Ships ahoy

Autor: Gerald Krystal, Jacqueline E Damen, Cheryl D Helgason, Michael Huber, Michael R Hughes, Janet Kalesnikoff, Vivian Lam, Patty Rosten, Mark D Ware, Sandie Yew, R.Keith Humphries
Rok vydání: 1999
Předmět:
Zdroj: The International Journal of Biochemistry & Cell Biology. 31:1007-1010
ISSN: 1357-2725
Popis: 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.
Databáze: OpenAIRE