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Volumn 1840, Issue 12, 2014, Pages 3367-3373

Allosteric inhibitors of calpains: Reevaluating inhibition by PD150606 and LSEAL

Author keywords

Allosteric inhibitor Calcium activated protease Calpain Penta EF hand PD150606 Enzyme kinetics

Indexed keywords

CALPAIN 1; CALPAIN 2; CALPASTATIN; CASEIN; LSEAL PEPTIDE; PD 150606; UNCLASSIFIED DRUG;

EID: 84907148946     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2014.08.014     Document Type: Article
Times cited : (22)

References (44)
  • 3
    • 33644897573 scopus 로고    scopus 로고
    • Calpain inhibition: A therapeutic strategy targeting multiple disease states
    • N. Carragher Calpain inhibition: a therapeutic strategy targeting multiple disease states Curr. Pharm. Des. 12 2006 615 638
    • (2006) Curr. Pharm. Des. , vol.12 , pp. 615-638
    • Carragher, N.1
  • 4
    • 33746126134 scopus 로고    scopus 로고
    • Implication of calpain in neuronal apoptosis
    • F. Raynaud, and A. Marcilhac Implication of calpain in neuronal apoptosis FEBS J. 273 2006 3437 3443
    • (2006) FEBS J. , vol.273 , pp. 3437-3443
    • Raynaud, F.1    Marcilhac, A.2
  • 5
    • 0028905205 scopus 로고
    • Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A
    • I. Richard, O. Broux, V. Allamand, F. Fougerousse, N. Chiannilkulchai, and N. Bourg Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A Cell 81 1995 27 40
    • (1995) Cell , vol.81 , pp. 27-40
    • Richard, I.1    Broux, O.2    Allamand, V.3    Fougerousse, F.4    Chiannilkulchai, N.5    Bourg, N.6
  • 6
    • 36148990505 scopus 로고    scopus 로고
    • The calpains: Modular designs and functional diversity
    • D.E. Croall, and K. Ersfeld The calpains: modular designs and functional diversity Genome Biol. 8 2007 218 10.1186/gb-2007-8-6-218
    • (2007) Genome Biol. , vol.8 , pp. 218
    • Croall, D.E.1    Ersfeld, K.2
  • 7
    • 79960104591 scopus 로고    scopus 로고
    • Impact of genetic insights into calpain biology
    • H. Sorimachi, S. Hata, and Y. Ono Impact of genetic insights into calpain biology J. Biochem. 150 2011 23 37 10.1093/jb/mvr070
    • (2011) J. Biochem. , vol.150 , pp. 23-37
    • Sorimachi, H.1    Hata, S.2    Ono, Y.3
  • 9
    • 84867270850 scopus 로고    scopus 로고
    • Structure-function relationships in calpains
    • R.L. Campbell, and P.L. Davies Structure-function relationships in calpains Biochem. J. 447 2012 335 351 10.1042/BJ20120921
    • (2012) Biochem. J. , vol.447 , pp. 335-351
    • Campbell, R.L.1    Davies, P.L.2
  • 10
    • 56749172400 scopus 로고    scopus 로고
    • Calcium-bound structure of calpain and its mechanism of inhibition by calpastatin
    • R.A. Hanna, R.L. Campbell, and P.L. Davies Calcium-bound structure of calpain and its mechanism of inhibition by calpastatin Nature 456 2008 409 412
    • (2008) Nature , vol.456 , pp. 409-412
    • Hanna, R.A.1    Campbell, R.L.2    Davies, P.L.3
  • 11
    • 56749143763 scopus 로고    scopus 로고
    • Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains
    • T. Moldoveanu, K. Gehring, and D.R. Green Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains Nature 456 2008 404 408
    • (2008) Nature , vol.456 , pp. 404-408
    • Moldoveanu, T.1    Gehring, K.2    Green, D.R.3
