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Volumn 447, Issue 3, 2012, Pages 335-351

Structure-function relationships in calpains

Author keywords

Calcium binding; Domain structure; Enzyme activation; Inhibitor complex; Proteinase; Proteolysis; X ray crystallography

Indexed keywords

CALPAIN; CALPAIN 1; CALPAIN 2;

EID: 84867270850     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20120921     Document Type: Review
Times cited : (176)

References (121)
  • 2
    • 0001070415 scopus 로고
    • A neutral, calcium-activated proteinase from the soluble fraction of rat brain
    • Guroff, G. (1964) A neutral, calcium-activated proteinase from the soluble fraction of rat brain. J. Biol. Chem. 239, 149-155
    • (1964) J. Biol. Chem. , vol.239 , pp. 149-155
    • Guroff, G.1
  • 3
    • 0014300929 scopus 로고
    • 2+. II. Identification of the kinase activating factor as a proteolytic enzyme
    • 2+. II. Identification of the kinase activating factor as a proteolytic enzyme. Biochemistry 7, 2116-2122
    • (1968) Biochemistry , vol.7 , pp. 2116-2122
    • Huston, R.B.1    Krebs, E.G.2
  • 4
    • 0017101439 scopus 로고
    • 2+-activated protease possibly involved in myofibrillar protein turnover. Purification from porcine muscle
    • 2+-activated protease possibly involved in myofibrillar protein turnover. Purification from porcine muscle. Biochemistry 15, 2150-2158
    • (1976) Biochemistry , vol.15 , pp. 2150-2158
    • Dayton, W.R.1    Goll, D.E.2    Zeece, M.G.3    Robson, R.M.4    Reville, W.J.5
  • 5
    • 0017101433 scopus 로고
    • 2+-activated protease possibly involved in myofibrillar protein turnover. Partial characterization of the purified enzyme
    • 2+-activated protease possibly involved in myofibrillar protein turnover. Partial characterization of the purified enzyme. Biochemistry 15, 2159-2167
    • (1976) Biochemistry , vol.15 , pp. 2159-2167
    • Dayton, W.R.1    Reville, W.J.2    Goll, D.E.3    Stromer, M.H.4
  • 6
    • 0018834017 scopus 로고
    • Calcium-activated neutral protease. Its localization in the myofibril, especially at the Z-band
    • Ishiura, S., Sugita, H., Nonaka, I. and Imahori, K. (1980) Calcium-activated neutral protease. Its localization in the myofibril, especially at the Z-band. J. Biochem. 87, 343-346 (Pubitemid 10138349)
    • (1980) Journal of Biochemistry , vol.87 , Issue.1 , pp. 343-346
    • Ishiura, S.1    Sugita, H.2    Nonaka, I.3    Imahori, K.4
  • 7
    • 0019234255 scopus 로고
    • 2+-dependent protease (calpain) and its high-molecular-weight endogenous inhibitor (calpastatin)
    • 2+-dependent protease (calpain) and its high-molecular-weight endogenous inhibitor (calpastatin). Adv. Enzyme Regul. 19, 407-424
    • (1980) Adv. Enzyme Regul. , vol.19 , pp. 407-424
    • Murachi, T.1    Tanaka, K.2    Hatanaka, M.3    Murakami, T.4
  • 8
    • 0019188854 scopus 로고
    • Alzheimer-type dementia. Possible relation to hypofunction of the cholinergic central nervous system
    • Mellgren, S. I. (1980) [Alzheimer-type dementia. Possible relation to hypofunction of the cholinergic central nervous system]. Tidsskr. Nor. Laegeforen. 100, 1355-1356
    • (1980) Tidsskr. Nor. Laegeforen. , vol.100 , pp. 1355-1356
    • Mellgren, S.I.1
  • 9
    • 0020441884 scopus 로고
    • 2+-activated protease
    • 2+-activated protease. J. Biol. Chem. 257, 12471-12474
    • (1982) J. Biol. Chem. , vol.257 , pp. 12471-12474
    • Wheelock, M.J.1
  • 10
    • 0021749729 scopus 로고
    • Evolutionary origin of a calcium-dependent protease by fusion of genes for a thiol protease and a calcium-binding protein?
