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Class 3 Hydrolases pp 61–80Cite as

Calpain-2

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References

  1. Dutt, P.; Springgs, C.N.; Davies, P.L.; Jia, Z.; Elce, J.S.: Origins of the difference in Ca2+ requirement for activation of μ-and m-calpain. Biochem. J., 367, 263–269 (2002)

    Article  PubMed  CAS  Google Scholar 

  2. Emori, Y.; Kawasaki, H.; Sugihara, H.; Imajoh, S.; Kawashima, S.; Suzuki K.: Isolation and sequence analyses of cDNA clones for the large subunits of two isozymes of rabbit calcium-dependent protease. J. Biol. Chem., 261, 9465–9471 (1986)

    PubMed  CAS  Google Scholar 

  3. Minami, Y.; Emori, Y.; Kawasaki, H.; Suzuki, K: E-F hand structure-domain of calcium-activated neutral protease (CANP) can bind Ca2+ ions. J. Biochem., 101, 889–895 (1987)

    PubMed  CAS  Google Scholar 

  4. Sun, W.; Ji, S.Q.; Ebert, P.J.; Bidwell, C.A.; Hancock, D.L.: Cloning the partial cDNAs of μ-calpain and m-calpain from porcine skeletal muscle. Biochimie, 75, 931–936 (1993)

    Article  PubMed  CAS  Google Scholar 

  5. Nakajima, T.; Fukiage, C.; Azuma, M.; Ma, H.; Shearer, T.R.: Different expression patterns for ubiquitous calpains and Capn3 splice variants in monkey ocular tissues. Biochim. Biophys. Acta, 1519, 55–64 (2001)

    PubMed  CAS  Google Scholar 

  6. Murachi, T.; Tanaka, K.; Hatanaka, M.; Murakami, T.: Intracellular cellular Ca2+-dependent protease (calpain) and its high-molecular-weight endogenous inhibitor (calpastatin). Adv. Enzyme Regul., 19, 407–424 (1981)

    Article  CAS  Google Scholar 

  7. Kishimoto, A.; Kajikawa, N.; Tabuchi, H.; Shiota, M.; Nishizuka, Y.: Calcium-dependent neutral proteases, widespread occurence of a species of protease active at lower concentrations of calcium. J. Biochem., 90, 889–892 (1981)

    PubMed  CAS  Google Scholar 

  8. Penny, I.F.; Taylor, M.A.J.; Harris, A.G.; Etherington, D.J.: Purification and immunological characterization of two calcium-activated neutral proteinases from rabbit skeletal muscle. Biochim. Biophys. Acta, 829, 244–252 (1985)

    PubMed  CAS  Google Scholar 

  9. Fukui, I.; Toyohara, H.; Ito, K.; Hamakubo, T.; Murachi, T.: Molecular and catalytic characterization of intact heterodimeric and derived monomeric calpains isolated under different conditions from pig polymorphonuclear leukocytes. Biochemistry, 27, 3260–3267 (1988)

    Article  PubMed  CAS  Google Scholar 

  10. Yoshimura, N.; Tsukahara, I.; Murachi, T.: Calpain and calpastatin in porcine retina. Biochem. J., 223, 47–51 (1984)

    PubMed  CAS  Google Scholar 

  11. Kitahara, A.; Sasaki, T.; Kikuchi, T.; Yumoto, N.; Yoshimura, N.; Hatanaka, M.; Murachi, T.: Large-scale purification of porcine calpain I and calpain II and comparison of proteolytic fragments of their subunits. J. Biochem., 95, 1759–1766 (1984)

    PubMed  CAS  Google Scholar 

  12. Shastri, R.; Jagadeesh, G.; Anandaraj, M.P.J.S.: Human placental calcium activated neutral proteinase: Separation and functional characterization of subunits. J. Biosci., 15, 427–434 (1990)

