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Titolo:
c-jun N-terminal kinase activation by hydrogen peroxide in endothelial cells involves Src-dependent epidermal growth factor receptor transactivation
Autore:
Chen, K; Vita, JA; Berk, BC; Keaney, JF;
Indirizzi:
Boston Univ, Sch Med, Whitaker Cardiovasc Inst, Boston, MA 02118 USA Boston Univ Boston MA USA 02118 ker Cardiovasc Inst, Boston, MA 02118 USA Boston Univ, Sch Med, Evans Mem Dept Med, Boston, MA 02118 USA Boston Univ Boston MA USA 02118 Evans Mem Dept Med, Boston, MA 02118 USA Univ Rochester, Med Ctr, Cardiovasc Res Ctr, Rochester, NY 14642 USA Univ Rochester Rochester NY USA 14642 sc Res Ctr, Rochester, NY 14642 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 19, volume: 276, anno: 2001,
pagine: 16045 - 16050
SICI:
0021-9258(20010511)276:19<16045:CNKABH>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
SMOOTH-MUSCLE CELLS; OXIDATIVE STRESS; PROTEIN-KINASE; TYROSINE PHOSPHORYLATION; REVERSIBLE INACTIVATION; SIGNALING PATHWAYS; REDOX REGULATION; JNK ACTIVATION; MAP KINASES; P38;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
45
Recensione:
Indirizzi per estratti:
Indirizzo: Keaney, JF Boston Univ, Sch Med, Whitaker Cardiovasc Inst, 715 Albany St,Rm W507, Boston, MA 02118 USA Boston Univ 715 Albany St,Rm W507 Boston MA USA 02118 02118 USA
Citazione:
K. Chen et al., "c-jun N-terminal kinase activation by hydrogen peroxide in endothelial cells involves Src-dependent epidermal growth factor receptor transactivation", J BIOL CHEM, 276(19), 2001, pp. 16045-16050

Abstract

The phenotypic properties of the endothelium are subject to modulation by oxidative stress, and the c-dun N-terminal kinase (JNK) pathway is important in mediating cellular responses to stress, although activation of this pathway in endothelial cells has not been fully characterized. Therefore, we exposed endothelial cells to hydrogen peroxide (H2O2) and observed rapid activation of JNK within 15 min that involved phosphorylation of JNK and c-Jun and induction of AP-1 DNA binding activity, Inhibition of protein kinase C and phosphoinositide 3-kinase did not effect JNK activation. In contrast,the tyrosine kinase inhibitors, genistein, herbimycin A, and 4-amino-5-(4-chlorophenyl)-7-(t-butyl)pyrazolo[3,4-D]pyrimidine (PP2) significantly attenuated H2O2-induced JNK activation as did endothelial cell adenoviral transfection with a dominant-negative form of Src, implicating Src as an upstream activator of JNK, Activation of JNK by H2O2 was also inhibited by AG1478 and antisense oligonucleotides directed against the epidermal growth factorreceptor (EGFR), implicating the EGFR in this process. Consistent with this observation, H2O2 stimulated EGFR tyrosine phosphorylation and complex formation with Shc-Grb2 that was abolished by PP2, implicating Src in H2O2-induced EGFR activation. Tyrosine phosphorylation of the EGFR by H2O2 did notinvolve receptor autophosphorylation at Tyr(1173) as assessed by an autophosphorylation-specific antibody. These data indicate that H2O2-induced JNK activation in endothelial cells involves the EGFR through an Src-dependent pathway that is distinct from EGFR ligand activation. These data represent one potential pathway for mediating oxidative stress-induced phenotypic changes in the endothelium.

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Documento generato il 06/04/20 alle ore 08:43:46