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Titolo:
Vascular endothelial growth factor (VEGF)-driven actin-based motility is mediated by VEGFR2 and requires concerted activation of stress-activated protein kinase 2 (SAPK2/p38) and geldanamycin-sensitive phosphorylation of focal adhesion kinase
Autore:
Rousseau, S; Houle, F; Kotanides, H; Witte, L; Waltenberger, J; Landry, J; Huot, J;
Indirizzi:
Univ Laval, Hotel Dieu Quebec, Ctr Rech Cancerol, Quebec City, PQ G1R 2J6,Canada Univ Laval Quebec City PQ Canada G1R 2J6 , Quebec City, PQ G1R 2J6,Canada Univ Ulm, Med Ctr, Dept Internal Med 2, D-89081 Ulm, Germany Univ Ulm Ulm Germany D-89081 , Dept Internal Med 2, D-89081 Ulm, Germany ImClone Syst Inc, Dept Mol & Cell Biol, New York, NY 10014 USA ImClone Syst Inc New York NY USA 10014 Cell Biol, New York, NY 10014 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 14, volume: 275, anno: 2000,
pagine: 10661 - 10672
SICI:
0021-9258(20000407)275:14<10661:VEGF(A>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
P38 MAP KINASE; SIGNAL-TRANSDUCTION PATHWAYS; PHOSPHOLIPASE-C-GAMMA; HEAT-SHOCK PROTEIN-27; GTP-BINDING PROTEIN; FACTOR RECEPTOR KDR; NITRIC-OXIDE; TYROSINE KINASE; CELL-MIGRATION; OXIDATIVE STRESS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
81
Recensione:
Indirizzi per estratti:
Indirizzo: Huot, J Univ Laval, Hotel Dieu Quebec, Ctr Rech Cancerol, 11 Cote Palais, Quebec City, PQ G1R 2J6, Canada Univ Laval 11 Cote Palais Quebec City PQ Canada G1R 2J6 J6, Canada
Citazione:
S. Rousseau et al., "Vascular endothelial growth factor (VEGF)-driven actin-based motility is mediated by VEGFR2 and requires concerted activation of stress-activated protein kinase 2 (SAPK2/p38) and geldanamycin-sensitive phosphorylation of focal adhesion kinase", J BIOL CHEM, 275(14), 2000, pp. 10661-10672

Abstract

In endothelial cells, vascular endothelial growth factor (VEGF) induces anaccumulation of stress fibers associated with new actin polymerization andrapid formation of focal adhesions at the ventral surface of the cells. This cytoskeletal reorganization results in an intense motogenic activity. Using porcine endothelial cells expressing one or the other type of the VEGF receptors, VEGFR1 or VEGFR2, or human umbilical vein endothelial cells pretreated with a VEGFR2 neutralizing antibody, we show that VEGFR2 is responsible for VEGF-induced activation of the stress-activated protein kinase-2/p38 (SAPK2/p38), phosphorylation of focal adhesion kinase (FAK), and enhancedmigratory activity. Activation of SAPK2/p38 triggered actin polymerizationwhereas FAX, which was phosphorylated independently of SAPK2/p38, initiated assembly of focal adhesions. Both processes contributed to the formation of stress fibers. Geldanamycin, an inhibitor of HSP90 blocked tyrosine phosphorylation of FAK, assembly of focal adhesions, actin reorganization, and cell, migration, all of which were reversed by overexpressing HSP90. We conclude that VEGFR2 mediates the physiological effect of VEGF on cell migration and that two independent pathways downstream of VEGFR2 regulate actin-based motility. One pathway involves SAPK2/p38 and leads to enhanced actin polymerization activity. The other involves HSP90 as a permissive signal transduction factor implicated in FAK phosphorylation and assembly of focal adhesions.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/07/20 alle ore 06:16:34