    • DOI 10.1038/312566a0
    • Ohno, S., Emori, Y., Imajoh, S., Kawasaki, H., Kisaragi, M. and Suzuki, K. (1984) Evolutionary origin of a calcium-dependent protease by fusion of genes for a thiol protease and a calcium-binding protein? Nature 312, 566-570 (Pubitemid 15182291)
    • (1984) Nature , vol.312 , Issue.5994 , pp. 566-570
    • Ohno, S.1    Emori, Y.2    Imajoh, S.3
  • 11
    • 0024369426 scopus 로고
    • Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and mu-types. Specific expression of the mRNA in skeletal muscle
    • Sorimachi, H., Imajoh-Ohmi, S., Emori, Y., Kawasaki, H., Ohno, S., Minami, Y. and Suzuki, K. (1989) Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and mu-types. Specific expression of the mRNA in skeletal muscle. J. Biol. Chem. 264, 20106-20111 (Pubitemid 20008132)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.33 , pp. 20106-20111
    • Sorimachi, H.1    Imajoh-Ohmi, S.2    Emori, Y.3    Kawasaki, H.4    Ohno, S.5    Minami, Y.6    Suzuki, K.7
  • 12
    • 0031259933 scopus 로고    scopus 로고
    • A new subfamily of vertebrate calpains lacking a calmodulin-like domain: Implications for calpain regulation and evolution
    • DOI 10.1006/geno.1997.4870
    • Dear, N., Matena, K., Vingron, M. and Boehm, T. (1997) A new subfamily of vertebrate calpains lacking a calmodulin-like domain: implications for calpain regulation and evolution. Genomics 45, 175-184 (Pubitemid 27449397)
    • (1997) Genomics , vol.45 , Issue.1 , pp. 175-184
    • Dear, N.1    Matena, K.2    Vingron, M.3    Boehm, T.4
  • 13
    • 0035934230 scopus 로고    scopus 로고
    • Identification and characterization of two novel calpain large subunit genes
    • DOI 10.1016/S0378-1119(01)00599-6, PII S0378111901005996
    • Dear, T. N. and Boehm, T. (2001) Identification and characterization of two novel calpain large subunit genes. Gene 274, 245-252 (Pubitemid 32817142)
    • (2001) Gene , vol.274 , Issue.1-2 , pp. 245-252
    • Dear, T.N.1    Boehm, T.2
  • 14
    • 36148990505 scopus 로고    scopus 로고
    • The calpains: Modular designs and functional diversity
    • Croall, D. E. and Ersfeld, K. (2007) The calpains: modular designs and functional diversity. Genome Biol. 8, 218
    • (2007) Genome Biol. , vol.8 , pp. 218
    • Croall, D.E.1    Ersfeld, K.2
  • 15
    • 79960104591 scopus 로고    scopus 로고
    • Impact of genetic insights into calpain biology
    • Sorimachi, H., Hata, S. and Ono, Y. (2011) Impact of genetic insights into calpain biology. J. Biochem. 150, 23-37
    • (2011) J. Biochem. , vol.150 , pp. 23-37
    • Sorimachi, H.1    Hata, S.2    Ono, Y.3
  • 17
    • 0028113302 scopus 로고
    • Active recombinant rat calpain II. Bacterially produced large and small subunits associate both in vivo and in vitro
    • Graham-Siegenthaler, K., Gauthier, S., Davies, P. L. and Elce, J. S. (1994) Active recombinant rat calpain II. Bacterially produced large and small subunits associate both in vivo and in vitro. J. Biol. Chem. 269, 30457-30460
    • (1994) J. Biol. Chem. , vol.269 , pp. 30457-30460
    • Graham-Siegenthaler, K.1    Gauthier, S.2    Davies, P.L.3    Elce, J.S.4
  • 19
    • 0031892439 scopus 로고    scopus 로고
    • Cloning and expression of mRNA for calpain Lp82 from rat lens: Splice variant of p94
    • Ma, H., Fukiage, C., Azuma, M. and Shearer, T. R. (1998) Cloning and expression of mRNA for calpain Lp82 from rat lens: splice variant of p94. Invest. Ophthalmol. Vis. Sci. 39, 454-461 (Pubitemid 28093887)
    • (1998) Investigative Ophthalmology and Visual Science , vol.39 , Issue.2 , pp. 454-461
    • Ma, H.1    Fukiage, C.2    Azuma, M.3    Shearer, T.R.4
  • 20
    • 34948817818 scopus 로고    scopus 로고
    • Stomach-specific calpain, nCL-2/calpain 8, is active without calpain regulatory subunit and oligomerizes through C2-like domains
    • DOI 10.1074/jbc.M703168200
    • Hata, S., Doi, N., Kitamura, F. and Sorimachi, H. (2007) Stomach-specific calpain, nCL-2/calpain 8, is active without calpain regulatory subunit and oligomerizes through C2-like domains. J. Biol. Chem. 282, 27847-27856 (Pubitemid 47529505)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.38 , pp. 27847-27856
    • Hata, S.1    Doi, N.2    Kitamura, F.3    Sorimachi, H.4
  • 21
    • 77957341192 scopus 로고    scopus 로고
    • Calpain 8/nCL-2 and calpain 9/nCL-4 constitute an active protease complex, G-calpain, involved in gastric mucosal defense
    • Hata, S., Abe, M., Suzuki, H., Kitamura, F., Toyama-Sorimachi, N., Abe, K., Sakimura, K. and Sorimachi, H. (2010) Calpain 8/nCL-2 and calpain 9/nCL-4 constitute an active protease complex, G-calpain, involved in gastric mucosal defense. PLoS Genet. 6, e1001040
    • (2010) PLoS Genet. , vol.6
    • Hata, S.1    Abe, M.2    Suzuki, H.3    Kitamura, F.4    Toyama-Sorimachi, N.5    Abe, K.6    Sakimura, K.7    Sorimachi, H.8
  • 22
    • 0036499475 scopus 로고    scopus 로고
    • A novel human small subunit of calpains
    • DOI 10.1042/0264-6021:3620383
