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Titolo:
Evidence for functional role of epsilon PKC isozyme in the regulation of cardiac Na+ channels
Autore:
Xiao, GQ; Qu, YX; Sun, ZQ; Mochly-Rosen, D; Boutjdir, M;
Indirizzi:
Vet Affairs New York Harbor Healthcare Syst, Res & Dev Off 151, Mol & Cellular Cardiol Program, Brooklyn, NY 11209 USA Vet Affairs New York Harbor Healthcare Syst Brooklyn NY USA 11209 209 USA SUNY Hlth Sci Ctr, Brooklyn, NY 11209 USA SUNY Hlth Sci Ctr Brooklyn NY USA 11209 h Sci Ctr, Brooklyn, NY 11209 USA Stanford Univ, Dept Mol Pharmacol, Stanford, CA 94305 USA Stanford Univ Stanford CA USA 94305 Mol Pharmacol, Stanford, CA 94305 USA
Titolo Testata:
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY
fascicolo: 5, volume: 281, anno: 2001,
pagine: C1477 - C1486
SICI:
0363-6143(200111)281:5<C1477:EFFROE>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-KINASE-C; RAT-HEART MYOCYTES; PHORBOL ESTER; NEONATAL RAT; SODIUM-CHANNELS; ION CHANNELS; VENTRICULAR MYOCYTES; ANCHORING PROTEINS; XENOPUS-LAEVIS; ANGIOTENSIN-II;
Keywords:
protein kinase C; two-electrode voltage clamp; peptides; Xenopus oocyte; electrophysiology;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
54
Recensione:
Indirizzi per estratti:
Indirizzo: Boutjdir, M Vet Affairs New York Harbor Healthcare Syst, Res & Dev Off 151, Mol & Cellular Cardiol Program, 800 Poly Pl, Brooklyn, NY 11209 USA Vet Affairs New York Harbor Healthcare Syst 800 Poly Pl Brooklyn NY USA 11209
Citazione:
G.Q. Xiao et al., "Evidence for functional role of epsilon PKC isozyme in the regulation of cardiac Na+ channels", AM J P-CELL, 281(5), 2001, pp. C1477-C1486

Abstract

Investigation of the role of individual protein kinase C (PKC) isozymes inthe regulation of Na+ channels has been largely limited by the lack of isozyme-selective modulators. Here we used a novel peptide-specific activator (epsilon V1-7) of epsilon PKC and other peptide isozyme-specific inhibitorsin addition to the general PKC activator phorbol 12-myristate 13-acetate (PMA) to dissect the role of individual PKCs in the regulation of the human cardiac Na+ channel hH1, heterologously expressed in Xenopus oocytes. Peptides were injected individually or in combination into the oocyte. Whole cell Na+ current (I-Na) was recorded using two-electrode voltage clamp. epsilon V1-7 (100 nM) and PMA (100 nM) inhibited I-Na by 31 +/- 5% and 44 +/- 8% (at -20 mV), respectively. These effects were not seen with the scrambled peptide for epsilon V1-7 (100 nM) or the PMA analog 4 alpha -phorbol 12,13-didecanoate (100 nM). However, epsilon V1-7- and PMA-induced I-Na inhibitionwas abolished by epsilon V1-2, a peptide-specific antagonist of epsilon PKC. Furthermore, PMA-induced I-Na inhibition was not altered by 100 nM peptide-specific inhibitors for alpha-, beta-, delta-, or eta PKC. PMA and epsilon V1-7 induced translocation of ePKC from soluble to particulate fraction in Xenopus oocytes. This translocation was antagonized by epsilon V1-2. In native rat ventricular myocytes, PMA and epsilon V1-7 also inhibited I-Na; this inhibition was antagonized by epsilon V1-2. In conclusion, the resultsprovide evidence for selective regulation of cardiac Na+ channels by epsilon PKC isozyme.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 15:26:32