TY - JOUR
T1 - Calpain activity contributes to the control of SNAP-25 levels in neurons
AU - Grumelli, Carlotta
AU - Berghuis, Paul
AU - Pozzi, Davide
AU - Caleo, Matteo
AU - Antonucci, Flavia
AU - Bonanno, Giambattista
AU - Carmignoto, Giorgio
AU - Dobszay, Marton Benedek
AU - Harkany, Tibor
AU - Matteoli, Michela
AU - Verderio, Claudia
PY - 2008/10/29
Y1 - 2008/10/29
N2 - 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.
AB - 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.
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U2 - 10.1016/j.mcn.2008.07.011
DO - 10.1016/j.mcn.2008.07.011
M3 - Article
C2 - 18721885
AN - SCOPUS:53649086931
VL - 39
SP - 314
EP - 323
JO - Molecular and Cellular Neurosciences
JF - Molecular and Cellular Neurosciences
SN - 1044-7431
IS - 3
ER -