    • Schad, E., Farkas, A., Jekely, G., Tompa, P. and Friedrich, P. (2002) A novel human small subunit of calpains. Biochem. J. 362, 383-388 (Pubitemid 34214480)
    • (2002) Biochemical Journal , vol.362 , Issue.2 , pp. 383-388
    • Schad, E.1    Farkas, A.2    Jekely, G.3    Tompa, P.4    Friedrich, P.5
  • 23
    • 0033573028 scopus 로고    scopus 로고
    • 2+-dependent protease activity and a novel mode of enzyme activation
    • 2+-dependent protease activity and a novel mode of enzyme activation. EMBO J. 18, 6880-6889
    • (1999) EMBO J , vol.18 , pp. 6880-6889
    • Hosfield, C.M.1    Elce, J.S.2    Davies, P.L.3    Jia, Z.4
  • 26
    • 84859426282 scopus 로고    scopus 로고
    • MEROPS: The database of proteolytic enzymes, their substrates and inhibitors
    • Rawlings, N. D., Barrett, A. J. and Bateman, A. (2012) MEROPS: the database of proteolytic enzymes, their substrates and inhibitors. Nucleic Acids Res. 40, D343-D350
    • (2012) Nucleic Acids Res , vol.40
    • Rawlings, N.D.1    Barrett, A.J.2    Bateman, A.3
  • 27
    • 77951132229 scopus 로고    scopus 로고
    • The C2 domains of classical and novel PKCs as versatile decoders of membrane signals
    • Corbalan-Garcia, S. and Gomez-Fernandez, J. C. (2010) The C2 domains of classical and novel PKCs as versatile decoders of membrane signals. Biofactors 36, 1-7
    • (2010) Biofactors , vol.36 , pp. 1-7
    • Corbalan-Garcia, S.1    Gomez-Fernandez, J.C.2
  • 29
    • 56749172400 scopus 로고    scopus 로고
    • Calcium-bound structure of calpain and its mechanism of inhibition by calpastatin
    • Hanna, R. A., Campbell, R. L. and Davies, P. L. (2008) Calcium-bound structure of calpain and its mechanism of inhibition by calpastatin. Nature 456, 409-412
    • (2008) Nature , vol.456 , pp. 409-412
    • Hanna, R.A.1    Campbell, R.L.2    Davies, P.L.3
  • 30
    • 56749143763 scopus 로고    scopus 로고
    • Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains
    • Moldoveanu, T., Gehring, K. and Green, D. R. (2008) Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains. Nature 456, 404-408
    • (2008) Nature , vol.456 , pp. 404-408
    • Moldoveanu, T.1    Gehring, K.2    Green, D.R.3
  • 32
    • 82755189495 scopus 로고    scopus 로고
    • Calpains: An elaborate proteolytic system
    • Ono, Y. and Sorimachi, H. (2012) Calpains: an elaborate proteolytic system. Biochim. Biophys. Acta 1824, 224-236
    • (2012) Biochim. Biophys. Acta , vol.1824 , pp. 224-236
    • Ono, Y.1    Sorimachi, H.2
  • 33
  • 34
  • 35
    • 0031696884 scopus 로고    scopus 로고
    • Skeletal muscle-specific calpain, p49: Structure and physiological function
    • Kinbara, K., Sorimachi, H., Ishiura, S. and Suzuki, K. (1998) Skeletal muscle-specific calpain, p49: structure and physiological function. Biochem. Pharmacol. 56, 415-420
    • (1998) Biochem. Pharmacol. , vol.56 , pp. 415-420
    • Kinbara, K.1    Sorimachi, H.2    Ishiura, S.3    Suzuki, K.4
  • 36
    • 20544440116 scopus 로고    scopus 로고
    • Homodimerization of calpain 3 penta-EF-hand domain
    • DOI 10.1042/BJ20041821
    • Ravulapalli, R., Diaz, B. G., Campbell, R. L. and Davies, P. L. (2005) Homodimerization of calpain 3 penta-EF-hand domain. Biochem. J. 388, 585-591 (Pubitemid 40839936)
    • (2005) Biochemical Journal , vol.388 , Issue.2 , pp. 585-591
    • Ravulapalli, R.1    Diaz, B.G.2    Campbell, R.L.3    Davies, P.L.4
  • 37
    • 79959301027 scopus 로고    scopus 로고
    • Calpain chronicle - An enzyme family under multidisciplinary characterization
    • Sorimachi, H., Hata, S. and Ono, Y. (2011) Calpain chronicle - an enzyme family under multidisciplinary characterization. Proc. Jpn. Acad. Ser. B 87, 287-327
    • (2011) Proc. Jpn. Acad. Ser. B , vol.87 , pp. 287-327
    • Sorimachi, H.1    Hata, S.2    Ono, Y.3
  • 38
    • 26244434596 scopus 로고    scopus 로고
    • Regulating cell migration: Calpains make the cut
    • DOI 10.1242/jcs.02562
    • Franco, S. J. and Huttenlocher, A. (2005) Regulating cell migration: calpains make the cut. J. Cell Sci. 118, 3829-3838 (Pubitemid 41410267)
    • (2005) Journal of Cell Science , vol.118 , Issue.17 , pp. 3829-3838
    • Franco, S.J.1    Huttenlocher, A.2
  • 39
    • 33746155723 scopus 로고    scopus 로고
    • Calpain involvement in the remodeling of cytoskeletal anchorage complexes
    • Lebart, M. C. and Benyamin, Y. (2006) Calpain involvement in the remodeling of cytoskeletal anchorage complexes. FEBS J. 273, 3415-3426
    • (2006) FEBS J , vol.273 , pp. 3415-3426
    • Lebart, M.C.1    Benyamin, Y.2
  • 40
    • 77951242361 scopus 로고    scopus 로고
    • Regulation of adhesion dynamics by calpain-mediated proteolysis of focal adhesion kinase (FAK)
    • Chan, K. T., Bennin, D. A. and Huttenlocher, A. (2010) Regulation of adhesion dynamics by calpain-mediated proteolysis of focal adhesion kinase (FAK). J. Biol. Chem. 285, 11418-11426
    • (2010) J. Biol. Chem. , vol.285 , pp. 11418-11426
    • Chan, K.T.1    Bennin, D.A.2    Huttenlocher, A.3
  • 42
    • 75649115390 scopus 로고    scopus 로고
    • Actin-binding protein-1 interacts with WASp-interacting protein to regulate growth factor-induced dorsal ruffle formation
