Polyphosphoinositide Breakdown without Calcium Mobilization: Studies with Adrenal Chromaffin Cells and Retina

  • J. N. Hawthorne
  • F. A. Millar
  • A. M. F. Swilem
  • H. Yagisawa
Conference paper
Part of the FIDIA Research Series book series (FIDIA, volume 4)

Abstract

The polyphosphoinositides (PtdIns4P and PtdIns(4, 5)P 2) have a considerable affinity for divalent cations and many years ago a physiological role in connection with calcium ions was suggested (Hawthorne and Kemp, 1964). In nervous tissue at least, the monoesterase and diesterase enzymes hydrolysing these lipids are much more active than the kinases responsible for their synthesis. The original description of PtdIns4P kinase by Kai et al. (1968) contains the following comment: “It (PtdIns(4, 5)P 2) resembles a transmitter substance in that the capacity for its destruction is very great”.

Keywords

Hydrolysis Nicotine Retina Catecholamine Acetylcholine 

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References

  1. Abdel-Latif AA, Akhtar RA, Hawthorne JN (1977) Biochem J 162: 61–73.PubMedGoogle Scholar
  2. Adnan NAM, Hawthorne JN (1981) J Neurochem 36: 1858–1860.CrossRefGoogle Scholar
  3. Berridge MJ (1983) Biochem J 212: 849–858.PubMedGoogle Scholar
  4. Berridge MJ, Irvine RF (1984) Nature 312: 315–321.PubMedCrossRefGoogle Scholar
  5. Brown SL, Brown JH (1983) Molec Pharmacol 24: 351–356.Google Scholar
  6. Brown JE, Rubin LJ, Ghalayini GJ, Tarver AP, Irvine RF, Berridge MJ, Anderson RE (1984) Nature 311: 160–163.PubMedCrossRefGoogle Scholar
  7. Burgoyne RD (1984) Biochim Biophys Acta 779: 201–216.PubMedCrossRefGoogle Scholar
  8. Cheek TR, Burgoyne RD (1985) Biochim Biophys Acta 846: 167–173.PubMedCrossRefGoogle Scholar
  9. Cockroft S (1981) Trends Pharmac Sci 2: 340–342.CrossRefGoogle Scholar
  10. Dawson RMC (1954) Biochem J 57: 237–245.PubMedGoogle Scholar
  11. Derome G, Tseng R, Mercier P, Lemaire I, Lemaire S (1981) Biochem Pharmacol 30: 855–860.PubMedCrossRefGoogle Scholar
  12. Ellis RB, Galliard T, Hawthorne JN (1963) Biochem J 88: 125–131.PubMedGoogle Scholar
  13. Fein A, Payne R, Corson DW, Berridge MJ, Irvine RF (1984) Nature 311: 157–160.PubMedCrossRefGoogle Scholar
  14. Fesenko EE, Kolesnikov SS, Lyubarsky AL (1985) Nature 313: 310–313.PubMedCrossRefGoogle Scholar
  15. Fisher SK, Holz RW, Agranoff BW (1981) J Neurochem 37: 491–497.PubMedCrossRefGoogle Scholar
  16. Ghalayini A, Anderson RE (1984) Biochem Biophys Res Commun 124: 503–506.PubMedCrossRefGoogle Scholar
  17. Hawthorne JN (1982) Nature 295: 281–282.PubMedCrossRefGoogle Scholar
  18. Hawthorne JN, Kemp P (1964) Adv Lipid Res 2: 127–166.PubMedGoogle Scholar
  19. Hawthorne JN, Pickard MR (1979) J Neurochem 32: 5–14.PubMedCrossRefGoogle Scholar
  20. Hokin MR, Benfey BG, Hokin LE (1958) J Biol Chem 233: 814–817.PubMedGoogle Scholar
  21. Kai M, Salway JG, Hawthorne JN (1968) Biochem J 106: 791–801.PubMedGoogle Scholar
  22. Kao LS, Schneider AS (1985) J Biol Chem 260: 2019–2022.PubMedGoogle Scholar
  23. Kirk CJ, Creba JA, Downes CP, Michell RH (1981) Biochem Soc Trans 9: 377–379.PubMedGoogle Scholar
  24. Knight DE, Baker PF (1983a) FEBS Lett 160: 98–100.PubMedCrossRefGoogle Scholar
  25. Knight DE, Baker PF (1983b) Quart J Exp Physiol 68: 123–143.Google Scholar
  26. Litosch I, Lee HS, Fain JN (1984) Am J Physiol 246: C141–C147.PubMedGoogle Scholar
  27. Michell RH (1975) Biochim Biophys Acta 415: 81–147.PubMedCrossRefGoogle Scholar
  28. Nishizuka Y (1984) Nature 308: 693–698.PubMedCrossRefGoogle Scholar
  29. Swilem AMF, Hawthorne JN (1983) Biochem Pharmacol 32: 3873–3874.PubMedCrossRefGoogle Scholar
  30. Tsien RY (1981) Nature 290: 527–528.PubMedCrossRefGoogle Scholar
  31. Weiss SJ, McKinney JS, Putney Jr JW (1982) Biochem J 206: 555–560.PubMedGoogle Scholar
  32. Whitaker MJ, Irvine RF (1984) Nature 312: 636–639.CrossRefGoogle Scholar
  33. Wilson DB, Bross TE, Hofmann SL, Majerus PW (1984) J Biol Chem 259: 11718–11724.PubMedGoogle Scholar
  34. Yagihara Y, Bleasdale JE, Hawthorne JN (1973) J Neurochem 21: 173–190.PubMedCrossRefGoogle Scholar
  35. Yau KW, Nakatani K (1985) Nature 313: 579–582.PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1986

Authors and Affiliations

  • J. N. Hawthorne
    • 1
  • F. A. Millar
    • 1
  • A. M. F. Swilem
    • 1
  • H. Yagisawa
    • 1
  1. 1.Department of Biochemistry, Queen’s Medical CentreUniversity of Nottingham Medical SchoolNottinghamUK

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