  • 13
    • 3242798339 scopus 로고    scopus 로고
    • Interaction of calpastatin with calpain: A review
    • A. Wendt, V.F. Thompson, and D.E. Goll Interaction of calpastatin with calpain: a review Biol. Chem. 385 2004 465 472 10.1515/BC.2004.054
    • (2004) Biol. Chem. , vol.385 , pp. 465-472
    • Wendt, A.1    Thompson, V.F.2    Goll, D.E.3
  • 14
  • 17
    • 0030963932 scopus 로고    scopus 로고
    • Crystal structure of calcium bound domain VI of calpain at 1.9 A resolution and its role in enzyme assembly, regulation, and inhibitor binding
    • G. Lin, D. Chattopadhyay, M. Maki, K. Wang, M. Carson, and L. Jin Crystal structure of calcium bound domain VI of calpain at 1.9 A resolution and its role in enzyme assembly, regulation, and inhibitor binding Nat. Struct. Biol. 4 1997 539
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 539
    • Lin, G.1    Chattopadhyay, D.2    Maki, M.3    Wang, K.4    Carson, M.5    Jin, L.6
  • 18
    • 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
    • B. Todd, D. Moore, C. Deivanayagam, G. Lin, D. Chattopadhyay, and M. Maki 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 J. Mol. Biol. 328 2003 131 146
    • (2003) J. Mol. Biol. , vol.328 , pp. 131-146
    • Todd, B.1    Moore, D.2    Deivanayagam, C.3    Lin, G.4    Chattopadhyay, D.5    Maki, M.6
  • 20
    • 57749181289 scopus 로고    scopus 로고
    • NMR structural characterization of the penta-peptide calpain inhibitor
    • L. Deshmukh, L. Wu, R.P. Guttmann, and O. Vinogradova NMR structural characterization of the penta-peptide calpain inhibitor FEBS Lett. 583 2009 135 140
    • (2009) FEBS Lett. , vol.583 , pp. 135-140
    • Deshmukh, L.1    Wu, L.2    Guttmann, R.P.3    Vinogradova, O.4
  • 21
    • 0028880896 scopus 로고
    • Recombinant calpain II: Improved expression systems and production of a C105A active-site mutant for crystallography
    • J.S. Elce, C. Hegadorn, S. Gauthier, J.W. Vince, and P.L. Davies Recombinant calpain II: improved expression systems and production of a C105A active-site mutant for crystallography Protein Eng. 8 1995 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
  • 23
    • 0033557480 scopus 로고    scopus 로고
    • Use of a fluorescence plate reader for measuring kinetic parameters with inner filter effect correction
    • Y. Liu, W. Kati, C.M. Chen, R. Tripathi, A. Molla, and W. Kohlbrenner Use of a fluorescence plate reader for measuring kinetic parameters with inner filter effect correction Anal. Biochem. 267 1999 331 335
    • (1999) Anal. Biochem. , vol.267 , pp. 331-335
    • Liu, Y.1    Kati, W.2    Chen, C.M.3    Tripathi, R.4    Molla, A.5    Kohlbrenner, W.6
  • 24
    • 0029828717 scopus 로고    scopus 로고
    • Interaction of aspartic acid-104 and proline-287 with the active site of m-calpain
    • J.S. Arthur, and J.S. Elce Interaction of aspartic acid-104 and proline-287 with the active site of m-calpain Biochem. J. 319 1996 535
    • (1996) Biochem. J. , vol.319 , pp. 535
    • Arthur, J.S.1    Elce, J.S.2
  • 25
    • 33750470057 scopus 로고    scopus 로고
    • Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination
    • M. Vedadi, F.H. Niesen, A. Allali-Hassani, O.Y. Fedorov, P.J. Finerty, and G.A. Wasney Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination Proc. Natl. Acad. Sci. 103 2006 15835 15840 10.1073/pnas.0605224103
