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Titolo:
Role of p38 MAP kinase in diperoxovanadate-induced phospholipase D activation in endothelial cells
Autore:
Natarajan, V; Scribner, WM; Morris, AJ; Roy, S; Vepa, S; Yang, JB; Wadgaonkar, R; Reddy, SPM; Garcia, JGN; Parinandi, NL;
Indirizzi:
Johns Hopkins Univ, Sch Med, Div Pulm & Crit Care Med, Baltimore, MD 21224USA Johns Hopkins Univ Baltimore MD USA 21224 are Med, Baltimore, MD 21224USA SUNY Stony Brook, Hlth Sci Ctr, Dept Pharmacol Sci, Stony Brook, NY 11794 USA SUNY Stony Brook Stony Brook NY USA 11794 Sci, Stony Brook, NY 11794 USA
Titolo Testata:
AMERICAN JOURNAL OF PHYSIOLOGY-LUNG CELLULAR AND MOLECULAR PHYSIOLOGY
fascicolo: 2, volume: 281, anno: 2001,
pagine: L435 - L449
SICI:
1040-0605(200108)281:2<L435:ROPMKI>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
ADP-RIBOSYLATION FACTOR; SMOOTH-MUSCLE CELLS; PROTEIN-TYROSINE PHOSPHORYLATION; PHOSPHATASE INHIBITORS; INOSITOL PHOSPHATES; SIGNAL-TRANSDUCTION; HUMAN NEUTROPHILS; ARACHIDONIC-ACID; RAT ADIPOCYTES; IN-VIVO;
Keywords:
reactive oxygen species; p38 mitogen-activated protein kinase; vascular endothelium; phospholipase D; phosphorylation; peroxovanadate;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
55
Recensione:
Indirizzi per estratti:
Indirizzo: Natarajan, V Johns Hopkins Univ, Sch Med, Div Pulm & Crit Care Med, Johns Hopkins Asthma & Allergy Bldg,5501 Hopkins, Baltimore, MD 21224 USA Johns Hopkins Univ Johns Hopkins Asthma & Allergy Bldg,5501 Hopkins Baltimore MD USA 21224
Citazione:
V. Natarajan et al., "Role of p38 MAP kinase in diperoxovanadate-induced phospholipase D activation in endothelial cells", AM J P-LUNG, 281(2), 2001, pp. L435-L449

Abstract

We previously demonstrated that diperoxovanadate (DPV), a synthetic peroxovanadium compound and cell-permeable oxidant that acts as a protein tyrosine phosphatase inhibitor and insulinomimetic, increased phospholipase D (PLD) activation in endothelial cells (ECs). In this report, the regulation of DPV-induced PLD activation by mitogen-activated protein kinases (MAPKs) wasinvestigated. DPV activated extracellular signal-regulated kinase, c-Jun NH2-terminal kinase (JNK), and p38 MAPK in a dose- and time-dependent fashion. Treatment of ECs with p38 MAPK inhibitors SB-203580 and SB-202190 or transient transfection with a p38 dominant negative mutant mitigated the PLD activation by DPV but not by phorbol ester. SB-202190 blocked DPV-mediated p38 MAPK activity as determined by activated transcription factor-2 phosphorylation. Immunoprecipitation of PLD from EC lysates with PLD1 and PLD2 antibodies revealed both PLD isoforms associated with p38 MAPK. Similarly, PLD1and PLD2 were detected in p38 immunoprecipitates from control and DPV-challenged ECs. Binding assays demonstrated interaction of glutathione S-transferase-p38 fusion protein with PLD1 and PLD2. Both PLD1 and PLD2 were phosphorylated by p38 MAPK in vitro, and DPV increased phosphorylation of PLD1 and PLD2 in vivo. However, phosphorylation of PLD by p38 failed to affect PLDactivity in vitro. These results provide evidence for p38 MAPK-mediated regulation of PLD in ECs.

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Documento generato il 01/10/20 alle ore 14:54:56