Muramyl dipeptide mimicry in the regulation of murine macrophage activation by serotonin

Int J Immunopharmacol. 1995 Mar;17(3):225-32. doi: 10.1016/0192-0561(94)00097-8.

Abstract

Muramyl peptides (MPs) are regulators of macrophage function. That the activities of MPs may be mediated by serotonin (5-HT) is supported by earlier work that demonstrated specific binding sites for MPs on macrophages that competitively bind 5-HT. Both mediators were also shown to enhance the production of superoxide anion (an antibacterial agent) by these cells. We now report on two additional macrophage activation phenomena affected by 5-HT: phagocytosis and induction of tumor necrosis factor alpha (TNF) mRNA. Serotonin acts as a muramyl peptide-like agonist by increasing phagocytosis of tubercle bacilli by murine peritoneal macrophages, and as a partial agonist/antagonist in the induction of mRNA for tumor necrosis factor. These observations provide further evidence for a serotonergic involvement in some of the physiological responses to MPs.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acetylmuramyl-Alanyl-Isoglutamine / immunology
  • Acetylmuramyl-Alanyl-Isoglutamine / pharmacology*
  • Adjuvants, Immunologic / pharmacology*
  • Animals
  • Cells, Cultured
  • Interleukin-1 / genetics
  • Iodine Radioisotopes
  • Macrophage Activation / drug effects*
  • Male
  • Mice
  • Mycobacterium tuberculosis / immunology
  • Phagocytosis / drug effects
  • Serotonin / immunology
  • Serotonin / pharmacology*
  • Tumor Necrosis Factor-alpha / drug effects
  • Tumor Necrosis Factor-alpha / genetics

Substances

  • Adjuvants, Immunologic
  • Interleukin-1
  • Iodine Radioisotopes
  • Tumor Necrosis Factor-alpha
  • Serotonin
  • Acetylmuramyl-Alanyl-Isoglutamine