Skip to main content
PMC home page
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1986 Dec 1;103(6):2707–2714. doi: 10.1083/jcb.103.6.2707

An actin-nucleating activity in polymorphonuclear leukocytes is modulated by chemotactic peptides

PMCID: PMC2114615  PMID: 3793753

Abstract

We examined the actin-nucleating activity in polymorphonuclear leukocyte lysates prepared at various times after chemotactic peptide addition. The actin nucleation increases two- to threefold within 15 s after peptide addition, decays to basal levels within 90 s, and is largely independent of cytoplasmic calcium fluxes. The peptide-induced nucleation sites behave as free barbed ends and therefore may increase the level of polymerized actin in vivo. The new nucleation sites may also determine the cellular sites of actin polymerization. This localization of actin polymerization could be important for the directional extension of lamellipodia during chemotaxis.

Full Text

The Full Text of this article is available as a PDF (777.2 KB).

Selected References

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

  1. Amrein P. C., Stossel T. P. Prevention of degradation of human polymorphonuclear leukocyte proteins by diisopropylfluorophosphate. Blood. 1980 Sep;56(3):442–447. [PubMed] [Google Scholar]
  2. Bradford P. G., Rubin R. P. Characterization of formylmethionyl-leucyl-phenylalanine stimulation of inositol trisphosphate accumulation in rabbit neutrophils. Mol Pharmacol. 1985 Jan;27(1):74–78. [PubMed] [Google Scholar]
  3. Brown S. S., Spudich J. A. Cytochalasin inhibits the rate of elongation of actin filament fragments. J Cell Biol. 1979 Dec;83(3):657–662. doi: 10.1083/jcb.83.3.657. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Burgess D. R., Schroeder T. E. Polarized bundles of actin filaments within microvilli of fertilized sea urchin eggs. J Cell Biol. 1977 Sep;74(3):1032–1037. doi: 10.1083/jcb.74.3.1032. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Carlsson L., Nyström L. E., Sundkvist I., Markey F., Lindberg U. Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells. J Mol Biol. 1977 Sep 25;115(3):465–483. doi: 10.1016/0022-2836(77)90166-8. [DOI] [PubMed] [Google Scholar]
  6. Cooper J. A., Pollard T. D. Methods to measure actin polymerization. Methods Enzymol. 1982;85(Pt B):182–210. doi: 10.1016/0076-6879(82)85021-0. [DOI] [PubMed] [Google Scholar]
  7. Cooper J. A., Walker S. B., Pollard T. D. Pyrene actin: documentation of the validity of a sensitive assay for actin polymerization. J Muscle Res Cell Motil. 1983 Apr;4(2):253–262. doi: 10.1007/BF00712034. [DOI] [PubMed] [Google Scholar]
  8. Di Virgilio F., Lew D. P., Pozzan T. Protein kinase C activation of physiological processes in human neutrophils at vanishingly small cytosolic Ca2+ levels. Nature. 1984 Aug 23;310(5979):691–693. doi: 10.1038/310691a0. [DOI] [PubMed] [Google Scholar]
  9. 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]
  10. Fox J. E., Phillips D. R. Inhibition of actin polymerization in blood platelets by cytochalasins. Nature. 1981 Aug 13;292(5824):650–652. doi: 10.1038/292650a0. [DOI] [PubMed] [Google Scholar]
  11. Howard T. H., Meyer W. H. Chemotactic peptide modulation of actin assembly and locomotion in neutrophils. J Cell Biol. 1984 Apr;98(4):1265–1271. doi: 10.1083/jcb.98.4.1265. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Howard T. H., Oresajo C. O. The kinetics of chemotactic peptide-induced change in F-actin content, F-actin distribution, and the shape of neutrophils. J Cell Biol. 1985 Sep;101(3):1078–1085. doi: 10.1083/jcb.101.3.1078. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. 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]
  14. Kouyama T., Mihashi K. Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin. Eur J Biochem. 1981;114(1):33–38. [PubMed] [Google Scholar]
  15. Kurth M. C., Wang L. L., Dingus J., Bryan J. Purification and characterization of a gelsolin-actin complex from human platelets. Evidence for Ca2+-insensitive functions. J Biol Chem. 1983 Sep 25;258(18):10895–10903. [PubMed] [Google Scholar]
  16. Lassing I., Lindberg U. Specific interaction between phosphatidylinositol 4,5-bisphosphate and profilactin. Nature. 1985 Apr 4;314(6010):472–474. doi: 10.1038/314472a0. [DOI] [PubMed] [Google Scholar]
  17. MacLean-Fletcher S., Pollard T. D. Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association. Biochem Biophys Res Commun. 1980 Sep 16;96(1):18–27. doi: 10.1016/0006-291x(80)91175-4. [DOI] [PubMed] [Google Scholar]
