Mast cell chymase reduces the toxicity of Gila monster venom, scorpion venom, and vasoactive intestinal polypeptide in mice

J Clin Invest. 2011 Oct;121(10):4180-91. doi: 10.1172/JCI46139. Epub 2011 Sep 19.

Abstract

Mast cell degranulation is important in the pathogenesis of anaphylaxis and allergic disorders. Many animal venoms contain components that can induce mast cell degranulation, and this has been thought to contribute to the pathology and mortality caused by envenomation. However, we recently reported evidence that mast cells can enhance the resistance of mice to the venoms of certain snakes and that mouse mast cell-derived carboxypeptidase A3 (CPA3) can contribute to this effect. Here, we investigated whether mast cells can enhance resistance to the venom of the Gila monster, a toxic component of that venom (helodermin), and the structurally similar mammalian peptide, vasoactive intestinal polypeptide (VIP). Using 2 types of mast cell-deficient mice, as well as mice selectively lacking CPA3 activity or the chymase mouse mast cell protease-4 (MCPT4), we found that mast cells and MCPT4, which can degrade helodermin, can enhance host resistance to the toxicity of Gila monster venom. Mast cells and MCPT4 also can limit the toxicity associated with high concentrations of VIP and can reduce the morbidity and mortality induced by venoms from 2 species of scorpions. Our findings support the notion that mast cells can enhance innate defense by degradation of diverse animal toxins and that release of MCPT4, in addition to CPA3, can contribute to this mast cell function.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Carboxypeptidases A / deficiency
  • Carboxypeptidases A / genetics
  • Carboxypeptidases A / physiology*
  • Intercellular Signaling Peptides and Proteins
  • Lizards
  • Mast Cells / enzymology*
  • Mice
  • Mice, Inbred C57BL
  • Mice, Knockout
  • Mice, Mutant Strains
  • Molecular Sequence Data
  • Peptides / antagonists & inhibitors
  • Peptides / genetics
  • Peptides / toxicity
  • Scorpion Venoms / antagonists & inhibitors
  • Scorpion Venoms / toxicity*
  • Serine Endopeptidases / deficiency
  • Serine Endopeptidases / genetics
  • Serine Endopeptidases / physiology*
  • Vasoactive Intestinal Peptide / antagonists & inhibitors
  • Vasoactive Intestinal Peptide / genetics
  • Vasoactive Intestinal Peptide / toxicity*
  • Venoms / toxicity*

Substances

  • Intercellular Signaling Peptides and Proteins
  • Peptides
  • Scorpion Venoms
  • Venoms
  • Vasoactive Intestinal Peptide
  • heliodermin
  • Carboxypeptidases A
  • Cpa3 protein, mouse
  • Serine Endopeptidases
  • mast cell protease 4