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Signalling by protein kinase C isoforms in the heart

  • Chapter
Biochemistry of Signal Transduction in Myocardium

Part of the book series: Developments in Molecular and Cellular Biochemistry ((DMCB,volume 17))

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 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 (CI) 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.

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  1. Laboratoire de Physiopathologie Cardiovasculaire, INSERM U-390, Hopital A. de Villeneuve, 371 avenue du doyen Giraud, 34295, Montpellier, France

    Michel Pucéat & Guy Vassort

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  1. Michel Pucéat
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  2. Guy Vassort
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  1. Department of Biochemistry, Cardiovascular Research Institute COEUR, Faculty of Medicine of Health Science, Erasmus University Rotterdam, P.O. Box 1738, 3300 DR, Rotterdam, The Netherlands

    Jos M. J. Lamers

  2. Department of Cardiology, Cardiovascular Research Institute COEUR, Erasmus University Rotterdam, P.O. Box 1738, 3300 DR, Rotterdam, The Netherlands

    Pieter D. Verdouw

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Pucéat, M., Vassort, G. (1996). Signalling by protein kinase C isoforms in the heart. In: Lamers, J.M.J., Verdouw, P.D. (eds) Biochemistry of Signal Transduction in Myocardium. Developments in Molecular and Cellular Biochemistry, vol 17. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1275-8_8

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