Skip to main content
NCBI home page
Immunology logoLink to Immunology
. 1991 Jun;73(2):205–211.

Modulation of phagocytic function in murine peritoneal macrophages by bombesin, gastrin-releasing peptide and neuromedin C.

M De la Fuente 1, M Del Rio 1, M D Ferrandez 1, A Hernanz 1
PMCID: PMC1384466  PMID: 1649124

Abstract

Bombesin, as well as the two mammalian bombesin-like peptides gastrin-releasing peptide and neuromedin C, have been shown in this study to stimulate in vitro all steps of the phagocytic process in murine peritoneal macrophages: adherence to substrate, chemotaxis, ingestion of cells (Candida albicans) and inert particles (latex beads), and production of superoxide anion as measured by nitroblue tetrazolium reduction. A dose-response relationship was observed, with maximal stimulation of phagocytic process between 10(-12)M and 10(-9)M. Gastrin-releasing peptide (GRP) and neuromedin C caused a higher activation of adherence, chemotaxis and ingestion of C. albicans than bombesin. The three neuropeptides induced in murine macrophages a significant, but transient, increase of inositol 1,4,5-trisphosphate (IP3) levels at 60 seconds. On the contrary, these neuropeptides produced a rapid, transient and significant decrease of cAMP at 30 seconds. These results suggest that there are close relations between IP3 and cAMP messenger systems and the phagocytic process in murine peritoneal macrophages when these cells are incubated in the presence of bombesin, GRP or neuromedin C.

