New antimicrobial activity for the catecholamine release-inhibitory peptide from chromogranin A

Cell Mol Life Sci. 2005 Feb;62(3):377-85. doi: 10.1007/s00018-004-4461-9.


Catestatin (bCGA(344-364)), an endogenous peptide of bovine chromogranin A, was initially characterized for its effect on the inhibition of catecholamine release from chromaffin cells. Catestatin and its active domain (bCGA(344-358)) were identified in chromaffin cells and in secretion medium. The present study identified a potent antimicrobial activity of bCGA(344-358) in the lowmicromolar range against bacteria, fungi and yeasts, without showing any haemolytic activity. Confocal laser microscopy demonstrated penetration of the rhodaminated peptide into the cell membranes of fungi and yeasts and its intracellular accumulation. Time-lapse videomicroscopy showed arrest of fungal growth upon penetration of the labelled peptide into a fungal filament. We identified several catestatin-containing fragments in the stimulated secretion medium of human polymorphonuclear neutrophils, suggesting the N-terminal sequence of catestatin (bCGA(344-358)) (named cateslytin) as a novel component of innate immunity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Anti-Infective Agents / chemistry
  • Anti-Infective Agents / pharmacology*
  • Bacteria / drug effects
  • Catecholamines / chemistry*
  • Cattle
  • Chromogranin A
  • Chromogranins / chemistry*
  • Chromogranins / pharmacology*
  • Fungi / drug effects
  • Humans
  • Microbial Sensitivity Tests
  • Molecular Sequence Data
  • Peptide Fragments / chemistry
  • Peptide Fragments / pharmacology*
  • Time Factors
  • Yeasts / drug effects


  • Anti-Infective Agents
  • CHGA protein, human
  • Catecholamines
  • Chromogranin A
  • Chromogranins
  • Peptide Fragments
  • chromogranin A (344-364)