    • Cortesio, C. L., Perrin, B. J., Bennin, D. A. and Huttenlocher, A. (2010) Actin-binding protein-1 interacts with WASp-interacting protein to regulate growth factor-induced dorsal ruffle formation. Mol. Biol. Cell 21, 186-197
    • (2010) Mol. Biol. Cell , vol.21 , pp. 186-197
    • Cortesio, C.L.1    Perrin, B.J.2    Bennin, D.A.3    Huttenlocher, A.4
  • 43
    • 70349653079 scopus 로고    scopus 로고
    • Calcium pumps in health and disease
    • Brini, M. and Carafoli, E. (2009) Calcium pumps in health and disease. Physiol. Rev. 89, 1341-1378
    • (2009) Physiol. Rev. , vol.89 , pp. 1341-1378
    • Brini, M.1    Carafoli, E.2
  • 44
    • 78649634982 scopus 로고    scopus 로고
    • Genetic control of necrosis - Another type of programmed cell death
    • McCall, K. (2010) Genetic control of necrosis - another type of programmed cell death. Curr. Opin. Cell Biol. 22, 882-888
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 882-888
    • McCall, K.1
  • 49
    • 77949469511 scopus 로고    scopus 로고
    • Calpains: Attractive targets for the development of synthetic inhibitors
    • Pietsch, M., Chua, K. C. and Abell, A. D. (2010) Calpains: attractive targets for the development of synthetic inhibitors. Curr. Top. Med. Chem. 10, 270-293
    • (2010) Curr. Top. Med. Chem. , vol.10 , pp. 270-293
    • Pietsch, M.1    Chua, K.C.2    Abell, A.D.3
  • 50
    • 33644897573 scopus 로고    scopus 로고
    • Calpain inhibition: A therapeutic strategy targeting multiple disease states
    • Carragher, N. O. (2006) Calpain inhibition: a therapeutic strategy targeting multiple disease states. Curr. Pharm. Des. 12, 615-638
    • (2006) Curr. Pharm. Des. , vol.12 , pp. 615-638
    • Carragher, N.O.1
  • 51
    • 79955106083 scopus 로고    scopus 로고
    • Calpain inhibitors: A survey of compounds reported in the patent and scientific literature
    • Donkor, I. O. (2011) Calpain inhibitors: a survey of compounds reported in the patent and scientific literature. Expert Opin. Ther. Pat. 21, 601-636
    • (2011) Expert Opin. Ther. Pat. , vol.21 , pp. 601-636
    • Donkor, I.O.1
  • 53
    • 0035919730 scopus 로고    scopus 로고
    • Domain II of m-calpain is a Ca2 + -dependent cysteine protease
    • Hata, S., Sorimachi, H., Nakagawa, K., Maeda, T., Abe, K. and Suzuki, K. (2001) Domain II of m-calpain is a Ca2 + -dependent cysteine protease. FEBS Lett. 501, 111-114
    • (2001) FEBS Lett. , vol.501 , pp. 111-114
    • Hata, S.1    Sorimachi, H.2    Nakagawa, K.3    Maeda, T.4    Abe, K.5    Suzuki, K.6
  • 55
    • 0022918253 scopus 로고
    • Structure and function of the small (30K) subunit of calcium-activated neutral protease (CANP)
    • Suzuki, K., Emori, Y., Ohno, S., Imahori, S., Kawasaki, H. and Miyake, S. (1986) Structure and function of the small (30K) subunit of calcium-activated neutral protease (CANP). Biomed. Biochim. Acta 45, 1487-1491 (Pubitemid 17018580)
    • (1986) Biomedica Biochimica Acta , vol.45 , Issue.11-12 , pp. 1487-1491
    • Suzuki, K.1    Emori, Y.2    Ohno, S.3
  • 56
    • 0035200353 scopus 로고    scopus 로고
    • Dissociation of m-calpain subunits occurs after autolysis of the N-terminus of the catalytic subunit, and is not required for activation
    • Nakagawa, K., Masumoto, H., Sorimachi, H. and Suzuki, K. (2001) Dissociation of m-calpain subunits occurs after autolysis of the N-terminus of the catalytic subunit, and is not required for activation. J. Biochem. 130, 605-611 (Pubitemid 33115526)
    • (2001) Journal of Biochemistry , vol.130 , Issue.5 , pp. 605-611
    • Nakagawa, K.1    Masumoto, H.2    Sorimachi, H.3    Suzuki, K.4
  • 59
    • 0032557553 scopus 로고    scopus 로고
    • Molecular and functional properties of a calpain activator protein specific for mu-isoforms
    • DOI 10.1074/jbc.273.21.12827
    • Melloni, E., Michetti, M., Salamino, F. and Pontremoli, S. (1998) Molecular and functional properties of a calpain activator protein specific for mu-isoforms. J. Biol. Chem. 273, 12827-12831 (Pubitemid 28246838)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.21 , pp. 12827-12831
    • Melloni, E.1    Michetti, M.2    Salamino, F.3    Pontremoli, S.4
  • 60
    • 4644303903 scopus 로고    scopus 로고
    • DUK114, tin Drosophila orthologue of bovine brain calpain activator protein, is a molecular chaperone
    • DOI 10.1042/BJ20040668
    • Farkas, A., Nardai, G., Csermely, P., Tompa, P. and Friedrich, P. (2004) DUK114, the Drosophila orthologue of bovine brain calpain activator protein, is a molecular chaperone. Biochem. J. 383, 165-170 (Pubitemid 39389462)
    • (2004) Biochemical Journal , vol.383 , Issue.1 , pp. 165-170
    • Farkas, A.1    Nardai, G.2    Csermely, P.3    Tompa, P.4    Friedrich, P.5
  • 62
    • 0029862431 scopus 로고    scopus 로고
    • Purification of active calpain by affinity chromatography on an immobilized peptide inhibitor
    • Anagli, J., Vilei, E. M., Molinari, M., Calderara, S. and Carafoli, E. (1996) Purification of active calpain by affinity chromatography on an immobilized peptide inhibitor. Eur. J. Biochem. 241, 948-954 (Pubitemid 26379401)
