Historical Background
Calpains are a family of non-lysosomal cysteine proteases that are activated by calcium. Calcium-dependent protease activity has already been detected in 1964 in brain tissue from rats, and this activity was later related to calpain. Yet, the identification of the protein started off with structural analysis of muscle tissue and its alteration by post mortem degradation (history broadly reviewed by Goll et al. 1990, 2003): In the late 1960s, Wayne Busch and Darrel Goll studied the physiological effects of Ca2+ in tissue specimen of rabbit muscle. When muscle strips were left overnight in a 1 mM Ca2+buffer solution, it became apparent that the Z-line (a structural element separating sarcomers in skeletal muscle) had completely disappeared. Busch and Goll subsequently incubated the stripes in EGTA, thereby preventing degradation of the Z-line. With the help of...
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Bevers MB, Neumar RW. Mechanistic role of calpains in postischemic neurodegeneration. J Cereb Blood Flow Metab. 2008;28:655–73.
Glading A, Lauffenburger DA, Wells A. Cutting to the chase: calpain proteases in cell motility. Trends Cell Biol. 2002;12:46–54.
Goll DE, Kleese WC, Okitani A, Kumamoto T, Cong J, Kapprell H-P. Historical background and current status of the Ca-dependent proteinase system. In: Intracellular calcium-dependent proteolysis. Boca Raton: CRC Press; 1990.
Goll DE, Thomson VF, Li H, Wei W, Cong J. The calpain system. Physiol Rev. 2003;83:731–801.
Inserte J, Barrabes JA, Hernando V, Garcia-Dorado D. Orphan targets for reperfusion injury. Cardiovasc Res. 2009;83:169–78.
Khorchid A, Ikura M. How calpain is activated by calcium. Nat Struct Biol. 2002;9:239–41.
Liu J, Liu MC, Wang KKW. Calpain in the CNS: from synaptic function to neurotoxicity. Sci Signal. 2008;1:re1. 29:152–8.
Pietsch M, Chua K, Abell AD. Calpains: attractive targets for the development of synthetic inhibitors. Curr Top Med Chem. 2010;10:270–93.
Rachel AH, Campbell RL, Davies PL. Calcium-bound structure of calpain and its mechanism of inhibition by calpastatin. Nature. 2008;456:409–12.
Saatman KE, Creed J, Raghupathi R. Calpain as a therapeutic target in traumatic brain injury. Neurotherapeutics. 2010;7:31–42.
Saez ME, Ramirez-Lorca R, Moron FJ, Ruiz A. The therapeutic potential of the calpain family: new aspects. Drug Discov Today. 2006;11:917–23.
Strobl S, Fernandez-Catalan C, Braun M, Huber R, Masumoto H, Nakagawa K, Irie A, Sorimachi H, Bourenkowi G, Bartuniki H, Suzuki K, Bode W. The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium. PNAS. 2000;97:588–92.
Vosler PS, Brennan CS, Chen J. Calpain-mediated signaling mechanisms in neuronal injury and neurodegeneration. Mol Neurobiol. 2008;38:78–100.
Wu H-Y, Lynch DR. Calpain synaptic function. Mol Neurobiol. 2006;33:215–36.
Zatz M, Starling A. Calpains and disease. New Engl J Med. 2005;352:2413–23.
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Nimmrich, V., Bespalov, A., Möller, A. (2018). Calpain. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham. https://doi.org/10.1007/978-3-319-67199-4_23
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DOI: https://doi.org/10.1007/978-3-319-67199-4_23
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