three groups independently cloned a hemopoietic specific, src homology 2-containing inositol 5'-phosphatase which, based on its structure, was called SHIP. More recently, a second more widely expressed SHIP-like protein has been cloned and called SHIP2. Both specifically hydrolyze phosphatidylinositol-3,4,5-trisphosphate and inositol 1,3,4,5-tetrakisphosphate in vitro. Moreover, SHIP has been shown in vivo to be the primary enzyme responsible for breaking down phosphatidylinositol-3,4,5-trisphosphate to phosphatidylinositol-3,4-bisphosphate in normal mast cells and, as a result, limits normal and prevents inappropriate mast cell degranulation. Because of their ability to break down phosphatidylinositol-3,4,5-trisphosphate, the SHIPs have the potential to regulate many, if not all, phosphatidylinositol-3-kinase induced events including, proliferation, differentiation, apoptosis, end cell activation, cell movement and adhesion and will thus likely be the subject of intensive research over the next few years.Entities:
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Year: 1999 PMID: 10582334 DOI: 10.1016/s1357-2725(99)00072-2
Source DB: PubMed Journal: Int J Biochem Cell Biol ISSN: 1357-2725 Impact factor: 5.085