    • (1996) European Journal of Biochemistry , vol.241 , Issue.3 , pp. 948-954
    • Anagli, J.1    Vilei, E.M.2    Molinari, M.3    Calderara, S.4    Carafoli, E.5
  • 64
    • 0035861569 scopus 로고    scopus 로고
    • Dissociation and aggregation of calpain in the presence of calcium
    • Pal, G. P., Elce, J. S. and Jia, Z. (2001) Dissociation and aggregation of calpain in the presence of calcium. J. Biol. Chem. 276, 47233-47238
    • (2001) J. Biol. Chem. , vol.276 , pp. 47233-47238
    • Pal, G.P.1    Elce, J.S.2    Jia, Z.3
  • 65
    • 1542344328 scopus 로고    scopus 로고
    • Epidermal Growth Factor Activates m-Calpain (Calpain II), at Least in Part, by Extracellular Signal-Regulated Kinase-Mediated Phosphorylation
    • DOI 10.1128/MCB.24.6.2499-2512.2004
    • Glading, A., Bodnar, R. J., Reynolds, I. J., Shiraha, H., Satish, L., Potter, D. A., Blair, H. C. and Wells, A. (2004) Epidermal growth factor activates m-calpain (calpain II), at least in part, by extracellular signal-regulated kinase-mediated phosphorylation. Mol. Cell. Biol. 24, 2499-2512 (Pubitemid 38326004)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.6 , pp. 2499-2512
    • Glading, A.1    Bodnar, R.J.2    Reynolds, I.J.3    Shiraha, H.4    Satish, L.5    Potter, D.A.6    Blair, H.C.7    Wells, A.8
  • 67
    • 0027417774 scopus 로고
    • 2+ sensitivity on activation of m-calpain
    • 2+ sensitivity on activation of m-calpain. FEBS Lett. 322, 65-68
    • (1993) FEBS Lett. , vol.322 , pp. 65-68
    • Brown, N.1    Crawford, C.2
  • 70
    • 79957607207 scopus 로고    scopus 로고
    • m-Calpain activation in vitro does not require autolysis or subunit dissociation
    • Chou, J. S., Impens, F., Gevaert, K. and Davies, P. L. (2011) m-Calpain activation in vitro does not require autolysis or subunit dissociation. Biochim. Biophys. Acta 1814, 864-872
    • (2011) Biochim. Biophys. Acta , vol.1814 , pp. 864-872
    • Chou, J.S.1    Impens, F.2    Gevaert, K.3    Davies, P.L.4
  • 72
    • 0023479147 scopus 로고
    • The effects of autolysis on the structure of chicken calpain II
    • Crawford, C., Willis, A. C. and Gagnon, J. (1987) The effects of autolysis on the structure of chicken calpain II. Biochem. J. 248, 579-588
    • (1987) Biochem. J. , vol.248 , pp. 579-588
    • Crawford, C.1    Willis, A.C.2    Gagnon, J.3
  • 73
    • 0022971268 scopus 로고
    • Autoproteolysis of the small subunit of calcium-dependent protease II activates and regulates protease activity
    • DeMartino, G. N., Huff, C. A. and Croall, D. E. (1986) Autoproteolysis of the small subunit of calcium-dependent protease II activates and regulates protease activity. J. Biol. Chem. 261, 12047-12052 (Pubitemid 17202762)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.26 , pp. 12047-12052
    • DeMartino, G.N.1    Huff, C.A.2    Croall, D.E.3
  • 74
    • 0028908947 scopus 로고
    • A catalytic subunit of calpain possesses full proteolytic activity
    • Yoshizawa, T., Sorimachi, H., Tomioka, S., Ishiura, S. and Suzuki, K. (1995) A catalytic subunit of calpain possesses full proteolytic activity. FEBS Lett. 358, 101-103
    • (1995) FEBS Lett. , vol.358 , pp. 101-103
    • Yoshizawa, T.1    Sorimachi, H.2    Tomioka, S.3    Ishiura, S.4    Suzuki, K.5
  • 75
    • 0031839786 scopus 로고    scopus 로고
    • A novel aspect of calpain activation
    • DOI 10.1016/S0014-5793(98)00856-4, PII S0014579398008564
    • Suzuki, K. and Sorimachi, H. (1998) A novel aspect of calpain activation. FEBS Lett. 433, 1-4 (Pubitemid 28386719)
    • (1998) FEBS Letters , vol.433 , Issue.1-2 , pp. 1-4
    • Suzuki, K.1    Sorimachi, H.2
  • 76
    • 0030599354 scopus 로고    scopus 로고
    • Calpain subunits remain associated during catalysis
    • Zhang, W. and Mellgren, R. L. (1996) Calpain subunits remain associated during catalysis. Biochem. Biophys. Res. Commun. 227, 891-896
    • (1996) Biochem. Biophys. Res. Commun. , vol.227 , pp. 891-896
    • Zhang, W.1    Mellgren, R.L.2
  • 77
    • 0031787140 scopus 로고    scopus 로고
    • m-Calpain subunits remain associated in the presence of calcium
    • DOI 10.1016/S0014-5793(98)01167-3, PII S0014579398011673
    • Dutt, P., Arthur, J. S., Croall, D. E. and Elce, J. S. (1998) m-Calpain subunits remain associated in the presence of calcium. FEBS Lett. 436, 367-371 (Pubitemid 28482963)
    • (1998) FEBS Letters , vol.436 , Issue.3 , pp. 367-371
    • Dutt, P.1    Arthur, J.S.C.2    Croall, D.E.3    Elce, J.S.4
  • 81
    • 0029165075 scopus 로고
    • Active site residues in m-calpain: Identification by site-directed mutagenesis
    • Arthur, J. S., Gauthier, S. and Elce, J. S. (1995) Active site residues in m-calpain: identification by site-directed mutagenesis. FEBS Lett. 368, 397-400
    • (1995) FEBS Lett. , vol.368 , pp. 397-400
    • Arthur, J.S.1    Gauthier, S.2    Elce, J.S.3
  • 82
    • 0028880896 scopus 로고
    • Recombinant calpain II: Improved expression systems and production of a C105A active-site mutant for crystallography