    Article  CAS  Google Scholar 

  13. Murakami, T.; Ueda, M.; Hamakubo, T.; Murachi, T.: Identification of both calpains I and II in nucleated chicken erythrocytes. J. Biochem., 103, 168–171 (1988)

    PubMed  CAS  Google Scholar 

  14. Yoshimura, N.; Kikuchi, T.; Sasaki, T.; Kithara, A.; Hatanaka, M.; Murachi, T.: Two distinct Ca2+ proteases (calpain I and calpain II) purified concurrently by the same method from rat kidney. J. Biol. Chem., 258, 8883–8889 (1983)

    PubMed  CAS  Google Scholar 

  15. Inomata, M.; Nomoto, M.; Hayashi, M.; Nakamura, M.; Imahori, K.; Kawashima, S.: Comparison of low and high calcium requiring forms of the calcium-activated neutral protease (CANP) from rabbit skeletal muscle. J. Biochem., 95, 1661–1670 (1984)

    PubMed  CAS  Google Scholar 

  16. Molinari, M.; maki, M.; Carafoli, E.: Purification of μ-calpain by a novel affinity chromatography approach. New insight into the mechanism of the interaction of the protease with targets. J. Biol. Chem., 270, 14576–14581 (1995)

    Article  PubMed  CAS  Google Scholar 

  17. Zhang, H.; Yamamoto, Y.; Shumiya, S.; Kunimatsu, M.; Nishi, K.; Ohkubo, I.; Kani, K.: Peptidases play an important role in cataractogenesis: an immunohistochemical study on lenses derived from Shumiya cataract rats. Histochem. J., 33, 511–521 (2002)

    Article  CAS  Google Scholar 

  18. Rojas, F.J.; Brush, M.; Moretti-Rojas, I.: Calpain-calpastatin: a novel, complete calcium-dependent protease system in human spermatozoa. Mol. Hum. Reprod., 5, 520–526 (1999)

    Article  PubMed  CAS  Google Scholar 

  19. Sazontova, T.G.; Matskevich, A.A.; Arkhipenko, Y.V.: Calpains: physiological and pathophysiological significance. Pathophysiology, 6, 91–102 (1999)

    Article  CAS  Google Scholar 

  20. Strobl S.; Fernandez-Catalan C.; Braun M.; Huber R.; Masumoto H.; Nakagawa K.; Irie A.; Sorimachi H.; Bourenkow G.; Bartunik H.; Suzuki K.; Bode W.: The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium. Proc. Natl. Acad. Sci. USA, 97, 588–592 (2000)

    Article  PubMed  CAS  Google Scholar 

  21. Imajoh, S.; Aoki, K.; Ohno, S.; Emori, Y.; Kawasaki, H.; Sugihara, H.; Suzuki, K.: Molecular cloning of the cDNA for the large subunit of the high-Ca2+-requiring form of human Ca2+-activated neutral protease. Biochemistry, 27, 8122–8128 (1988)

    Article  PubMed  CAS  Google Scholar 

  22. Hata, A.; Ohno, S.; Akita, Y.; Suzuki, K.: Tandemly reiterated negative enhancer-like elements regulate transcription of a human gene for the large subunit of calcium-dependent protease. J. Biol. Chem., 264, 6404–6411 (1989)

    PubMed  CAS  Google Scholar 

  23. Ye, Z.; Connor, J.R.: cDNA cloning by amplification of circularized first strand cDNAs reveals non-IRE-regulated iron-responsive mRNAs. Biochem. Biophys. Res. Commun., 275, 223–227 (2000)

    Article  PubMed  CAS  Google Scholar 

  24. Strausberg, R.L.; Feingold, E.A.; Grouse, L.H.; Derge, J.G., et al.: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc. Natl. Acad. Sci. USA, 99, 16899–16903 (2002)

    Article  PubMed  Google Scholar 

  25. Sorimachi, H.; Tsukahara, T.; Okada-Ban, M.; Sugita, H.; Ishiura, S.; Suzuki, K.: Identification of a third ubiquitous calpain species — chicken muscle expresses four distinct calpains. Biochim. Biophys. Acta, 1261, 381–393 (1995)