  18. MacLean-Fletcher S., Pollard T. D. Mechanism of action of cytochalasin B on actin. Cell. 1980 Jun;20(2):329–341. doi: 10.1016/0092-8674(80)90619-4. [DOI] [PubMed] [Google Scholar]
  19. Murray J. M., Weber A., Knox M. K. Myosin subfragment 1 binding to relaxed actin filaments and steric model of relaxation. Biochemistry. 1981 Feb 3;20(3):641–649. doi: 10.1021/bi00506a030. [DOI] [PubMed] [Google Scholar]
  20. Pozzan T., Lew D. P., Wollheim C. B., Tsien R. Y. Is cytosolic ionized calcium regulating neutrophil activation? Science. 1983 Sep 30;221(4618):1413–1415. doi: 10.1126/science.6310757. [DOI] [PubMed] [Google Scholar]
  21. 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]
  22. Schiffmann E. Leukocyte chemotaxis. Annu Rev Physiol. 1982;44:553–568. doi: 10.1146/annurev.ph.44.030182.003005. [DOI] [PubMed] [Google Scholar]
  23. Selden L. A., Estes J. E., Gershman L. C. The tightly bound divalent cation regulates actin polymerization. Biochem Biophys Res Commun. 1983 Oct 31;116(2):478–485. doi: 10.1016/0006-291x(83)90548-x. [DOI] [PubMed] [Google Scholar]
  24. Sha'afi R. I., Shefcyk J., Yassin R., Molski T. F., Volpi M., Naccache P. H., White J. R., Feinstein M. B., Becker E. L. Is a rise in intracellular concentration of free calcium necessary or sufficient for stimulated cytoskeletal-associated actin? J Cell Biol. 1986 Apr;102(4):1459–1463. doi: 10.1083/jcb.102.4.1459. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Sklar L. A., Omann G. M., Painter R. G. Relationship of actin polymerization and depolymerization to light scattering in human neutrophils: dependence on receptor occupancy and intracellular Ca++. J Cell Biol. 1985 Sep;101(3):1161–1166. doi: 10.1083/jcb.101.3.1161. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Slonczewski J. L., Wilde M. W., Zigmond S. H. Phosphorylase a activity as an indicator of neutrophil activation by chemotactic peptide. J Cell Biol. 1985 Oct;101(4):1191–1197. doi: 10.1083/jcb.101.4.1191. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Smith C. D., Lane B. C., Kusaka I., Verghese M. W., Snyderman R. Chemoattractant receptor-induced hydrolysis of phosphatidylinositol 4,5-bisphosphate in human polymorphonuclear leukocyte membranes. Requirement for a guanine nucleotide regulatory protein. J Biol Chem. 1985 May 25;260(10):5875–5878. [PubMed] [Google Scholar]
  28. Southwick F. S., Stossel T. P. Contractile proteins in leukocyte function. Semin Hematol. 1983 Oct;20(4):305–321. [PubMed] [Google Scholar]
  29. Spudich J. A., Watt S. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J Biol Chem. 1971 Aug 10;246(15):4866–4871. [PubMed] [Google Scholar]
  30. Tilney L. G., Bonder E. M., Coluccio L. M., Mooseker M. S. Actin from Thyone sperm assembles on only one end of an actin filament: a behavior regulated by profilin. J Cell Biol. 1983 Jul;97(1):112–124. doi: 10.1083/jcb.97.1.112. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Tilney L. G., Hatano S., Ishikawa H., Mooseker M. S. The polymerization of actin: its role in the generation of the acrosomal process of certain echinoderm sperm. J Cell Biol. 1973 Oct;59(1):109–126. doi: 10.1083/jcb.59.1.109. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Tobacman L. S., Korn E. D. The regulation of actin polymerization and the inhibition of monomeric actin ATPase activity by Acanthamoeba profilin. J Biol Chem. 1982 Apr 25;257(8):4166–4170. [PubMed] [Google Scholar]
  33. Wallace P. J., Wersto R. P., Packman C. H., Lichtman M. A. Chemotactic peptide-induced changes in neutrophil actin conformation. J Cell Biol. 1984 Sep;99(3):1060–1065. doi: 10.1083/jcb.99.3.1060. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Walsh T. P., Weber A., Davis K., Bonder E., Mooseker M. Calcium dependence of villin-induced actin depolymerization. Biochemistry. 1984 Dec 4;23(25):6099–6102. doi: 10.1021/bi00320a030. [DOI] [PubMed] [Google Scholar]
  35. 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]
  36. 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]
  37. Yin H. L., Stossel T. P. Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium-dependent regulatory protein. Nature. 1979 Oct 18;281(5732):583–586. doi: 10.1038/281583a0. [DOI] [PubMed] [Google Scholar]
  38. Zigmond S. H., Sullivan S. J. Sensory adaptation of leukocytes to chemotactic peptides. J Cell Biol. 1979 Aug;82(2):517–527. doi: 10.1083/jcb.82.2.517. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES