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Titolo:
A novel receptor-mediated regulation mechanism of type I inositol polyphosphate 5-phosphatase by calcium/calmodulindependent protein kinase II phosphorylation
Autore:
Communi, D; Gevaert, K; Demol, H; Vandekerckhove, J; Erneux, C;
Indirizzi:
Free Univ Brussels, Inst Interdisciplinary Res, B-1070 Brussels, Belgium Free Univ Brussels Brussels Belgium B-1070 Res, B-1070 Brussels, Belgium Ghent Univ, Flanders Interuniv Inst Biotechnol, Dept Med Prot Res, Fac Med& Hlth Sci, B-9000 Ghent, Belgium Ghent Univ Ghent Belgium B-9000 Fac Med& Hlth Sci, B-9000 Ghent, Belgium
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 42, volume: 276, anno: 2001,
pagine: 38738 - 38747
SICI:
0021-9258(20011019)276:42<38738:ANRRMO>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
CEREBELLAR PURKINJE-CELLS; 1,4,5-TRISPHOSPHATE 3-KINASE; CA2+ OSCILLATIONS; DENDRITIC SPINES; INOSITOL-1,4,5-TRISPHOSPHATE 5-PHOSPHATASE; PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE; ESCHERICHIA-COLI; RBL-2H3 CELLS; CAM KINASE; RAT-BRAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
67
Recensione:
Indirizzi per estratti:
Indirizzo: Communi, D Free Univ Brussels, Inst Interdisciplinary Res, Campus Erasme,Bldg C,808 Route Lennik, B-1070 Brussels, Belgium Free Univ Brussels Campus Erasme,Bldg C,808 Route Lennik Brussels Belgium B-1070
Citazione:
D. Communi et al., "A novel receptor-mediated regulation mechanism of type I inositol polyphosphate 5-phosphatase by calcium/calmodulindependent protein kinase II phosphorylation", J BIOL CHEM, 276(42), 2001, pp. 38738-38747

Abstract

D-myo-inositol 1,4,5-trisphosphate (Ins(1,4,5)P-3) and D-myo-inositol 1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P-4) are both substrates of the 43-kDa type I inositol polyphosphate 5-phosphatase. Transient and okadaic acid-sensitive inhibition by 70-85% of Ins(1,4,5)P-3 and Ins(1,3,4,5)P4 5-phosphatase activities was observed in homogenates from rat cortical astrocytes, human astrocytoma 1321N1 cells, and rat basophilic leukemia RBL-2H3 cells afterincubation with carbachol. The effect was reproduced in response to UTP inrat astrocytic cells and Chinese hamster ovary cells overexpressing human type I 5-phosphatase. Immunodetection as well as mass spectrometric peptidemass fingerprinting and post-source decay (PSD) sequence data analysis after immunoprecipitation permitted unambiguous identification of the major native 5-phosphatase isoform hydrolyzing Ins(1,4,5)P-3 and Ins(1,3,4,5)P4 as type I inositol polyphosphate 5-phosphatase. In ortho P-32-preincubated cells, the phosphorylated 43 kDa-enzyme could be identified after receptor activation by immunoprecipitation followed by electrophoretic separation. Phosphorylation of type I 5-phosphatase was blocked after cell preincubation inthe presence of Ca2+/calmodulin kinase II inhibitors (i.e. KN-93 and KN-62). In vitro phosphorylation of recombinant type I enzyme by Ca2+/calmodulinkinase II resulted in an inhibition (i.e. 60-80%) of 5-phosphatase activity. In this study, we demonstrated for the first time a novel regulation mechanism of type I 5-phosphatase by phosphorylation in intact cells.

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Documento generato il 07/07/20 alle ore 21:21:43