Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Cell cycle protein expression in vascular smooth muscle cells in vitro andin vivo is regulated through phosphatidylinositol 3-kinase and mammalian target of rapamycin
Autore:
Braun-Dullaeus, RC; Mann, MJ; Seay, U; Zhang, LN; von der Leyen, HE; Morris, RE; Dzau, VJ;
Indirizzi:
Harvard Univ, Brigham & Womens Hosp, Sch Med, Boston, MA 02115 USA HarvardUniv Boston MA USA 02115 mens Hosp, Sch Med, Boston, MA 02115 USA Univ Giessen, Dept Med Cardiol, Giessen, Germany Univ Giessen Giessen Germany iessen, Dept Med Cardiol, Giessen, Germany Med Hsch Hannover, Hannover, Germany Med Hsch Hannover Hannover GermanyMed Hsch Hannover, Hannover, Germany Stanford Univ, Sch Med, Falk Cardiovasc Res Ctr, Stanford, CA USA StanfordUniv Stanford CA USA Falk Cardiovasc Res Ctr, Stanford, CA USA
Titolo Testata:
ARTERIOSCLEROSIS THROMBOSIS AND VASCULAR BIOLOGY
fascicolo: 7, volume: 21, anno: 2001,
pagine: 1152 - 1158
SICI:
1079-5642(200107)21:7<1152:CCPEIV>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
P70 S6 KINASE; GLYCOGEN-SYNTHASE KINASE-3; RAT CAROTID-ARTERY; INTIMAL HYPERPLASIA; MESSENGER-RNA; IN-VIVO; PROLIFERATION; INHIBITION; WORTMANNIN; ACTIVATION;
Keywords:
cell cycle protein; S6 kinase; phosphatidylinositol 3-kinase; balloon injury; vascular smooth muscle;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Dzau, VJ Harvard Univ, Brigham & Womens Hosp, Sch Med, Thorn 13,75 FrancisSt, Boston, MA 02115 USA Harvard Univ Thorn 13,75 Francis St Boston MA USA02115 02115 USA
Citazione:
R.C. Braun-Dullaeus et al., "Cell cycle protein expression in vascular smooth muscle cells in vitro andin vivo is regulated through phosphatidylinositol 3-kinase and mammalian target of rapamycin", ART THROM V, 21(7), 2001, pp. 1152-1158

Abstract

Cell cycle progression represents a key event in vascular proliferative diseases, one that depends on an increased rate of protein synthesis. An increase in phosphatidylinositol 3-kinase (PI 3-kinase) activity is associated with vascular smooth muscle cell proliferation, and rapamycin, which blocksthe activity of the mammalian target of rapamycin, inhibits this proliferation in vitro and in vivo. We hypothesized that these 2 molecules converge on a critical pathway of translational regulation that is essential for successful upregulation of cell cycle-regulatory proteins in activated smooth muscle cells, p70(S6) kinase, a target of PI 3-kinase and the mammalian target of rapamycin, was rapidly activated on growth factor stimulation of quiescent coronary artery smooth muscle cells and after balloon injury of rat carotid arteries. The translational repressor protein 4E-binding protein 1 was similarly hyperphosphorylated under these conditions. These events wereassociated with increases in the protein levels of cyclin B1, cyclin DI, cyclin E, cyclin-dependent kinase 1, cyclin-dependent kinase 2, proliferating cell nuclear antigen, and p21(Cip1) in vivo and in vitro, whereas inhibition of the PI 3-kinase signaling pathway with either rapamycin or wortmannin blocked the upregulation of these cell cycle proteins, but not mRNA, and arrested the cells in vitro before S phase. In contrast to findings in other cell types, growth factor- or balloon injury-induced downregulation of the cell cycle inhibitor p27(Kip1) was not affected by rapamycin treatment. These data suggest that cell cycle progression in vascular cells in vitro and in vivo depends on the integrity of the PI 3-kinase signaling pathway in allowing posttranscriptional accumulation of cell cycle proteins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 08/08/20 alle ore 09:02:43