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. 1986 Apr 1;102(4):1459–1463. doi: 10.1083/jcb.102.4.1459

Is a rise in intracellular concentration of free calcium necessary or sufficient for stimulated cytoskeletal-associated actin?

PMCID: PMC2114170  PMID: 3082894

Abstract

The addition of the calcium ionophore A23187 to rabbit neutrophils increases the amount of actin associated with the cytoskeleton regardless of the presence or absence of calcium in the incubation medium. In the presence of extracellular calcium, the effect of A23187 is biphasic with respect to concentration. The action of the ionophore is rapid, transient, and is inhibited by pertussis toxin, hyperosmolarity, and quinacrine. On the other hand, the addition of pertussis toxin or hyperosmolarity has small if any, effect on the rise in intracellular calcium produced by A23187. While quinacrine does not affect the fMet-Leu-Phe-induced increase in cytoskeletal actin and the polyphosphoinositide turnover, its addition inhibits completely the stimulated increase in Ca-influx produced by the same stimulus. The results presented here suggest that a rise in the intracellular concentration of free calcium is neither necessary nor sufficient for the stimulated increase in cytoskeletal-associated actin. A possible relationship between the lipid remodeling stimulated by chemoattractants and the increased cytoskeletal actin is discussed.

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Selected References

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  1. Berridge M. J. Inositol trisphosphate and diacylglycerol as second messengers. Biochem J. 1984 Jun 1;220(2):345–360. doi: 10.1042/bj2200345. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Fechheimer M., Zigmond S. H. Changes in cytoskeletal proteins of polymorphonuclear leukocytes induced by chemotactic peptides. Cell Motil. 1983;3(4):349–361. doi: 10.1002/cm.970030406. [DOI] [PubMed] [Google Scholar]
  3. Fox J. E., Boyles J. K., Reynolds C. C., Phillips D. R. Actin filament content and organization in unstimulated platelets. J Cell Biol. 1984 Jun;98(6):1985–1991. doi: 10.1083/jcb.98.6.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Hirata F., Corcoran B. A., Venkatasubramanian K., Schiffmann E., Axelrod J. Chemoattractants stimulate degradation of methylated phospholipids and release of arachidonic acid in rabbit leukocytes. Proc Natl Acad Sci U S A. 1979 Jun;76(6):2640–2643. doi: 10.1073/pnas.76.6.2640. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Korn E. D. Actin polymerization and its regulation by proteins from nonmuscle cells. Physiol Rev. 1982 Apr;62(2):672–737. doi: 10.1152/physrev.1982.62.2.672. [DOI] [PubMed] [Google Scholar]
  6. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  7. Naccache P. H., Showell H. J., Becker E. L., Sha'afi R. I. Transport of sodium, potassium, and calcium across rabbit polymorphonuclear leukocyte membranes. Effect of chemotactic factor. J Cell Biol. 1977 May;73(2):428–444. doi: 10.1083/jcb.73.2.428. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Phillips D. R., Jennings L. K., Edwards H. H. Identification of membrane proteins mediating the interaction of human platelets. J Cell Biol. 1980 Jul;86(1):77–86. doi: 10.1083/jcb.86.1.77. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Pollard T. D. Functional implications of the biochemical and structural properties of cytoplasmic contractile proteins. Soc Gen Physiol Ser. 1975;30:259–286. [PubMed] [Google Scholar]
  10. Rao K. M., Varani J. Actin polymerization induced by chemotactic peptide and concanavalin A in rat neutrophils. J Immunol. 1982 Oct;129(4):1605–1607. [PubMed] [Google Scholar]
  11. Rink T. J., Sanchez A., Hallam T. J. Diacylglycerol and phorbol ester stimulate secretion without raising cytoplasmic free calcium in human platelets. Nature. 1983 Sep 22;305(5932):317–319. doi: 10.1038/305317a0. [DOI] [PubMed] [Google Scholar]
  12. Sha'afi R. I., White J. R., Molski T. F., Shefcyk J., Volpi M., Naccache P. H., Feinstein M. B. Phorbol 12-myristate 13-acetate activates rabbit neutrophils without an apparent rise in the level of intracellular free calcium. Biochem Biophys Res Commun. 1983 Jul 29;114(2):638–645. doi: 10.1016/0006-291x(83)90828-8. [DOI] [PubMed] [Google Scholar]
  13. Southwick F. S., Stossel T. P. Contractile proteins in leukocyte function. Semin Hematol. 1983 Oct;20(4):305–321. [PubMed] [Google Scholar]
  14. Takenawa T., Homma Y., Nagai Y. Role of Ca2+ in phosphatidylinositol response and arachidonic acid release in formylated tripeptide- or Ca2+ ionophore A23187-stimulated guinea pig neutrophils. J Immunol. 1983 Jun;130(6):2849–2855. [PubMed] [Google Scholar]
  15. Volpi M., Molski T. F., Naccache P. H., Feinstein M. B., Sha'afi R. I. Phorbol 12-myristate, 13-acetate potentiates the action of the calcium ionophore in stimulating arachidonic acid release and production of phosphatidic acid in rabbit neutrophils. Biochem Biophys Res Commun. 1985 Apr 30;128(2):594–600. doi: 10.1016/0006-291x(85)90087-7. [DOI] [PubMed] [Google Scholar]
  16. Volpi M., Yassin R., Naccache P. H., Sha'afi R. I. Chemotactic factor causes rapid decreases in phosphatidylinositol,4,5-bisphosphate and phosphatidylinositol 4-monophosphate in rabbit neutrophils. Biochem Biophys Res Commun. 1983 May 16;112(3):957–964. doi: 10.1016/0006-291x(83)91711-4. [DOI] [PubMed] [Google Scholar]
  17. White J. R., Naccache P. H., Molski T. F., Borgeat P., Sha'afi R. I. Direct demonstration of increased intracellular concentration of free calcium in rabbit and human neutrophils following stimulation by chemotactic factor. Biochem Biophys Res Commun. 1983 May 31;113(1):44–50. doi: 10.1016/0006-291x(83)90429-1. [DOI] [PubMed] [Google Scholar]
  18. White J. R., Naccache P. H., Sha'afi R. I. Stimulation by chemotactic factor of actin association with the cytoskeleton in rabbit neutrophils. Effects of calcium and cytochalasin B. J Biol Chem. 1983 Nov 25;258(22):14041–14047. [PubMed] [Google Scholar]
  19. Yassin R., Shefcyk J., White J. R., Tao W., Volpi M., Molski T. F., Naccache P. H., Feinstein M. B., Sha'afi R. I. Effects of chemotactic factors and other agents on the amounts of actin and a 65,000-mol-wt protein associated with the cytoskeleton of rabbit and human neutrophils. J Cell Biol. 1985 Jul;101(1):182–188. doi: 10.1083/jcb.101.1.182. [DOI] [PMC free article] [PubMed] [Google Scholar]

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