Abstract
The role of C-kinase in the triggering of the neutrophil oxidase by two stimuli (latex beads and the chemotactic peptide fMet-Leu-Phe), representative of endocytotic and exocytotic routes of activation, were investigated by using experimental agents that activate, or inhibit C-kinase, in intact cells. The activation by the phagocytotic stimulus latex beads was mimicked by C-kinase activators giving the same characteristic lag (20-30s), followed by a constant oxygen consumption rate with the same maximum rate and affinity for oxygen (Km approx. 13 microM), competed with activation by PMA (4 beta-phorbol 12-myristate 13-acetate) in a simple common-target manner, and was inhibited by retinal, an inhibitor shown to inhibit activation by PMA. In contrast, activation by chemotactic peptide was not mimicked by C-kinase activation alone, chemotactic peptide inducing biphasic oxygen consumption with a Km for oxygen of the second prolonged phase of 3.9 microM, did not compete with activation by PMA, and was not inhibited by retinal. However, PMA and retinal produced slight enhancements of activation by chemotactic peptide and production of monophasic oxygen consumption. It was concluded that C-kinase activation plays a simple central transducing role in activation of the oxidase by latex beads, but that its role in activation by chemotactic peptide is a part of a more complex set of interactions that involve other Ca2+-activated and non-Ca2+-activated processes.
Full text
PDF
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Babior B. M., Kipnes R. S., Curnutte J. T. Biological defense mechanisms. The production by leukocytes of superoxide, a potential bactericidal agent. J Clin Invest. 1973 Mar;52(3):741–744. doi: 10.1172/JCI107236. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Campbell A. K., Hallett M. B. Measurement of intracellular calcium ions and oxygen radicals in polymorphonuclear leucocyte-erythrocyte 'ghost' hybrids. J Physiol. 1983 May;338:537–550. doi: 10.1113/jphysiol.1983.sp014688. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cross A. R., Parkinson J. F., Jones O. T. Mechanism of the superoxide-producing oxidase of neutrophils. O2 is necessary for the fast reduction of cytochrome b-245 by NADPH. Biochem J. 1985 Mar 15;226(3):881–884. doi: 10.1042/bj2260881. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Dale M. M., Penfield A. Synergism between phorbol ester and A23187 in superoxide production by neutrophils. FEBS Lett. 1984 Sep 17;175(1):170–172. doi: 10.1016/0014-5793(84)80592-x. [DOI] [PubMed] [Google Scholar]
- Edwards S. W., Hallett M. B., Lloyd D., Campbell A. K. Decrease in apparent Km for oxygen after stimulation of respiration of rat polymorphonuclear leukocytes. FEBS Lett. 1983 Sep 5;161(1):60–64. doi: 10.1016/0014-5793(83)80730-3. [DOI] [PubMed] [Google Scholar]
- Hallett M. B., Campbell A. K. Is intracellular Ca2+ the trigger for oxygen radical production by polymorphonuclear leucocytes? Cell Calcium. 1984 Feb;5(1):1–19. doi: 10.1016/0143-4160(84)90150-7. [DOI] [PubMed] [Google Scholar]
- Hallett M. B., Campbell A. K. Measurement of changes in cytoplasmic free CA2+ in fused cell hybrids. Nature. 1982 Jan 14;295(5845):155–158. doi: 10.1038/295155a0. [DOI] [PubMed] [Google Scholar]
- Hallett M. B., Luzio J. P., Campbell A. K. Stimulation of Ca2+-dependent chemiluminescence in rat polymorphonuclear leucocytes by polystyrene beads and the non-lytic action of complement. Immunology. 1981 Nov;44(3):569–576. [PMC free article] [PubMed] [Google Scholar]
- Huang C. K., Hill J. M., Jr, Bormann B. J., Mackin W. M., Becker E. L. Endogenous substrates for cyclic AMP-dependent and calcium-dependent protein phosphorylation in rabbit peritoneal neutrophils. Biochim Biophys Acta. 1983 Oct 4;760(1):126–135. doi: 10.1016/0304-4165(83)90133-2. [DOI] [PubMed] [Google Scholar]
- Kajikawa N., Kaibuchi K., Matsubara T., Kikkawa U., Takai Y., Nishizuka Y., Itoh K., Tomioka C. A possible role of protein kinase C in signal-induced lysosomal enzyme release. Biochem Biophys Res Commun. 1983 Oct 31;116(2):743–750. doi: 10.1016/0006-291x(83)90587-9. [DOI] [PubMed] [Google Scholar]
- Lew P. D., Wollheim C. B., Waldvogel F. A., Pozzan T. Modulation of cytosolic-free calcium transients by changes in intracellular calcium-buffering capacity: correlation with exocytosis and O2-production in human neutrophils. J Cell Biol. 1984 Oct;99(4 Pt 1):1212–1220. doi: 10.1083/jcb.99.4.1212. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Miyake R., Tanaka Y., Tsuda T., Kaibuchi K., Kikkawa U., Nishizuka Y. Activation of protein kinase C by non-phorbol tumor promoter, mezerein. Biochem Biophys Res Commun. 1984 Jun 15;121(2):649–656. doi: 10.1016/0006-291x(84)90231-6. [DOI] [PubMed] [Google Scholar]
- Mori T., Takai Y., Yu B., Takahashi J., Nishizuka Y., Fujikura T. Specificity of the fatty acyl moieties of diacylglycerol for the activation of calcium-activated, phospholipid-dependent protein kinase. J Biochem. 1982 Feb;91(2):427–431. doi: 10.1093/oxfordjournals.jbchem.a133714. [DOI] [PubMed] [Google Scholar]
- Nishizuka Y. The role of protein kinase C in cell surface signal transduction and tumour promotion. Nature. 1984 Apr 19;308(5961):693–698. doi: 10.1038/308693a0. [DOI] [PubMed] [Google Scholar]
- Taffet S. M., Greenfield A. R., Haddox M. K. Retinal inhibits TPA activated, calcium-dependent, phospholipid-dependent protein kinase ("C" kinase). Biochem Biophys Res Commun. 1983 Aug 12;114(3):1194–1199. doi: 10.1016/0006-291x(83)90689-7. [DOI] [PubMed] [Google Scholar]