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Titolo:
REGULATION OF MAP KINASE-ACTIVITY BY GROWTH STIMULI IN VASCULAR SMOOTH-MUSCLE
Autore:
LANGAN EM; YOUKEY JR; ELMORE JR; FRANKLIN DP; SINGER HA;
Indirizzi:
GEISINGER MED CLIN,SIGFRIED & JANET WEIS CTR RES,100 N ACAD AVE DANVILLE PA 17822 GEISINGER MED CLIN,DEPT VASC SURG DANVILLE PA 17822
Titolo Testata:
The Journal of surgical research
fascicolo: 1, volume: 57, anno: 1994,
pagine: 215 - 220
SICI:
0022-4804(1994)57:1<215:ROMKBG>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACTIVATED PROTEIN-KINASE; SIGNAL-TRANSDUCTION; BIPHASIC ACTIVATION; CELLS; FIBROBLASTS; RSK; VASOPRESSIN; P42(MAPK); P44(MAPK); TYROSINE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
24
Recensione:
Indirizzi per estratti:
Citazione:
E.M. Langan et al., "REGULATION OF MAP KINASE-ACTIVITY BY GROWTH STIMULI IN VASCULAR SMOOTH-MUSCLE", The Journal of surgical research, 57(1), 1994, pp. 215-220

Abstract

Intracellular signaling pathways regulating vascular smooth muscle (VSM) cell growth and hypertrophy can be initiated by activation of receptor tyrosine kinases and/or protein kinase C (PKC). Mitogen-activatedprotein kinases (MAP kinases) are cytosolic serine/threonine kinases,proposed to act as a point of convergence for diverse growth factors utilizing these signaling pathways. The goals of this study were (1) to determine whether MAP kinase is expressed in cultured rat aortic VSM, (2) to assess the activation of MAP kinase by known proliferative and hypertrophic stimuli, and (3) to determine if stimulation of a PKC-dependent signaling pathway in these cells results in MAP kinase activation. MAP kinase activity was measured in cytosolic extracts of aorticVSM by quantifying myelin basic protein phosphorylation. Three peaks of activity were resolved chromatographically and identified as MAP kinase isoforms (MW 42, 44, and 46 kDa) by immunoblotting with antipeptide antibodies specific for MAP kinase. MAP kinase activity in quiescent growth-arrested cells (157 +/- 19 pmole P-32/min/mg) was markedly stimulated within 15 min by known mitogens (10% serum, 731 +/- 40 pmole P-32/min/mg; 40 ng/ml PDGF, 670 +/- 105 pmole P-32/min/mg; P < 0.01) and partially sustained for at least 90 min (serum, 606 +/- 34 pmole P-32/min/mg; PDGF, 323 +/- 59 pmole P-32/min/mg P < 0.05). Angiotensin II (AII, 0.1 mu M) and a pharmacological PKC activator, phorbol 12,13-dibutyrate (PDB, 0.1 mu M), are reported to be nonmitogenic hypertrophic stimuli in these cells. These stimuli transiently increased MAP kinase activity with a peak at 5 min (AII, 328 +/- 15 pmole P-32/min/mg; PDB, 592 +/- 41 pmole P-32/min/mg; P < 0.05). Regulation of MAP kinase by a PKC-dependent signaling pathway in aortic smooth muscle could contribute to cellular responses elicited by proliferative and/or hypertrophic stimuli. (C) 1994 Academic Press, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/08/20 alle ore 04:18:19