Calpain activity contributes to the control of SNAP-25 levels in neurons

Carlotta Grumelli, Paul Berghuis, Davide Pozzi, Matteo Caleo, Flavia Antonucci, Giambattista Bonanno, Giorgio Carmignoto, Marton Benedek Dobszay, Tibor Harkany, Michela Matteoli, Claudia Verderio

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19 Citations (Scopus)


Calpains are a family of calcium-dependent proteases with abundant expression in the CNS, and potent in cleaving some synaptic components. Assessment of calpain activity by its fluorescent substrate, Boc-Leu-Met-CMAC, revealed that Cultured neurons display a significant level of constitutive enzyme activity. Notably, calpain activity differs in distinct neuronal populations, with a significantly higher level of activity in GABAergic cells. Using selectively-enriched cultures of fast-spiking GABAergic interneurons, we show that calpain activity partially contributes to the post-translational down regulation of SNAP-25, a calpain substrate, in differentiated GABA cells. In addition, we demonstrate that SNAP-25 is cleaved by calpain in response to acute seizures induced by intraperitoneal kainate injection in vivo. These data indicate that calpains in neurons are active even at physiological calcium concentrations and that different levels of calpain activation in selected neuron subtypes may contribute to the pattern of synaptic protein expression. (C) 2008 Elsevier Inc. All rights reserved.

Original languageEnglish
Pages (from-to)314-323
Number of pages10
JournalMolecular and Cellular Neuroscience
Issue number3
Early online date29 Jul 2008
Publication statusPublished - 29 Oct 2008


  • pancreatic beta-cells
  • GABAergic neurons
  • hippocampal-neurons
  • synaptic vesicles
  • in-situ
  • cleavage
  • expression
  • proteolysis
  • activation
  • calcium


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