The Control and Function of Inositide-Metabolizing Enzymes

  • R. F. Irvine
  • A. J. Letcher
  • D. J. Lander
  • R. M. C. Dawson
Conference paper
Part of the FIDIA Research Series book series (FIDIA, volume 4)


Recent advances in our understanding of the role of inositides in intracellular signalling (Michell et al., 1981; Berridge, 1984a; Berridge and Irvine, 1984) have highlighted the need to understand the mechanisms by which the cellular levels of inositides, and hence indirectly of the second messengers generated from them, are controlled. A stimulation of PtdInsP 2 phosphodiesterase is the likely initial event occurring after cell activation by a large number of agonists (Fig. 1). As a result of phosphodiesteratic cleavage of PtdInsP 2 the two second messengers, diacylglycerol (Nishizuka, 1984) and InsP 3 (Berridge, 1984a; Berridge and Irvine, 1984), are formed. The former activates protein kinase C (Nishizuka, 1984) and the latter primarily mobilizes intracellular calcium (Berridge and Irvine, 1984), and these two pathways frequently, but not always (Labarca et al., 1984; Danthurluri and Deth, 1984), act synergistically to produce a final cell activation (Kaibuchi et al., 1984; Rink et al., 1983; Putney et al., 1984). Although the acute control of the levels of these intracellular messengers lies in the regulation of PtdInsP 2 phosphodiesterase activity, the regulation of diacylglycerol and InsP 3 over the longer term (after the first few seconds of stimulation) lies in the hands of the enzymes which generate PtdInsP 2, and those which degrade diacylglycerol and InsP 3. It is the possible mechanism for regulation of these enzymes which are discussed here.


Diacylglycerol Lipase Phosphatidate Phosphohydrolase Acute Control PtdIns Kinase Diacylglycerol Level 
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Copyright information

© Springer-Verlag Berlin Heidelberg 1986

Authors and Affiliations

  • R. F. Irvine
    • 1
  • A. J. Letcher
    • 1
  • D. J. Lander
    • 1
  • R. M. C. Dawson
    • 1
  1. 1.Department of BiochemistryAFRC Institute of Animal PhysiologyBabraham, CambridgeUK

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