Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
Sci. Signal., 8 April 2008
Vol. 1, Issue 14, p. re1
[DOI: 10.1126/stke.114re1]
REVIEWS
Calpain in the CNS: From Synaptic Function to Neurotoxicity
Jing Liu1*,
Ming Cheng Liu2,3, and
Kevin K. W. Wang1,2,3*
1Center for Neuroproteomics and Biomarkers Research, Department of Psychiatry, McKnight Brain Institute, Post Office Box 100256, University of Florida, Gainesville, FL 32610, USA. 2Center for Traumatic Brain Injury Studies, Department of Neuroscience, McKnight Brain Institute, Post Office Box 100256, University of Florida, Gainesville, FL 32610, USA. 3Center of Innovative Research, Banyan Biomarkers, Inc., 12085 Research Drive, Alachua, FL 32615, USA.
Gloss: The calpains constitute a class of cellular cysteine proteases that require calcium and are functionally active at neutral pH. In the central nervous system (CNS), controlled activation of calpains may be critical to synaptic function and memory formation. In contrast, physical trauma, or chemical or ischemic insults that lead to a sustained increase in intracellular calcium concentration, may elicit calpain hyperactivation, which is generally associated with severe cellular damage.
Citation: J. Liu, M. C. Liu, K. K. W. Wang, Calpain in the CNS: From Synaptic Function to Neurotoxicity. Sci. Signal.1, re1 (2008).
The editors suggest the following Related Resources on Science sites:
In Science Signaling
EDITORS' CHOICE
Nancy R. Gough (30 April 2013) Sci. Signal.6 (273), ec94.
[DOI: 10.1126/scisignal.2004279] |Abstract »
EDITORS' CHOICE
Nancy R. Gough (23 October 2012) Sci. Signal.5 (247), ec272.
[DOI: 10.1126/scisignal.2003712] |Abstract »
EDITORS' CHOICE
Nancy R. Gough (22 May 2012) Sci. Signal.5 (225), ec142.
[DOI: 10.1126/scisignal.2003241] |Abstract »
PERSPECTIVES
Kambiz Mousavi and Vittorio Sartorelli (14 December 2010) Sci. Signal.3 (152), pe49.
[DOI: 10.1126/scisignal.3152pe49] |Abstract »|Full Text »|PDF »
EDITORS' CHOICE
Nancy R. Gough (10 August 2010) Sci. Signal.3 (134), ec246.
[DOI: 10.1126/scisignal.3134ec246] |Abstract »
TEACHING RESOURCES
Jing Liu, Ming Cheng Liu, and Kevin K. W. Wang (10 June 2008) Sci. Signal.1 (23), tr3.
[DOI: 10.1126/scisignal.123tr3] |Abstract »|Full Text »
THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
ALLN rescues an in vitro excitatory synaptic transmission deficit in Lis1 mutant mice.
J. Y. Sebe, M. Bershteyn, S. Hirotsune, A. Wynshaw-Boris, and S. C. Baraban (2013)
J Neurophysiol
109, 429-436
|Abstract »|Full Text »|PDF »
Activity-Dependent Cleavage of the K-Cl Cotransporter KCC2 Mediated by Calcium-Activated Protease Calpain.
M. Puskarjov, F. Ahmad, K. Kaila, and P. Blaesse (2012)
J. Neurosci.
32, 11356-11364
|Abstract »|Full Text »|PDF »
Calpastatin-mediated inhibition of calpains in the mouse brain prevents mutant ataxin 3 proteolysis, nuclear localization and aggregation, relieving Machado-Joseph disease.
A. T. Simoes, N. Goncalves, A. Koeppen, N. Deglon, S. Kugler, C. B. Duarte, and L. Pereira de Almeida (2012)
Brain
135, 2428-2439
|Abstract »|Full Text »|PDF »
Mechanistic involvement of the calpain-calpastatin system in Alzheimer neuropathology.
