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Titolo:
SIGNALING BY PROTEIN-KINASE-C ISOFORMS IN THE HEART
Autore:
PUCEAT M; VASSORT G;
Indirizzi:
HOP A DE VILLENEUVE,INSERM U390,LAB PHYSIOPATHOL CARDIOVASC,371 AVE DOYEN GIRAUD F-34295 MONTPELLIER FRANCE
Titolo Testata:
Molecular and cellular biochemistry
fascicolo: 1-2, volume: 157, anno: 1996,
pagine: 65 - 72
SICI:
0300-8177(1996)157:1-2<65:SBPIIT>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
RAT VENTRICULAR MYOCYTES; CARDIAC SARCOPLASMIC-RETICULUM; MYOSIN LIGHT CHAIN-2; PHORBOL ESTER; TROPONIN-I; XENOPUS OOCYTES; ACTOMYOSIN MGATPASE; MYOCARDIAL-ISCHEMIA; CHLORIDE CURRENT; PHOSPHOLIPASE-C;
Keywords:
PKC ISOFORMS; CARDIOMYOCYTES; HYPERTROPHY; PROTEIN PHOSPHORYLATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
91
Recensione:
Indirizzi per estratti:
Citazione:
M. Puceat e G. Vassort, "SIGNALING BY PROTEIN-KINASE-C ISOFORMS IN THE HEART", Molecular and cellular biochemistry, 157(1-2), 1996, pp. 65-72

Abstract

Understanding transmembrane signalling process is one of the major challenge of the decade. In most tissues, since Fisher and Krebs's discovery in the 1950's, protein phosphorylation has been widely recognizedas a key event of this cellular function. Indeed, binding of hormonesor neurotransmitters to specific membrane receptors leads to the generation of cytosoluble second messengers which in turn activate a specific protein kinase. Numerous protein kinases have been so far identified and roughly classified into two groups, namely serine/threonine andtyrosine kinases on the basis of the target amino acid although some more recently discovered kinases like MEK (or MAP kinase kinase) phosphorylate both serine and tyrosine residues. Protein kinase C is a serine/threonine kinase that was first described by Takai et al. [1] as a Ca- and phospholipid-dependent protein kinase. Later on, Kuo et al. [2] found that PKC was expressed in most tissues including the heart. The field of investigation became more complicated when it was found that the kinase is not a single molecular entity and that several isoforms exist. At present, 12 PKC isoforms and other PKC-related kinases [3]were identified in mammalian tissues. These are classified into threegroups. (1) the Ca-activated alpha-, beta-, and gamma-PKCs which display a Ca-binding site (C2); (2) the Ca-insensitive delta-, epsilon-, theta-, eta-, and mu-PKCs. The kinases that belong to both of these groups display two cystein-rich domains (C1) which bind phorbol esters (for recent review on PKC structure, see [4]). (3) The third group was named atypical PKCs and include zeta, lambda, and tau-PKCs that lack both the C2 and one cystein-rich domain. Consequently, these isoforms are Ca-insensitive and cannot be activated by phorbol esters [5]. In theheart, evidence that multiple PKC isoforms exist was first provided by Kosaka et al. [6] who identified by chromatography at least two PKC-related isoenzymes. Numerous studies were thus devoted to the biochemical characterization of these isoenzymes (see [7] for review on cardiac PKCs) as well as to the identification of their substrates. This overview aims at updating the present knowledge on the expression, activation and functions of PKC isoforms in cardiac cells.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 11:01:26