Advertisement

Cell and Tissue Research

, Volume 255, Issue 3, pp 553–557 | Cite as

Prostaglandins may play a signal-coupling role during phagocytosis in Amoeba proteus

  • Robert D. Prusch
  • Stella-Maris Goette
  • Paula Haberman
Article

Summary

Phagocytosis in Amoeba proteus can be induced with prostaglandins (PG). In addition, arachidonic acid (the fatty acid precursor to the PG-2 series) also induces phagocytosis. The induction of phagocytosis with arachidonic acid can be partially inhibited by the cyclooxygenase inhibitor indomethacin. Phagocytosis in the amoeba can also be induced with the chemotactic peptide N-formylmethionyl-leucylphenylalanine (NFMLP). The peptide presumably induces phagocytosis by interacting with receptors on the amoeba surface, which may initiate the release of arachidonic acid from membrane lipids. NFMLP-induced phagocytosis can also be partially inhibited by indomethacin. It is suggested that PG's or biochemically related substances may play a signal-coupling role during phagocytosis in the amoeba.

Key words

Phagocytosis Prostaglandins Amoeba proteus (Protozoa) 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Bareis DL, Hirata F, Schiffmann E, Axelrod J (1982) Phospholipid metabolism, calcium flux, and the receptor-mediated induction of chemotaxis in rabbit neutrophils. J Cell Biol 93:690–697Google Scholar
  2. Borman BJ, Huang C-K, Mackin WM, Becker EL (1984) Receptor-mediated activation of phospholipase A2 in rabbit neutrophil membrane. Proc Nat Acad Sci USA 81:767–770Google Scholar
  3. Christiansen RG, Marshall JM (1965) A study of phagocytosis in the amoeba Chaos chaos. J Cell Biol 254:443–457Google Scholar
  4. Flower RJ (1974) Drugs which inhibit prostaglandin biosynthesis. Pharamacol Rev 26:33–67Google Scholar
  5. Garcia Gil M, Alonso F, Alvarez Chiva V, Sanchez Crespo M, Mato JM (1982) Phospholipid turnover during phagocytosis in human polymorphonuclear leukocytes. Biochem J 206:67–72Google Scholar
  6. Leid RW, McConnell LA (1983) PGE2 generation and release by the larval stage of the cestode, Taenai taeniaeformis. Prostaglandins Leukotrienes Med 1:317–323Google Scholar
  7. Morse DE, Kayne M, Tidyman M, Anderson S (1978) Capacity for biosynthesis of prostaglandin-related compounds: distribution and properties of the rate-limiting enzyme in hydrocorals, gorgonians, and other coelenterates of the Caribbean and Pacific. Biol Bull 154:440–452Google Scholar
  8. Naccache PH, Sha'afi RI, Borgeat P, Goetzl EJ (1981) Monoand dihydroxyeicosatetraenoic acids alter calcium homeostasis in rabbit neutrophils. J Clin Invest 67:1584–1587Google Scholar
  9. Prescott DM, James TW (1955) Culturing Amoeba proteus on Tetrahymena. Exp Cell Res 8:256–258Google Scholar
  10. Prusch RD (1980) Endocytotic sucrose uptake in Amoeba proteus induced with the calcium ionophore A23187. Science 209:691–692Google Scholar
  11. Prusch RD (1986) Calcium and the initial surface binding phase of pinocytosis in Amoeba proteus. Am J Physiol 251:C153-C158Google Scholar
  12. Prusch RD, Britton JC (1987) Peptide stimulation of phagocytosis in Amoeba proteus. Cell Tissue Res 250:589–593Google Scholar
  13. Prusch RD, Hannafin J (1979) Sucrose uptake by pinocytosis in Amoeba proteus and the influence of external calcium. J Gen Physiol 74:523–535Google Scholar
  14. Prusch RD, Minck DR (1985) Chemical stimulation of phagocytosis in Amoeba proteus and the influence of external calcium. Cell Tissue Res 242:557–564Google Scholar
  15. Prusch RD, Vedovatti PA (1989) Calcium movements associated with peptide induced phagocytosis in Amoeba proteus. submitted for publicationGoogle Scholar
  16. Sha'afi RI, Naccache PH, Alobaidi T, Molski TFP, Volpi M (1980) Effect of arachidonic acid and the chemotactic factor f-Met-Leu-Phe on cation transport in rabbit neutrophils. J Cell Physiol 106:215–223Google Scholar
  17. Sha'afi RI, Volpi M, Naccache PH (1985) Differences between the effects of f-Met-Leu-Phe and leukotriene B4 on phosphoinositide turnover and their relationship to calcium mobilization and protein kinase C activation. In: Prostaglandins, Leukotrienes, and Lipoxins: Biochemistry, Mechanism of Action, and Clinical Applications, ed. JM Bailey, Plenum Press, NY, pp 241–150Google Scholar
  18. Siegel MI, McConnell RT, Porter NA, Selph JL, Truax JF, Vinegar R, Cuatrecasas P (1980) Aspirin-like drugs inhibit arachidonic acid metabolism via lipoxygenase and cyclooxygenase in rat neutrophils from carrageenan pleural exudates. Biochem Biophys Res Commun 92:688–695Google Scholar
  19. Stockem W, Hoffman HU, Gruber B (1983) Dynamics of the cytoskeleton in Amoeba proteus. I. Redistribution of micro-injected fluorescein-labeled actin during locomotion, immobilization and phagocytosis. Cell Tissue Res 232:79–96Google Scholar
  20. Taylor DL, Blinks JR, Reynolds G (1980) Contractile basis of ameboid movement. VII. Aequorin luminescence during ameboid movement, endocytosis, and capping. J Cell Biol 86:599–607Google Scholar
  21. Valone FH (1984) Regulation of human leukocyte function by lipoxygenase products of arachidonic acid. Cont Topics Immunobiol 14:155–170Google Scholar

Copyright information

© Springer-Verlag 1989

Authors and Affiliations

  • Robert D. Prusch
    • 1
  • Stella-Maris Goette
    • 2
  • Paula Haberman
    • 3
  1. 1.Department of Life SciencesGonzaga UniversitySpokaneUSA
  2. 2.Department of Biological SciencesStanford UniversityStanfordUSA
  3. 3.University of Washington, School of MedicineSeattleUSA

Personalised recommendations