    • Elce, J. S., Hegadorn, C., Gauthier, S., Vince, J. W. and Davies, P. L. (1995) Recombinant calpain II: improved expression systems and production of a C105A active-site mutant for crystallography. Protein Eng. 8, 843-848
    • (1995) Protein Eng. , vol.8 , pp. 843-848
    • Elce, J.S.1    Hegadorn, C.2    Gauthier, S.3    Vince, J.W.4    Davies, P.L.5
  • 84
    • 37249053219 scopus 로고    scopus 로고
    • Fetuin A stabilizes m-calpain and facilitates plasma membrane repair
    • DOI 10.1074/jbc.M706929200
    • Mellgren, R. L. and Huang, X. (2007) Fetuin A stabilizes m-calpain and facilitates plasma membrane repair. J. Biol. Chem. 282, 35868-35877 (Pubitemid 350277142)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.49 , pp. 35868-35877
    • Mellgren, R.L.1    Huang, X.2
  • 86
    • 18144407551 scopus 로고    scopus 로고
    • Calpain mediates excitotoxic DNA fragmentation via mitochondrial pathways in adult brains: Evidence from calpastatin mutant mice
    • DOI 10.1074/jbc.M414552200
    • Takano, J., Tomioka, M., Tsubuki, S., Higuchi, M., Iwata, N., Itohara, S., Maki, M. and Saido, T. C. (2005) Calpain mediates excitotoxic DNA fragmentation via mitochondrial pathways in adult brains: evidence from calpastatin mutant mice. J. Biol. Chem. 280, 16175-16184 (Pubitemid 40616744)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.16 , pp. 16175-16184
    • Takano, J.1    Tomioka, M.2    Tsubuki, S.3    Higuchi, M.4    Iwata, N.5    Itohara, S.6    Maki, M.7    Saido, T.C.8
  • 87
    • 17644393902 scopus 로고    scopus 로고
    • Distinct mechanistic roles of calpain and caspase activation in neurodegeneration as revealed in mice overexpressing their specific inhibitors
    • DOI 10.1074/jbc.M500939200
    • Higuchi, M., Tomioka, M., Takano, J., Shirotani, K., Iwata, N., Masumoto, H., Maki, M., Itohara, S. and Saido, T. C. (2005) Distinct mechanistic roles of calpain and caspase activation in neurodegeneration as revealed in mice overexpressing their specific inhibitors. J. Biol. Chem. 280, 15229-15237 (Pubitemid 40562879)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.15 , pp. 15229-15237
    • Higuchi, M.1    Tomioka, M.2    Takano, J.3    Shirotani, K.4    Iwata, N.5    Masumoto, H.6    Maki, M.7    Itohara, S.8    Saido, T.C.9
  • 88
    • 58149397537 scopus 로고    scopus 로고
    • Marked calpastatin (CAST) depletion in Alzheimer's disease accelerates cytoskeleton disruption and neurodegeneration: Neuroprotection by CAST overexpression
    • Rao, M. V., Mohan, P. S., Peterhoff, C. M., Yang, D. S., Schmidt, S. D., Stavrides, P. H., Campbell, J., Chen, Y., Jiang, Y., Paskevich, P. A. et al. (2008) Marked calpastatin (CAST) depletion in Alzheimer's disease accelerates cytoskeleton disruption and neurodegeneration: neuroprotection by CAST overexpression. J. Neurosci. 28, 12241-12254
    • (2008) J. Neurosci. , vol.28 , pp. 12241-12254
    • Rao, M.V.1    Mohan, P.S.2    Peterhoff, C.M.3    Yang, D.S.4    Schmidt, S.D.5    Stavrides, P.H.6    Campbell, J.7    Chen, Y.8    Jiang, Y.9    Paskevich, P.A.10
  • 90
    • 6344285318 scopus 로고    scopus 로고
    • Crystal structures of calpain-E64 and -leupeptin inhibitor complexes reveal mobile loops gating the active site
    • DOI 10.1016/j.jmb.2004.09.016, PII S0022283604011453
    • Moldoveanu, T., Campbell, R. L., Cuerrier, D. and Davies, P. L. (2004) Crystal structures of calpain-E64 and -leupeptin inhibitor complexes reveal mobile loops gating the active site. J. Mol. Biol. 343, 1313-1326 (Pubitemid 39387829)
    • (2004) Journal of Molecular Biology , vol.343 , Issue.5 , pp. 1313-1326
    • Moldoveanu, T.1    Campbell, R.L.2    Cuerrier, D.3    Davies, P.L.4
  • 91
    • 33745165901 scopus 로고    scopus 로고
    • Calpain inhibition by á-ketoamide and cyclic hemiacetal inhibitors revealed by X-ray crystallography
    • DOI 10.1021/bi060425j
    • Cuerrier, D., Moldoveanu, T., Inoue, J., Davies, P. L. and Campbell, R. L. (2006) Calpain inhibition by á -ketoamide and cyclic hemiacetal inhibitors revealed by X-ray crystallography. Biochemistry 45, 7446-7452 (Pubitemid 43894938)
    • (2006) Biochemistry , vol.45 , Issue.24 , pp. 7446-7452
    • Cuerrier, D.1    Moldoveanu, T.2    Inoue, J.3    Davies, P.L.4    Campbell, R.L.5
  • 93
    • 51849085222 scopus 로고    scopus 로고
    • Cocrystal structures of primed side-extending á -ketoamide inhibitors reveal novel calpain-inhibitor aromatic interactions
    • Qian, J., Cuerrier, D., Davies, P. L., Li, Z., Powers, J. C. and Campbell, R. L. (2008) Cocrystal structures of primed side-extending á -ketoamide inhibitors reveal novel calpain-inhibitor aromatic interactions. J. Med. Chem. 51, 5264-5270
    • (2008) J. Med. Chem. , vol.51 , pp. 5264-5270
    • Qian, J.1    Cuerrier, D.2    Davies, P.L.3    Li, Z.4    Powers, J.C.5    Campbell, R.L.6
  • 94
    • 31044454547 scopus 로고    scopus 로고
    • Molecular mode of action of a covalently inhibiting peptidomimetic on the human calpain protease core
    • DOI 10.1021/bi052077b
