期刊
MOLECULAR AND CELLULAR NEUROSCIENCE
卷 39, 期 3, 页码 314-323出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.mcn.2008.07.011
关键词
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资金
- EU [LSHM-CT-2005-019055]
- Telethon [GP04196]
- CARIPLO [2006.0779/109251]
- Ministero della Salute per la realizzazione dell progetto Ex art. [56 (2005)]
- Swedish Medical Research Council
- Alzheimer's Association
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.
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