    PubMed  Google Scholar 

  26. Deluca, C.I.; Davies P.L.; Samis, J.A.; Elce, J.S.: Molecular cloning and bacterial expression of cDNA for rat calpain II 80 kDa subunit. Biochim. Biophys. Acta, 1216, 81–93 (1993)

    PubMed  CAS  Google Scholar 

  27. Moldoveanu, T.; Hosfield, C.M.; Jia, Z.; Elce, J.S.; Davies, P.L.: Ca2+-induced structural changes in rat m-calpain revealed by partial proteolysis. Biochim. Biophys. Acta, 1545, 245–254 (2001)

    PubMed  CAS  Google Scholar 

  28. Arthur, J.S.; Gauthier, S.; Elce, J.S.: Active site residues in m-calpain: identification by site-directed mutagenesis. FEBS Lett., 368, 397–400 (1995)

    Article  PubMed  CAS  Google Scholar 

  29. Hosfield, C.M.; Moldoveanu, T.; Davies, P.L.; Elce, J.S.; Jia, Z.: Calpain mutants with increased Ca2+ sensitivity and implications for the role of the C2-like domain. J. Biol. Chem., 276, 7404–7407 (2001)

    Article  PubMed  CAS  Google Scholar 

  30. Hosfield, C.M.; Elce, J.S.; Davies, P.L.; Jia, Z.: Crystal structure of calpain reveals the structural basis for Ca2+-dependent protease activity and a novel mode of enzyme activation. EMBO J., 18, 6880–6889 (1999)

    Article  PubMed  CAS  Google Scholar 

  31. Zhang, J.L.; Patel, J.M.; Block, E.R.: Hypoxia-specific upregulation of calpain activity and gene expression in pulmonary artery endothelial cells. Am. J. Physiol., 275, L461–L468 (1998)

    PubMed  CAS  Google Scholar 

  32. Dear, T.N.; Matena, K.; Vingron, M.; Boehm, T.: A new subfamily of vertebrate calpains lacking a calmodulin-like domain: implications for calpain regulation and evolution. Genomics, 45, 175–184 (1997)

    Article  PubMed  CAS  Google Scholar 

  33. Hosfield, C.M.; Ye, Q.; Arthur, J.S.C.; Hegadorn, C.; Croall, D.E.; Elce, J.S.; Jia, Z.: Crystallization and X-ray crystallographic analysis of m-calpain, a Ca2+-dependent protease. Acta Crystallogr. Sect. D, 55, 1484–1486 (1999)

    Article  CAS  Google Scholar 

  34. Wang, J.-H.; Jiang, S.-T.: Properties of calpain II from Tilapia muscle. Agric. Biol. Chem., 55, 339–345 (1991)

    CAS  Google Scholar 

  35. Sargianos, N.; Gaitanaki, C.; Beis, I.: Purification and characterization of m-calpain from the skeletal muscle of the amphibian Rana ridibunda. J. Exp. Zool., 269, 95–105 (1994)

    Article  PubMed  CAS  Google Scholar 

  36. Elce, J.S.; Hegadorn, C.; Gauthier, S.; Vince, J.W.; Davies, P.L.: Recombinant calpain II: improved expression systems and production of a C105A active-site mutant for crystallography. Protein Eng., 8, 843–848 (1995)

    Article  PubMed  CAS  Google Scholar 

  37. Masumoto, H.; Yoshizawa, T.; Sorimachi, H.; Nishino, T.; Ishiura, S.; Suzuki, K.: Overexpression, purification, and characterization of human m-calpain and its active site mutant, m-C105S-calpain, using a baculovirus expression system. J. Biochem., 124, 957–961 (1998)

    PubMed  CAS  Google Scholar 

  38. Azarian, S.M.; Schlamp, C.L.; Williams, D.S.: Characterization of calpain II in the retina and photoreceptor outer segments. J. Cell Sci., 105, 787–798 (1993)

