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. 1980 Dec;77(12):7039–7043. doi: 10.1073/pnas.77.12.7039

Calcium-dependent protein kinase: widespread occurrence in various tissues and phyla of the animal kingdom and comparison of effects of phospholipid, calmodulin, and trifluoperazine.

J F Kuo, R G Andersson, B C Wise, L Mackerlova, I Salomonsson, N L Brackett, N Katoh, M Shoji, R W Wrenn
PMCID: PMC350436  PMID: 6938952

Abstract

A widespread occurrence of Ca2+-dependent protein kinase was shown in various tissues and phyla of the animal kingdom. Phosphatidylserine appeared to be more effective than calmodulin in supporting the Ca2+-dependent phosphotransferase activity. The phospholipid-sensitive Ca2+-dependent protein kinase activity, distributed in both the cytosolic and particulate fractions, was not inhibited by trifluoperazine, a specific inhibitor of calmodulin-sensitive, Ca2+-dependent reactions or processes. The enzyme activity levels, compared to those of cyclic AMP-dependent and cyclic GMP-dependent protein kinases, were exceedingly high in certain tissues (such as brain and spleen) and exhibited a much greater disparity among tissues. The Ka for Ca2+ was about 100 microM in the presence of phosphatidylserine; the value was as low as 2 microM in the presence of phosphatidylserine and diolein. It is suggested that phospholipid-sensitive Ca2+-dependent protein kinase may mediate certain actions of Ca2+ in tissues, acting independently or in a complementary manner with other protein phosphorylation systems stimulated by calmodulin-Ca2+, cyclic AMP, or cyclic GMP.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Berridge M. J. The interaction of cyclic nucleotides and calcium in the control of cellular activity. Adv Cyclic Nucleotide Res. 1975;6:1–98. [PubMed] [Google Scholar]
  2. Cheung W. Y. Calmodulin plays a pivotal role in cellular regulation. Science. 1980 Jan 4;207(4426):19–27. doi: 10.1126/science.6243188. [DOI] [PubMed] [Google Scholar]
  3. Cheung W. Y. Cyclic 3',5'-nucleotide phosphodiesterase. Evidence for and properties of a protein activator. J Biol Chem. 1971 May 10;246(9):2859–2869. [PubMed] [Google Scholar]
  4. Cohen P., Burchell A., Foulkes J. G., Cohen P. T., Vanaman T. C., Nairn C. Identification of the Ca2+-dependent modulator protein as the fourth subunit of rabbit skeletal muscle phosphorylase kinase. FEBS Lett. 1978 Aug 15;92(2):287–293. doi: 10.1016/0014-5793(78)80772-8. [DOI] [PubMed] [Google Scholar]
  5. Davis C. W., Kuo J. F. Purification and characterization of guanosine 3':5'-monophosphate-specific phosphodiesterase from guinea pig lung. J Biol Chem. 1977 Jun 25;252(12):4078–4084. [PubMed] [Google Scholar]
  6. DeLorenzo R. J., Freedman S. D., Yohe W. B., Maurer S. C. Stimulation of Ca2+-dependent neurotransmitter release and presynaptic nerve terminal protein phosphorylation by calmodulin and a calmodulin-like protein isolated from synaptic vesicles. Proc Natl Acad Sci U S A. 1979 Apr;76(4):1838–1842. doi: 10.1073/pnas.76.4.1838. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Greengard P. Phosphorylated proteins as physiological effectors. Science. 1978 Jan 13;199(4325):146–152. doi: 10.1126/science.22932. [DOI] [PubMed] [Google Scholar]
  8. Kishimoto A., Takai Y., Mori T., Kikkawa U., Nishizuka Y. Activation of calcium and phospholipid-dependent protein kinase by diacylglycerol, its possible relation to phosphatidylinositol turnover. J Biol Chem. 1980 Mar 25;255(6):2273–2276. [PubMed] [Google Scholar]
