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Titolo:
SHIP's C-terminus is essential for its hydrolysis of PIP3 and inhibition of mast cell degranulation
Autore:
Damen, JE; Ware, MD; Kalesnikoff, J; Hughes, MR; Krystal, G;
Indirizzi:
British Columbia Canc Agcy, Terry Fox Lab, Vancouver, BC V5Z 1L3, Canada British Columbia Canc Agcy Vancouver BC Canada V5Z 1L3 BC V5Z 1L3, Canada
Titolo Testata:
BLOOD
fascicolo: 5, volume: 97, anno: 2001,
pagine: 1343 - 1351
SICI:
0006-4971(20010301)97:5<1343:SCIEFI>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
INOSITOL PHOSPHATASE SHIP; FC-GAMMA-RIIB; AFFINITY IGE RECEPTOR; HOMOLOGY-2 SH2 DOMAIN; B-CELLS; TYROSINE PHOSPHORYLATION; 5-PHOSPHATASE SHIP; PHOSPHOINOSITIDE 3-KINASE; DIFFERENTIAL ASSOCIATION; NEGATIVE REGULATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Krystal, G British Columbia Canc Agcy, Terry Fox Lab, 601 W 10th Ave, Vancouver, BC V5Z 1L3, Canada British Columbia Canc Agcy 601 W 10th Ave Vancouver BC Canada V5Z 1L3
Citazione:
J.E. Damen et al., "SHIP's C-terminus is essential for its hydrolysis of PIP3 and inhibition of mast cell degranulation", BLOOD, 97(5), 2001, pp. 1343-1351

Abstract

The SH2-containing inositol-5'-phosphatase, SHIP, restrains bone marrow-derived mast cell(BMMC) degranulation, at least in part, by hydrolyzing phosphatidylinositol (PI)-3-kinase generated PI-3,4,5-P-3 (PIP3) to PI-3,4-P-2. To determine which domains within SHIP influence its ability to hydrolyze PIPE, bone marrow from SHIP-/- mice was retrovirally infected with various SHIP constructs. Introduction of wild-type SHIP into SHIP-/- BMMCs reverted the Steel factor (SF)-induced increases in PIP3, calcium entry, and degranulation to those observed in SHIP+/+ BMMCs. A 5'-phosphatase dead SHIP, however, could not revert the SHIP-/- response, whereas a SHIP mutant in which the 2 NPXY motifs were converted to NPXFs (2NPXF) could partially revert the SHIP-/- response. SF stimulation of BMMCs expressing the 2NPXF, which could not bind Shc, led to the same level of mitogen-activated protein kinase (MAPK) phosphorylation as that seen in BMMCs expressing the other constructs. Surprisingly, C-terminally truncated forms of SHIP, lacking different amounts of the proline rich C-terminus, could not revert the SHIP-/- responseat all. These results suggest that the C-terminus plays a critical role inenabling SHIP to hydrolyze PIP3 and inhibit BMMC degranulation. (Blood. 2001;97:1343-1351) (C) 2001 by The American Society of Hematology.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/04/20 alle ore 03:14:17