    PubMed  CAS  Google Scholar 

  39. Wang, J.-H.; Ma, W.-C.; Su, J.-C.; Chen, C.-S.; Jiang, S.-T.: Comparison of the properties of m-calpain from Tilapia and grass shrimp muscles. J. Agric. Food Chem., 41, 1379–1384 (1993)

    Article  CAS  Google Scholar 

  40. Hirao, T.; Takahashi, K.: Purification and characterization of a calcium-activated neutral protease from monkey brain and its action on neuropeptides. J. Biochem., 96, 775–784 (1984)

    PubMed  CAS  Google Scholar 

  41. Dourdin, N.; Balcerzak, D.; Brustis, J.J.; Poussard, S.; Cottin, P.; Ducastaing, A.: Potential m-calpain substrates during myoblast fusion. Exp. Cell Res., 246, 433–442 (1999)

    Article  PubMed  CAS  Google Scholar 

  42. Ojha, M.; Barja, F.: Spatial and cellular localization of calcium-dependent protease (CDP II) in Allomyces arbuscula. J. Cell Sci., 116, 1095–1105 (2003)

    Article  PubMed  CAS  Google Scholar 

  43. Mkwetshana, N.; Naude, R.J.; Oelofsen, W.; Muramoto, K.; Naganuma, T.: The purification and characterization of m-calpain from ostrich brain. Int. J. Biochem. Cell Biol., 34, 337–347 (2002)

    Article  PubMed  CAS  Google Scholar 

  44. Smith, S.D.; Jia, Z.; Huynh, K.K.; Wells, A.; Elce, J.S.: Glutamate substitutions at a PKA consensus site are consistent with inactivation of calpain by phosphorylation. FEBS Lett., 542, 115–118 (2003)

    Article  PubMed  CAS  Google Scholar 

  45. Glading, A.; Chang, P.; Lauffenburger, D.A.; Wells, A.: Epidermal growth factor receptor activation of calpain is required for fibroblast motility and occurs via an ERK/MAP kinase signaling pathway. J. Biol. Chem., 275, 2390–2398 (2000)

    Article  PubMed  CAS  Google Scholar 

  46. Han, Y.; Weinman, S.; Boldogh, I.; Walker, R.K.; Brasier, A.R.: Tumor necrosis factor-α-inducible IκBa proteolysis mediated by cytosolic m-calpain. A mechanism parallel to the ubiquitin-proteasome pathway for nuclear factor-κB activation. J. Biol. Chem., 274, 787–794 (1999)

    Article  PubMed  CAS  Google Scholar 

  47. Dedieu, S.; Mazeres, G.; Dourdin, N.; Cottin, P.; Brustis, J.-J.: Transactivation of capn2 by Myogenic Regulatory Factors During Myogenesis. J. Mol. Biol., 326, 453–465 (2003)

    Article  PubMed  CAS  Google Scholar 

  48. Ladrat, C.; Verrez-Bagnis, V.; Noel, J.; Fleurence, J.: Milli-calpain from sea bass (Dicentrarchus labrax) white muscle: purification, characterization of its activity and activation in vitro. Mar. Biotechnol., 4, 51–62 (2002)

    Article  PubMed  CAS  Google Scholar 

  49. Kawai, K.; Fujimoto, K.; Okamoto, A.; Inaba, A.; Yamada, H.; Katoh, S.: Transient activation of dihydropteridine reductase by Ca2+-activated proteolysis. Zool. Sci., 17, 437–443 (2000)

    CAS  Google Scholar 

  50. Hata, S.; Koyama, S.; Kawahara, H.; Doi, N.; Maeda, T.; Toyama-Sorimachi, N.; Abe, K.; Suzuki, K.; Sorimachi, H.: Stomach-specific calpain, nCL-2, localizes in mucus cells and proteolyzes the β-subunit of coatomer complex, β-COP. J. Biol. Chem., 281, 11214–11224 (2006)

