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Protein Kinase C: Structure, Function And Modulation Of Its Catalytic Activity By Physiological And Pharmacological Agents

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Abstract

Extracellular agonist-cell surface receptor cell activation pathways can be mediated through the second messengers diacylglycerol and inositol-triphosphate which in turn can activate PKC kinase activity directly in the former case and indirectly in the latter by release of internally stored calcium. The initial steps of physiological cell activation processes are often of a transient nature and hence there have to be mechanisms for turning off the activation process. Several mechanisms of deactivation have been elucidated such as the metabolism of DAG to either phosphatidic acid (re-generation of phosphatidylinositol path) or further catabolism to monoacyl-glycerol and glycerol thereby generating fatty acids such as arachidonic acid, which can be further metabolized to a series of potent biological effectors, the prostaglandins. Inositol-1,4,5-triphosphate (IP3) is also normally a transient message being further phosphorylated to IP4 and IP5 and IP6 or being dephosphorylated to IP2, IP1, and inositol (regeneration of phosphatidylinositol path) (for reviews see Nishizuka, 1984, 1986; Berridge, 1987).

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© 1988 Plenum Press, New York

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Mahoney, C.W., Azzi, A. (1988). Protein Kinase C: Structure, Function And Modulation Of Its Catalytic Activity By Physiological And Pharmacological Agents. In: Cañedo, L.E., Todd, L.E., Packer, L., Jaz, J. (eds) Cell Function and Disease. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0813-3_11

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  • DOI: https://doi.org/10.1007/978-1-4613-0813-3_11

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4612-8095-8

  • Online ISBN: 978-1-4613-0813-3

  • eBook Packages: Springer Book Archive

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