  9. Kuo J. F. Changes in relative levels of guanosine-3':5'-monophosphate-dependent and adenosine-3':5'-monophosphate-dependent protein kinases in lung, heart, and brain of developing guinea pigs. Proc Natl Acad Sci U S A. 1975 Jun;72(6):2256–2259. doi: 10.1073/pnas.72.6.2256. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Kuo J. F., Greengard P. Cyclic nucleotide-dependent protein kinases. IV. Widespread occurrence of adenosine 3',5'-monophosphate-dependent protein kinase in various tissues and phyla of the animal kingdom. Proc Natl Acad Sci U S A. 1969 Dec;64(4):1349–1355. doi: 10.1073/pnas.64.4.1349. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Kuo J. F., Greengard P. Cyclic nucleotide-dependent protein kinases. VI. Isolation and partial purification of a protein kinase activated by guanosine 3',5'-monophosphate. J Biol Chem. 1970 May 25;245(10):2493–2498. [PubMed] [Google Scholar]
  12. Kuo J. F. Guanosine 3':5'-monophosphate-dependent protein kinases in mammalian tissues. Proc Natl Acad Sci U S A. 1974 Oct;71(10):4037–4041. doi: 10.1073/pnas.71.10.4037. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Kuo W. N., Kuo J. F. Isolation of stimulatory modulator of guanosine 3':5'-monophosphate-dependent protein kinase from mammalian heart devoid of inhibitory modulator of adenosine 3':5'-monophosphate-dependent protein kinase. J Biol Chem. 1976 Jul 25;251(14):4283–4286. [PubMed] [Google Scholar]
  14. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  15. Mori T., Takai Y., Minakuchi R., Yu B., Nishizuka Y. Inhibitory action of chlorpromazine, dibucaine, and other phospholipid-interacting drugs on calcium-activated, phospholipid-dependent protein kinase. J Biol Chem. 1980 Sep 25;255(18):8378–8380. [PubMed] [Google Scholar]
  16. Pichard A. L., Cheung W. Y. Cyclic 3':5'-nucleotide phosphodiesterase. Stimulation of bovine brain cytoplasmic enzyme by lysophosphatidylcholine. J Biol Chem. 1977 Jul 25;252(14):4872–4875. [PubMed] [Google Scholar]
  17. Schulman H., Greengard P. Ca2+-dependent protein phosphorylation system in membranes from various tissues, and its activation by "calcium-dependent regulator". Proc Natl Acad Sci U S A. 1978 Nov;75(11):5432–5436. doi: 10.1073/pnas.75.11.5432. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Takai Y., Kishimoto A., Iwasa Y., Kawahara Y., Mori T., Nishizuka Y. Calcium-dependent activation of a multifunctional protein kinase by membrane phospholipids. J Biol Chem. 1979 May 25;254(10):3692–3695. [PubMed] [Google Scholar]
  19. Walsh M. P., Vallet B., Autric F., Demaille J. G. Purification and characterization of bovine cardiac calmodulin-dependent myosin light chain kinase. J Biol Chem. 1979 Dec 10;254(23):12136–12144. [PubMed] [Google Scholar]
  20. Weiss B., Levin R. M. Mechanism for selectively inhibiting the activation of cyclic nucleotide phosphodiesterase and adenylate cyclase by antipsychotic agents. Adv Cyclic Nucleotide Res. 1978;9:285–303. [PubMed] [Google Scholar]
  21. Wolff D. J., Brostrom C. O. Calcium-dependent cyclic nucleotide phosphodiesterase from brain identification of phospholipids as calcium-independent activators. Arch Biochem Biophys. 1976 Apr;173(2):720–731. doi: 10.1016/0003-9861(76)90310-6. [DOI] [PubMed] [Google Scholar]
  22. Yamauchi T., Fujisawa H. Activation of tryptophan 5-monooxygenase by calcium-dependent regulator protein. Biochem Biophys Res Commun. 1979 Sep 12;90(1):28–35. doi: 10.1016/0006-291x(79)91585-7. [DOI] [PubMed] [Google Scholar]

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