    • Li, Q., Hanzlik, R. P., Weaver, R. F. and Schonbrunn, E. (2006) Molecular mode of action of a covalently inhibiting peptidomimetic on the human calpain protease core. Biochemistry 45, 701-708 (Pubitemid 43122235)
    • (2006) Biochemistry , vol.45 , Issue.3 , pp. 701-708
    • Li, Q.1    Hanzlik, R.P.2    Weaver, R.F.3    Schonbrunn, E.4
  • 95
    • 33846268347 scopus 로고    scopus 로고
    • The Crystal Structures of Human Calpains 1 and 9 Imply Diverse Mechanisms of Action and Auto-inhibition
    • DOI 10.1016/j.jmb.2006.11.037, PII S0022283606015774
    • Davis, T. L., Walker, J. R., Finerty, Jr, P. J., Mackenzie, F., Newman, E. M. and Dhe-Paganon, S. (2007) The crystal structures of human calpains 1 and 9 imply diverse mechanisms of action and auto-inhibition. J. Mol. Biol. 366, 216-229 (Pubitemid 46123340)
    • (2007) Journal of Molecular Biology , vol.366 , Issue.1 , pp. 216-229
    • Davis, T.L.1    Walker, J.R.2    Finerty Jr., P.J.3    Mackenzie, F.4    Newman, E.M.5    Dhe-Paganon, S.6
  • 97
    • 0034946412 scopus 로고    scopus 로고
    • Determination of protease cleavage site motifs using mixture-based oriented peptide libraries
    • DOI 10.1038/90273
    • Turk, B. E., Huang, L. L., Piro, E. T. and Cantley, L. C. (2001) Determination of protease cleavage site motifs using mixture-based oriented peptide libraries. Nat. Biotechnol. 19, 661-667 (Pubitemid 32625438)
    • (2001) Nature Biotechnology , vol.19 , Issue.7 , pp. 661-667
    • Turk, B.E.1    Huang, L.L.2    Piro, E.T.3    Cantley, L.C.4
  • 98
    • 28844491633 scopus 로고    scopus 로고
    • Determination of peptide substrate specificity for mu-calpain by a peptide library-based approach: The importance of primed side interactions
    • DOI 10.1074/jbc.M506870200
    • Cuerrier, D., Moldoveanu, T. and Davies, P. L. (2005) Determination of peptide substrate specificity for mu-calpain by a peptide library-based approach: the importance of primed side interactions. J. Biol. Chem. 280, 40632-40641 (Pubitemid 41780554)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.49 , pp. 40632-40641
    • Cuerrier, D.1    Moldoveanu, T.2    Davies, P.L.3
  • 100
    • 0033644756 scopus 로고    scopus 로고
    • Expression of m-calpain in Escherichia coli
    • Elce, J. S. (2000) Expression of m-calpain in Escherichia coli. Methods Mol. Biol. 144, 47-54
    • (2000) Methods Mol. Biol. , vol.144 , pp. 47-54
    • Elce, J.S.1
  • 101
    • 0031755539 scopus 로고    scopus 로고
    • Overexpression, purification, and characterization of human m-calpain and its active site mutant, m-C105S-calpain, using a baculovirus expression system
    • Masumoto, H., Yoshizawa, T., Sorimachi, H., Nishino, T., Ishiura, S. and Suzuki, K. (1998) 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 (Pubitemid 28544906)
    • (1998) Journal of Biochemistry , vol.124 , Issue.5 , pp. 957-961
    • Masumoto, H.1    Yoshizawa, T.2    Sorimachi, H.3    Nishino, T.4    Ishiura, S.5    Suzuki, K.6
  • 102
    • 84859298336 scopus 로고    scopus 로고
    • Efficient expression and purification of recombinant human m-calpain using an Escherichia coli expression system at low temperature
    • Hata, S., Ueno, M., Kitamura, F. and Sorimachi, H. (2012) Efficient expression and purification of recombinant human m-calpain using an Escherichia coli expression system at low temperature. J. Biochem. 151, 417-422
    • (2012) J. Biochem. , vol.151 , pp. 417-422
    • Hata, S.1    Ueno, M.2    Kitamura, F.3    Sorimachi, H.4
  • 103
    • 3442884354 scopus 로고    scopus 로고
    • 2+ Requirement
    • DOI 10.1016/j.str.2003.11.007
    • Pal, G. P., De Veyra, T., Elce, J. S. and Jia, Z. (2003) Crystal structure of a micro-like calpain reveals a partially activated conformation with low Ca2+ requirement. Structure 11, 1521-1526 (Pubitemid 37510351)
    • (2003) Structure , vol.11 , Issue.12 , pp. 1521-1526
    • Pal, G.P.1    De Veyra, T.2    Elce, J.S.3    Jia, Z.4
  • 104
    • 3042597817 scopus 로고    scopus 로고
    • Insertion sequence 1 of muscle-specific calpain, p94, acts as an internal propeptide
    • DOI 10.1074/jbc.M313290200
    • Diaz, B. G., Moldoveanu, T., Kuiper, M. J., Campbell, R. L. and Davies, P. L. (2004) Insertion sequence 1 of muscle-specific calpain, p94, acts as an internal propeptide. J. Biol. Chem. 279, 27656-27666 (Pubitemid 38812607)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.26 , pp. 27656-27666
    • Diaz, B.G.1    Moldoveanu, T.2    Kuiper, M.J.3    Campbell, R.L.4    Davies, P.L.5
  • 105
    • 3242798339 scopus 로고    scopus 로고
    • Interaction of calpastatin with calpain: A review
    • DOI 10.1515/BC.2004.054
    • Wendt, A., Thompson, V. F. and Goll, D. E. (2004) Interaction of calpastatin with calpain: a review. Biol. Chem. 385, 465-472 (Pubitemid 38967773)
    • (2004) Biological Chemistry , vol.385 , Issue.6 , pp. 465-472
    • Wendt, A.1    Thompson, V.F.2    Goll, D.E.3
  • 106
    • 34250201882 scopus 로고    scopus 로고
    • Calpastatin simultaneously binds four calpains with different kinetic constants