M. Higuchi, N. Iwata, Y. Matsuba, J. Takano, T. Suemoto, J. Maeda, B. Ji, M. Ono, M. Staufenbiel, T. Suhara, et al. (2012)
FASEB J
26, 1204-1217
|Abstract »|Full Text »|PDF »
Activation of calpains mediates early lung neutrophilic inflammation in ventilator-induced lung injury.
D. Liu, Z. Yan, R. D. Minshall, D. E. Schwartz, Y. Chen, and G. Hu (2012)
Am J Physiol Lung Cell Mol Physiol
302, L370-L379
|Abstract »|Full Text »|PDF »
Regulation of GABAergic synapse formation and plasticity by GSK3{beta}-dependent phosphorylation of gephyrin.
S. K. Tyagarajan, H. Ghosh, G. E. Yevenes, I. Nikonenko, C. Ebeling, C. Schwerdel, C. Sidler, H. U. Zeilhofer, B. Gerrits, D. Muller, et al. (2011)
PNAS
108, 379-384
|Abstract »|Full Text »|PDF »
The Ankyrin Repeat-rich Membrane Spanning (ARMS)/Kidins220 Scaffold Protein Is Regulated by Activity-dependent Calpain Proteolysis and Modulates Synaptic Plasticity.
S. H. Wu, J. C. Arevalo, V. E. Neubrand, H. Zhang, O. Arancio, and M. V. Chao (2010)
J. Biol. Chem.
285, 40472-40478
|Abstract »|Full Text »|PDF »
Human Immunodeficiency Virus-1 Tat Activates Calpain Proteases via the Ryanodine Receptor to Enhance Surface Dopamine Transporter Levels and Increase Transporter-Specific Uptake and Vmax.
S. W. Perry, J. Barbieri, N. Tong, O. Polesskaya, S. Pudasaini, A. Stout, R. Lu, M. Kiebala, S. B. Maggirwar, and H. A. Gelbard (2010)
J. Neurosci.
30, 14153-14164
|Abstract »|Full Text »|PDF »
Physiological Basis of Tingling Paresthesia Evokedby Hydroxy-{alpha}-Sanshool.
R. C. Lennertz, M. Tsunozaki, D. M. Bautista, and C. L. Stucky (2010)
J. Neurosci.
30, 4353-4361
|Abstract »|Full Text »|PDF »
Adaptive Modifications in the Calpain/Calpastatin System in Brain Cells after Persistent Alteration in Ca2+ Homeostasis.
R. Stifanese, M. Averna, R. De Tullio, M. Pedrazzi, F. Beccaria, F. Salamino, M. Milanese, G. Bonanno, S. Pontremoli, and E. Melloni (2010)
J. Biol. Chem.
285, 631-643
|Abstract »|Full Text »|PDF »
Iron-Induced Oxidative Injury Differentially Regulates PI3K/Akt/GSK3{beta} Pathway in Synaptic Endings from Adult and Aged Rats.
R. M. Uranga, N. M. Giusto, and G. A. Salvador (2009)
Toxicol. Sci.
111, 331-344
|Abstract »|Full Text »|PDF »
Extrasynaptic NMDA Receptors Couple Preferentially to Excitotoxicity via Calpain-Mediated Cleavage of STEP.
J. Xu, P. Kurup, Y. Zhang, S. M. Goebel-Goody, P. H. Wu, A. H. Hawasli, M. L. Baum, J. A. Bibb, and P. J. Lombroso (2009)
J. Neurosci.
29, 9330-9343
|Abstract »|Full Text »|PDF »
Calpain Expression and Activity during Lens Fiber Cell Differentiation.
A. De Maria, Y. Shi, N. M. Kumar, and S. Bassnett (2009)
J. Biol. Chem.
284, 13542-13550
|Abstract »|Full Text »|PDF »
Calpain-Mediated N-Cadherin Proteolytic Processing in Brain Injury.
Y.-N. Jang, Y.-S. Jung, S. H. Lee, C.-H. Moon, C.-H. Kim, and E. J. Baik (2009)
J. Neurosci.
29, 5974-5984
|Abstract »|Full Text »|PDF »