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      Mononuclear-Cell Peptide Mediation of Chromaffin-Cell Epinephrine Secretion

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          Previously, we have shown that novel mononuclear-cell-derived factor(s) [molecular weight (MW) <3,000] stimulate the release of epinephrine (EPI) from adrenal medullary chromaffin cells to levels comparable to that of maximal cholinergic stimulation. The present study provides evidence that the observed bioactivity is due to the action of a single peptide of 627 Da apparent MW. The peptide nature of the bioactive component was suggested by a decreased bioactivity after acid hydrolysis as well as altered bioactivity subsequent to peptidase (carboxypeptidase Y, leucine aminopeptidase) treatment. The bioactive conditioned-medium (CM) peptide(s) were isolated and further characterized using SDS-PAGE analysis. SDS-PAGE separation of G-25 Sephadex purified CM shows that bioactivity resides in a single peptide band. Additional studies revealed that CM also mediates norepinephrine release from sympathetic ganglia cells. Regulation of peptide production was shown to involve negative feedback in that incubation with mononuclear cells with EPI prevented further bioactive peptide release. This feedback inhibition was partially blocked by theβ-adrenergic receptor antagonist propranolol. These findings suggest a novel and potentially important mechanism by which the immune system can alter neuroendocrine function.

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          Author and article information

          S. Karger AG
          08 November 1996
          : 3
          : 2-3
          : 119-130
          aDepartment of Physiology, bDepartment of Microbiology and Immunology, and cThe Burn and Shock Trauma Institute, Loyola University Medical Center, Maywood, Ill., USA; dDepartment of Neuropharmacology, University of Antwerp, Belgium
          97236 Neuroimmunomodulation 1996;3:119–130
          © 1996 S. Karger AG, Basel

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          Pages: 12
          Original Paper


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