caa a22 4500 477120059 CHVBK 20180405111634.0 cr unu---uuuuu 170330e19960401xx s 000 0 eng 10.1007/BF00227882 doi (NATIONALLICENCE)springer-10.1007/BF00227882 Signalling by protein kinase C isoforms in the heart [Elektronische Daten] [Michel Pucéat, Guy Vassort] 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 recognized as a key event of this cellular function. Indeed, binding of hormones or 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 and tyrosine 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 three groups. (1) the Ca-activated α-, β-,and γ-PKCs which display a Ca-binding site (C2); (2) the Ca-insensitive δ-, ε-, θ-, η-, and μ-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 ζ, λ, and τ-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 the heart. 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. (Mol Cell Biochem 157: 65-72, 1996) Kluwer Academic Publishers, 1996 PKC isoforms nationallicence cardiomyocytes nationallicence hypertrophy nationallicence protein phosphorylation nationallicence Pucéat Michel Laboratoire de Physiopathologic cardiovasculaire, INSERM U-390, Hopital A. de Villeneuve, 371 avenue du doyen Giraud, 34295, Montpellier, France aut Vassort Guy Laboratoire de Physiopathologic cardiovasculaire, INSERM U-390, Hopital A. de Villeneuve, 371 avenue du doyen Giraud, 34295, Montpellier, France aut Molecular and Cellular Biochemistry Kluwer Academic Publishers 157/1-2(1996-04-01), 65-72 0300-8177 157:1-2<65 1996 157 11010 https://doi.org/10.1007/BF00227882 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00227882 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Pucéat Michel Laboratoire de Physiopathologic cardiovasculaire, INSERM U-390, Hopital A. de Villeneuve, 371 avenue du doyen Giraud, 34295, Montpellier, France aut NATIONALLICENCE 700 1- Vassort Guy Laboratoire de Physiopathologic cardiovasculaire, INSERM U-390, Hopital A. de Villeneuve, 371 avenue du doyen Giraud, 34295, Montpellier, France aut NATIONALLICENCE 773 0- Molecular and Cellular Biochemistry Kluwer Academic Publishers 157/1-2(1996-04-01), 65-72 0300-8177 157:1-2<65 1996 157 11010 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer