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Titolo:
Transport function of the naturally occurring pathogenic polycystin-2 mutant, R742X
Autore:
Chen, XZ; Segal, Y; Basora, N; Guo, L; Peng, JB; Babakhanlou, H; Vassilev, PM; Brown, EM; Hediger, MA; Zhou, J;
Indirizzi:
Brigham & Womens Hosp, Div Renal, Boston, MA 02115 USA Brigham & Womens Hosp Boston MA USA 02115 Div Renal, Boston, MA 02115 USA Brigham & Womens Hosp, Div Endocrine Hypertens, Boston, MA 02115 USA Brigham & Womens Hosp Boston MA USA 02115 Hypertens, Boston, MA 02115 USA Brigham & Womens Hosp, Membrane Biol Program, Dept Med, Boston, MA 02115 USA Brigham & Womens Hosp Boston MA USA 02115 Dept Med, Boston, MA 02115 USA Harvard Univ, Sch Med, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 vard Univ, Sch Med, Boston, MA 02115 USA Univ Alberta, Dept Physiol, Edmonton, AB T6G 2H7, Canada Univ Alberta Edmonton AB Canada T6G 2H7 iol, Edmonton, AB T6G 2H7, Canada
Titolo Testata:
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
fascicolo: 5, volume: 282, anno: 2001,
pagine: 1251 - 1256
SICI:
0006-291X(20010420)282:5<1251:TFOTNO>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
KIDNEY-DISEASE; GENE-PRODUCT; PKD2 GENE; CALCIUM; PROTEIN; CHANNEL; IDENTIFICATION; CURRENTS;
Keywords:
electrophysiology; current; calcium; Xenopus oocyte; myc-tag; mutagenesis; cation; two-microelectrode voltage clamp;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Hediger, MA Harvard Univ, Inst Med, Room 522,77 Ave Louis Pasteur, Boston,MA 02115 USA Harvard Univ Room 522,77 Ave Louis Pasteur Boston MA USA 02115
Citazione:
X.Z. Chen et al., "Transport function of the naturally occurring pathogenic polycystin-2 mutant, R742X", BIOC BIOP R, 282(5), 2001, pp. 1251-1256

Abstract

Most patients with autosomal dominant polycystic kidney disease (ADPKD) harbor mutations truncating polycystin-1 (PC1) or polycystin-2 (PC2), products of the PKD1 and PKD2 genes, respectively. A third member of the polycystin family, polycystin-L (PCL), was recently shown to function as a Ca2+-modulated nonselective cat ion channel. More recently, PC2 was also shown to bea nonselective cation channel with comparable properties to PCL, though the membrane targeting of PC2 likely varies with cell types. Here we show that PC2 expressed heterologously in Xenopus oocytes is targeted to intracellular compartments. By contrast, a truncated form of mouse PC2 corresponding to a naturally occurring human mutation R742X is targeted predominantly to the plasma membrane where it mediates K+, Na+, and Ca2+ currents. Unlike PCL, the truncated form does not display Ca2+ activated transport activities,possibly due to loss of an EF-hand at the C-terminus. We propose that PC2 forms ion channels utilizing structural components which are preserved in the R742X form of the protein. Implications for epithelial cell signaling are discussed. (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/09/20 alle ore 07:08:15