    • (2006) Proc. Natl. Acad. Sci. , vol.103 , pp. 15835-15840
    • Vedadi, M.1    Niesen, F.H.2    Allali-Hassani, A.3    Fedorov, O.Y.4    Finerty, P.J.5    Wasney, G.A.6
  • 26
    • 0001396685 scopus 로고
    • The slow-binding and slow, tight-binding inhibition of enzyme-catalysed reactions
    • J.F. Morrison The slow-binding and slow, tight-binding inhibition of enzyme-catalysed reactions Trends Biochem. Sci. 7 1982 102 105 10.1016/0968-0004(82)90157-8
    • (1982) Trends Biochem. Sci. , vol.7 , pp. 102-105
    • Morrison, J.F.1
  • 27
    • 0034086654 scopus 로고    scopus 로고
    • Evaluation of a minimal experimental design for determination of enzyme kinetic parameters and inhibition mechanism
    • T. Kakkar, Y. Pak, and M. Mayersohn Evaluation of a minimal experimental design for determination of enzyme kinetic parameters and inhibition mechanism J. Pharmacol. Exp. Ther. 293 2000 861 869
    • (2000) J. Pharmacol. Exp. Ther. , vol.293 , pp. 861-869
    • Kakkar, T.1    Pak, Y.2    Mayersohn, M.3
  • 28
    • 0023677846 scopus 로고
    • Analysis of structure-function relationship of pig calpastatin by expression of mutated cDNAs in Escherichia coli
    • M. Maki, E. Takano, T. Osawa, T. Ooi, T. Murachi, and M. Hatanaka Analysis of structure-function relationship of pig calpastatin by expression of mutated cDNAs in Escherichia coli J. Biol. Chem. 263 1988 10254 10261
    • (1988) J. Biol. Chem. , vol.263 , pp. 10254-10261
    • Maki, M.1    Takano, E.2    Osawa, T.3    Ooi, T.4    Murachi, T.5    Hatanaka, M.6
  • 29
    • 0037088661 scopus 로고    scopus 로고
    • Calpastatin subdomains A and C are activators of calpain
    • P. Tompa, Z. Mucsi, G. Orosz, and P. Friedrich Calpastatin subdomains A and C are activators of calpain J. Biol. Chem. 277 2002 9022 9026 10.1074/jbc.C100700200
    • (2002) J. Biol. Chem. , vol.277 , pp. 9022-9026
    • Tompa, P.1    Mucsi, Z.2    Orosz, G.3    Friedrich, P.4
  • 30
    • 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 1999 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
  • 31
    • 0025934130 scopus 로고
    • Structure of the active 27-residue fragment of human calpastatin
    • R. Ishima, A. Tamura, K. Akasaka, K. Hamaguchi, K. Makino, and T. Murachi Structure of the active 27-residue fragment of human calpastatin FEBS Lett. 294 1991 64 66 10.1016/0014-5793(91)81344-8
    • (1991) FEBS Lett. , vol.294 , pp. 64-66
    • Ishima, R.1    Tamura, A.2    Akasaka, K.3    Hamaguchi, K.4    Makino, K.5    Murachi, T.6
  • 32
    • 0021658956 scopus 로고
    • Allostery without conformational change
    • A. Cooper, and D.T.F. Dryden Allostery without conformational change Eur. Biophys. J. 11 1984 103 109 10.1007/BF00276625
    • (1984) Eur. Biophys. J. , vol.11 , pp. 103-109
    • Cooper, A.1    Dryden, D.T.F.2
  • 33
    • 84898993517 scopus 로고    scopus 로고
    • The ensemble nature of allostery
    • H.N. Motlagh, J.O. Wrabl, J. Li, and V.J. Hilser The ensemble nature of allostery Nature 508 2014 331 339 10.1038/nature13001
    • (2014) Nature , vol.508 , pp. 331-339
    • Motlagh, H.N.1    Wrabl, J.O.2    Li, J.3    Hilser, V.J.4
  • 34
    • 33745165901 scopus 로고    scopus 로고
    • