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Titolo:
Cellular activation triggered by the autosomal dominant polycystic kidney disease gene product PKD2
Autore:
Arnould, T; Sellin, L; Benzing, T; Tsiokas, L; Cohen, HT; Kim, E; Walz, G;
Indirizzi:
Beth Israel Deaconess Med Ctr, Dept Med, Div Renal, Boston, MA 02215 USA Beth Israel Deaconess Med Ctr Boston MA USA 02215 l, Boston, MA 02215 USA Boston Univ, Med Ctr, Dept Med, Renal Sect, Boston, MA 02118 USA Boston Univ Boston MA USA 02118 ept Med, Renal Sect, Boston, MA 02118 USA Harvardon,iv, Massachusetts Gen Hosp, Sch Med, Lab Mol & Dev Neurosci, Bost Harvard Univ Boston MA USA 02114 p, Sch Med, Lab Mol & Dev Neurosci, Bost
Titolo Testata:
MOLECULAR AND CELLULAR BIOLOGY
fascicolo: 5, volume: 19, anno: 1999,
pagine: 3423 - 3434
SICI:
0270-7306(199905)19:5<3423:CATBTA>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-KINASE-C; GROWTH-FACTOR; SIGNAL-TRANSDUCTION; CPK MOUSE; JUN; CELLS; RHO; EXPRESSION; ISOFORMS; AP-1;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
55
Recensione:
Indirizzi per estratti:
Indirizzo: Walz, G Bethon,rael Deaconess Med Ctr, Dept Med, Div Renal, 330 Brookline Ave, Bost Beth Israel Deaconess Med Ctr 330 Brookline Ave Boston MA USA 02215
Citazione:
T. Arnould et al., "Cellular activation triggered by the autosomal dominant polycystic kidney disease gene product PKD2", MOL CELL B, 19(5), 1999, pp. 3423-3434

Abstract

Autosomal dominant polycystic kidney disease (ADPKD) is caused by germ line mutations in at least three ADPKD genes. Two recently isolated ADPKD genes, PKD1 and PKD2, encode integral membrane proteins of unknown function. Wefound that PKD2 upregulated AP-1-dependent transcription in human embryonic kidney 293T cells. The PKD2-mediated AP-1 activity was dependent upon activation of the mitogen-activated protein kinases p38 and JNK1 and protein kinase C (PKC) epsilon, a calcium-independent PKC isozyme. Staurosporine, but not the calcium chelator BAPTA [1,2-bis(o-aminophenoxy)ethane-N,N,N',N' -tetraacetate], inhibited PKD2-mediated signaling, consistent with the involvement of a calcium-independent PRC isozyme. Coexpression of PKD2 with the interacting C terminus of PKD1 dramatically augmented PKD2-mediated AP-1 activation. The synergistic signaling between PKD1 and PKD2 involved the activation of two distinct PKC isozymes, PKC alpha and PKC epsilon, respectively. Our findings are consistent with others that support a functional connection between PKD1 and PKD2 involving multiple signaling pathways that converge to induce AP-1 activity, a transcription factor that regulates different cellular programs such as proliferation, differentiation, and apoptosis. Activation of these signaling cascades may promote the full maturation of developing tubular epithelial cells, while inactivation of these signaling cascades may impair terminal differentiation and facilitate the development of renal tubular cysts.

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Documento generato il 27/10/20 alle ore 05:01:20