Full text

PDF
205

Selected References

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

  1. Anastasi A., Erspamer V., Bucci M. Isolation and structure of bombesin and alytesin, 2 analogous active peptides from the skin of the European amphibians Bombina and Alytes. Experientia. 1971 Feb 15;27(2):166–167. doi: 10.1007/BF02145873. [DOI] [PubMed] [Google Scholar]
  2. BOYDEN S. The chemotactic effect of mixtures of antibody and antigen on polymorphonuclear leucocytes. J Exp Med. 1962 Mar 1;115:453–466. doi: 10.1084/jem.115.3.453. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bagasra O., Howeedy A., Kajdacsy-Balla A. Macrophage function in chronic experimental alcoholism. I. Modulation of surface receptors and phagocytosis. Immunology. 1988 Nov;65(3):405–409. [PMC free article] [PubMed] [Google Scholar]
  4. Cook S. J., Palmer S., Plevin R., Wakelam M. J. Mass measurement of inositol 1,4,5-trisphosphate and sn-1,2-diacylglycerol in bombesin-stimulated Swiss 3T3 mouse fibroblasts. Biochem J. 1990 Jan 15;265(2):617–620. doi: 10.1042/bj2650617. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. De La Fuente M. Changes in the macrophage function with aging. Comp Biochem Physiol A Comp Physiol. 1985;81(4):935–938. doi: 10.1016/0300-9629(85)90933-8. [DOI] [PubMed] [Google Scholar]
  6. Doherty D. E., Haslett C., Tonnesen M. G., Henson P. M. Human monocyte adherence: a primary effect of chemotactic factors on the monocyte to stimulate adherence to human endothelium. J Immunol. 1987 Mar 15;138(6):1762–1771. [PubMed] [Google Scholar]
  7. Fink R., Ehrhardt R., Dancygier H. Bombesin and its analogues inhibit interleukin-2-induced proliferation of CTLL-2 cells. Regul Pept. 1988 Dec;23(3):323–330. doi: 10.1016/0167-0115(88)90233-9. [DOI] [PubMed] [Google Scholar]
  8. Fällman M., Lew D. P., Stendahl O., Andersson T. Receptor-mediated phagocytosis in human neutrophils is associated with increased formation of inositol phosphates and diacylglycerol. Elevation in cytosolic free calcium and formation of inositol phosphates can be dissociated from accumulation of diacylglycerol. J Clin Invest. 1989 Sep;84(3):886–891. doi: 10.1172/JCI114249. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Goldman R., Bar-Shavit Z., Romeo D. Neurotensin modulates human neutrophil locomotion and phagocytic capability. FEBS Lett. 1983 Aug 8;159(1-2):63–67. doi: 10.1016/0014-5793(83)80417-7. [DOI] [PubMed] [Google Scholar]
  10. Hatch G. E., Nichols W. K., Hill H. R. Cyclic nucleotide changes in human neutrophils induced by chemoattractants and chemotactic modulators. J Immunol. 1977 Aug;119(2):450–456. [PubMed] [Google Scholar]
  11. Hernanz A. Characterization and distribution of bombesin-like peptides in the rat brain and gastrointestinal tract. Biochem Cell Biol. 1990 Sep;68(9):1142–1145. doi: 10.1139/o90-170. [DOI] [PubMed] [Google Scholar]
  12. Jensen R. T., Moody T., Pert C., Rivier J. E., Gardner J. D. Interaction of bombesin and litorin with specific membrane receptors on pancreatic acinar cells. Proc Natl Acad Sci U S A. 1978 Dec;75(12):6139–6143. doi: 10.1073/pnas.75.12.6139. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Krco C. J., Gores A., Go V. L. Gastrointestinal regulatory peptides modulate mouse lymphocyte functions under serum-free conditions in vitro. Immunol Invest. 1986 Apr;15(2):103–111. doi: 10.3109/08820138609094136. [DOI] [PubMed] [Google Scholar]
  14. Marasco W. A., Showell H. J., Becker E. L. Substance P binds to the formylpeptide chemotaxis receptor on the rabbit neutrophil. Biochem Biophys Res Commun. 1981 Apr 30;99(4):1065–1072. doi: 10.1016/0006-291x(81)90727-0. [DOI] [PubMed] [Google Scholar]
  15. McDonald T. J., Jörnvall H., Nilsson G., Vagne M., Ghatei M., Bloom S. R., Mutt V. Characterization of a gastrin releasing peptide from porcine non-antral gastric tissue. Biochem Biophys Res Commun. 1979 Sep 12;90(1):227–233. doi: 10.1016/0006-291x(79)91614-0. [DOI] [PubMed] [Google Scholar]
  16. Minamino N., Kangawa K., Matsuo H. Neuromedin C: a bombesin-like peptide identified in porcine spinal cord. Biochem Biophys Res Commun. 1984 Feb 29;119(1):14–20. doi: 10.1016/0006-291x(84)91611-5. [DOI] [PubMed] [Google Scholar]
  17. Moody T. W., Kris R. M., Fiskum G., Linden C. D., Berg M., Schlessinger J. Characterization of receptors for bombesin/gastrin-releasing peptide in human and murine cells. Methods Enzymol. 1989;168:481–493. doi: 10.1016/0076-6879(89)68037-8. [DOI] [PubMed] [Google Scholar]
  18. Moore T. C. Modification of lymphocyte traffic by vasoactive neurotransmitter substances. Immunology. 1984 Jul;52(3):511–518. [PMC free article] [PubMed] [Google Scholar]
  19. Noga S. J., Normann S. J., Weiner R. S. Methods in laboratory investigation. Isolation of guinea pig monocytes and Kurloff cells: characterization of monocyte subsets by morphology, cytochemistry, and adherence. Lab Invest. 1984 Aug;51(2):244–252. [PubMed] [Google Scholar]
  20. Núez R. M., Rodriguez A. B., Barriga C., De la Fuente M. In vitro and in vivo effects of Imipenem on phagocytic activity of murine peritoneal macrophages. APMIS. 1989 Oct;97(10):879–886. [PubMed] [Google Scholar]
  21. Panula P. Histochemistry and function of bombesin-like peptides. Med Biol. 1986;64(4):177–192. [PubMed] [Google Scholar]
  22. Patel K. V., Schrey M. P. Activation of inositol phospholipid signaling and Ca2+ efflux in human breast cancer cells by bombesin. Cancer Res. 1990 Jan 15;50(2):235–239. [PubMed] [Google Scholar]
  23. Payan D. G., McGillis J. P., Goetzl E. J. Neuroimmunology. Adv Immunol. 1986;39:299–323. doi: 10.1016/s0065-2776(08)60353-3. [DOI] [PubMed] [Google Scholar]
  24. Roth K. A., Evans C. J., Lorenz R. G., Weber E., Barchas J. D., Chang J. K. Identification of gastrin releasing peptide-related substances in guinea pig and rat brain. Biochem Biophys Res Commun. 1983 Apr 29;112(2):528–536. doi: 10.1016/0006-291x(83)91497-3. [DOI] [PubMed] [Google Scholar]
  25. Rozengurt E., Sinnett-Smith J. Bombesin stimulation of DNA synthesis and cell division in cultures of Swiss 3T3 cells. Proc Natl Acad Sci U S A. 1983 May;80(10):2936–2940. doi: 10.1073/pnas.80.10.2936. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Ruff M., Schiffmann E., Terranova V., Pert C. B. Neuropeptides are chemoattractants for human tumor cells and monocytes: a possible mechanism for metastasis. Clin Immunol Immunopathol. 1985 Dec;37(3):387–396. doi: 10.1016/0090-1229(85)90108-4. [DOI] [PubMed] [Google Scholar]
  27. Sinnett-Smith J., Lehmann W., Rozengurt E. Bombesin receptor in membranes from Swiss 3T3 cells. Binding characteristics, affinity labelling and modulation by guanine nucleotides. Biochem J. 1990 Jan 15;265(2):485–493. doi: 10.1042/bj2650485. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Tohmatsu T., Nishida A., Nagao S., Nakashima S., Nozawa Y. Inhibitory action of cyclic AMP on inositol 1,4,5-trisphosphate-induced Ca2+ release in saponin-permeabilized platelets. Biochim Biophys Acta. 1989 Sep 19;1013(2):190–193. doi: 10.1016/0167-4889(89)90048-7. [DOI] [PubMed] [Google Scholar]
  29. Unanue E. R., Allen P. M. The basis for the immunoregulatory role of macrophages and other accessory cells. Science. 1987 May 1;236(4801):551–557. doi: 10.1126/science.2437650. [DOI] [PubMed] [Google Scholar]
  30. Wiedermann C. J. Bombesin-like peptides as growth factors. Wien Klin Wochenschr. 1989 Jun 23;101(13):435–440. [PubMed] [Google Scholar]
  31. Wiedermann C. J., Goldman M. E., Plutchok J. J., Sertl K., Kaliner M. A., Johnston-Early A., Cohen M. H., Ruff M. R., Pert C. B. Bombesin in human and guinea pig alveolar macrophages. J Immunol. 1986 Dec 15;137(12):3928–3932. [PubMed] [Google Scholar]
  32. Zabrenetzky V., Gallin E. K. Inositol 1,4,5-trisphosphate concentrations increase after adherence in the macrophage-like cell line J774.1. Biochem J. 1988 Nov 1;255(3):1037–1043. doi: 10.1042/bj2551037. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Immunology are provided here courtesy of British Society for Immunology

RESOURCES