    • DOI 10.1016/j.febslet.2007.05.035, PII S0014579307005637
    • Hanna, R. A., Garcia-Diaz, B. E. and Davies, P. L. (2007) Calpastatin simultaneously binds four calpains with different kinetic constants. FEBS Lett. 581, 2894-2898 (Pubitemid 46899031)
    • (2007) FEBS Letters , vol.581 , Issue.16 , pp. 2894-2898
    • Hanna, R.A.1    Garcia-Diaz, B.E.2    Davies, P.L.3
  • 107
    • 46049100589 scopus 로고    scopus 로고
    • Local structural preferences of calpastatin, the intrinsically unstructured protein inhibitor of calpain
    • DOI 10.1021/bi800201a
    • Kiss, R., Kovacs, D., Tompa, P. and Perczel, A. (2008) Local structural preferences of calpastatin, the intrinsically unstructured protein inhibitor of calpain. Biochemistry 47, 6936-6945 (Pubitemid 351898948)
    • (2008) Biochemistry , vol.47 , Issue.26 , pp. 6936-6945
    • Kiss, R.1    Kovacs, D.2    Tompa, P.3    Perczel, A.4
  • 109
    • 1542267770 scopus 로고    scopus 로고
    • 18 Side Chains Play a Direct Role in Calpain Inhibition
    • DOI 10.1021/bi0359832
    • Betts, R. and Anagli, J. (2004) The β- and γ-CH2 of B27-WT's Leu11 and Ile18 side chains play a direct role in calpain inhibition. Biochemistry 43, 2596-2604 (Pubitemid 38327855)
    • (2004) Biochemistry , vol.43 , Issue.9 , pp. 2596-2604
    • Betts, R.1    Anagli, J.2
  • 110
    • 0037424522 scopus 로고    scopus 로고
    • Structural determinants of the calpain inhibitory activity of calpastatin peptide B27-WT
    • DOI 10.1074/jbc.M208350200
    • Betts, R., Weinsheimer, S., Blouse, G. E. and Anagli, J. (2003) Structural determinants of the calpain inhibitory activity of calpastatin peptide B27-WT. J. Biol. Chem. 278, 7800-7809 (Pubitemid 36800513)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.10 , pp. 7800-7809
    • Betts, R.1    Weinsheimer, S.2    Blouse, G.E.3    Anagli, J.4
  • 111
    • 0037453230 scopus 로고    scopus 로고
    • A structural model for the inhibition of calpain by calpastatin: Crystal structures of the native domain VI of calpain and its complexes with calpastatin peptide and a small molecule inhibitor
    • DOI 10.1016/S0022-2836(03)00274-2
    • Todd, B., Moore, D., Deivanayagam, C. C., Lin, G. D., Chattopadhyay, D., Maki, M., Wang, K. K. and Narayana, S. V. (2003) A structural model for the inhibition of by calpastatin: crystal structures of the native domain VI of calpain and its complexes with calpastatin peptide and a small molecule inhibitor. J. Mol. Biol. 328, 131-146 (Pubitemid 36390286)
    • (2003) Journal of Molecular Biology , vol.328 , Issue.1 , pp. 131-146
    • Todd, B.1    Moore, D.2    Deivanayagam, C.C.S.3    Lin, G.-D.4    Chattopadhyay, D.5    Maki, M.6    Wang, K.K.W.7    Narayana, S.V.L.8
  • 113
    • 47249105570 scopus 로고    scopus 로고
    • Multiple molecular interactions implicate the connectin/titin N2A region as a modulating scaffold for p94/calpain 3 activity in skeletal muscle
    • Hayashi, C., Ono, Y., Doi, N., Kitamura, F., Tagami, M., Mineki, R., Arai, T., Taguchi, H., Yanagida, M., Hirner, S. et al. (2008) Multiple molecular interactions implicate the connectin/titin N2A region as a modulating scaffold for p94/calpain 3 activity in skeletal muscle. J. Biol. Chem. 283, 14801-14814
    • (2008) J. Biol. Chem. , vol.283 , pp. 14801-14814
    • Hayashi, C.1    Ono, Y.2    Doi, N.3    Kitamura, F.4    Tagami, M.5    Mineki, R.6    Arai, T.7    Taguchi, H.8    Yanagida, M.9    Hirner, S.10
  • 115
    • 0037132543 scopus 로고    scopus 로고
    • 2+ -dependent intramolecular autolysis
    • 2+ -dependent intramolecular autolysis. FEBS Lett. 532, 401-406
    • (2002) FEBS Lett. , vol.532 , pp. 401-406
    • Rey, M.A.1    Davies, P.L.2
  • 117
    • 0035004517 scopus 로고    scopus 로고
    • Mutations in calpain 3 associated with limb girdle muscular dystrophy: Analysis by molecular modeling and by mutation in m-calpain
    • Jia, Z., Petrounevitch, V., Wong, A., Moldoveanu, T., Davies, P. L., Elce, J. S. and Beckmann, J. S. (2001) Mutations in calpain 3 associated with limb girdle muscular dystrophy: analysis by molecular modeling and by mutation in m-calpain. Biophys. J. 80, 2590-2596 (Pubitemid 32521635)
    • (2001) Biophysical Journal , vol.80 , Issue.6 , pp. 2590-2596
    • Jia, Z.1    Petrounevitch, V.2    Wong, A.3    Moldoveanu, T.4    Davies, P.L.5    Elce, J.S.6    Beckmann, J.S.7
  • 118
    • 65249122500 scopus 로고    scopus 로고
    • Limb-girdle muscular dystrophy type 2A can result from accelerated autoproteolytic inactivation of calpain 3
    • Garnham, C. P., Hanna, R. A., Chou, J. S., Low, K. E., Gourlay, K., Campbell, R. L., Beckmann, J. S. and Davies, P. L. (2009) Limb-girdle muscular dystrophy type 2A can result from accelerated autoproteolytic inactivation of calpain 3. Biochemistry 48, 3457-3467
    • (2009) Biochemistry , vol.48 , pp. 3457-3467
    • Garnham, C.P.1    Hanna, R.A.2    Chou, J.S.3    Low, K.E.4    Gourlay, K.5    Campbell, R.L.6    Beckmann, J.S.7    Davies, P.L.8
  • 120


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