    Article  PubMed  CAS  Google Scholar 

  51. Veerann, V.; Kaji, T.; Boland, B.; Odrljin, T.; Mohan, P.; Basavarajappa, B.S.; Peterhoff, C.; Cataldo, A.; Rudnicki, A.; Amin, N.; Li, B.S.; Pant, H.C.; Hungund, B.L.; Arancio, O.; Nixon, R.A.: Calpain mediates calcium-induced activation of the Erk1,2 MAPK pathway and cytoskeletal phosphorylation in neurons: Relevance to Alzheimers disease. Am. J. Pathol., 165, 795–805 (2004)

    Google Scholar 

  52. Azuma, M.; Tamada, Y.; Kanaami, S.; Nakajima, E.; Nakamura, Y.; Fukiage, C.; Forsberg, N.E.; Duncan, M.K.; Shearer, T.R.: Differential influence of proteolysis by calpain 2 and Lp82 on in vitro precipitation of mouse lens crystallins. Biochem. Biophys. Res. Commun., 307, 558–563 (2003)

    Article  PubMed  CAS  Google Scholar 

  53. Li, H.; Thompson, V.F.; Goll, D.E.: Effects of autolysis on properties of μ-and m-calpain. Biochim. Biophys. Acta, 1691, 91–103 (2004)

    Article  PubMed  CAS  Google Scholar 

  54. Inserte, J.; Garcia-Dorado, D.; Hernando, V.; Soler-Soler, J.: Calpain-mediated impairment of Na+/K+-ATPase activity during early reperfusion contributes to cell death after myocardial ischemia. Circ. Res., 97, 465–473 (2005)

    Article  PubMed  CAS  Google Scholar 

  55. Carragher, N.O.: Calpain inhibition: a therapeutic strategy targeting multiple disease states. Curr. Pharm. Des., 12, 615–638 (2006)

    Article  PubMed  CAS  Google Scholar 

  56. Franco, S.; Perrin, B.; Huttenlocher, A.: Isoform specific function of calpain 2 in regulating membrane protrusion. Exp. Cell Res., 299, 179–187 (2004)

    Article  PubMed  CAS  Google Scholar 

  57. Reed, N.A.; Castellini, M.A.; Ma, H.; Shearer, T.R.; Duncan, M.K.: Protein expression patterns for ubiquitous and tissue specific calpains in the developing mouse lens. Exp. Eye Res., 76, 433–443 (2003)

    Article  PubMed  CAS  Google Scholar 

  58. Maddock, K.R.; Huff-Lonergan, E.; Rowe, L.J.; Lonergan, S.M.: Effect of pH and ionic strength on μ-and m-calpain inhibition by calpastatin. J. Anim. Sci., 83, 1370–1376 (2005)

    PubMed  CAS  Google Scholar 

  59. Carlin, K.R.; Huff-Lonergan, E.; Rowe, L.J.; Lonergan, S.M.: Effect of oxidation, pH, and ionic strength on calpastatin inhibition of μ-and m-calpain. J. Anim. Sci., 84, 925–937 (2006)

    PubMed  CAS  Google Scholar 

  60. Shao, H.; Chou, J.; Baty, C.J.; Burke, N.A.; Watkins, S.C.; Stolz, D.B.; Wells, A.: Spatial localization of m-calpain to the plasma membrane by phosphoinositide biphosphate binding during epidermal growth factor receptor-mediated activation. Mol. Cell. Biol., 26, 5481–5496 (2006)

    Article  PubMed  CAS  Google Scholar 

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  1. Bioinformatics & Systems Biology, Technical University Braunschweig, Langer Kamp 19b, 38106, Braunschweig, Germany

    Antje Chang

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(2009). Calpain-2. In: Chang, A. (eds) Class 3 Hydrolases. Springer Handbook of Enzymes, vol S6. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-85705-1_7

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