Botulinum neurotoxin light chains inhibit both Ca(2+)-induced and GTP analogue-induced catecholamine release from permeabilised adrenal chromaffin cells

FEBS Lett. 1996 May 20;386(2-3):137-40. doi: 10.1016/0014-5793(96)00432-2.

Abstract

Using digitonin-permeabilised bovine adrenal chromaffin cells, the effects of botulinum neurotoxin light chains on exocytosis triggered by Ca2+ or by GppNHp were examined. Botulinum neurotoxin D light chain, prepared as a His(6)-tagged recombinant protein, cleaved VAMP and substantially inhibited catecholamine release due to Ca2+ and GppNHp. Botulinum neurotoxin C1 and E light chains produced partial inhibition of both Ca(2+)- and GppNHp-induced catecholamine release. These results suggest that Ca(2+)-dependent exocytosis and Ca(2+)-independent exocytosis triggered by a non-hydrolysable GTP analogue occurs via a SNARE-dependent mechanism in chromaffin cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adrenal Medulla / cytology
  • Adrenal Medulla / drug effects*
  • Adrenal Medulla / metabolism
  • Animals
  • Botulinum Toxins / pharmacology*
  • Calcium / antagonists & inhibitors
  • Calcium / pharmacology*
  • Catecholamines / metabolism*
  • Cattle
  • Cell Membrane Permeability
  • Cells, Cultured
  • Culture Media
  • Guanylyl Imidodiphosphate / antagonists & inhibitors
  • Guanylyl Imidodiphosphate / pharmacology*
  • Membrane Proteins / metabolism
  • R-SNARE Proteins
  • Recombinant Fusion Proteins / pharmacology
  • SNARE Proteins
  • Signal Transduction
  • Vesicular Transport Proteins*

Substances

  • Catecholamines
  • Culture Media
  • Membrane Proteins
  • R-SNARE Proteins
  • Recombinant Fusion Proteins
  • SNARE Proteins
  • Vesicular Transport Proteins
  • Guanylyl Imidodiphosphate
  • Botulinum Toxins
  • Calcium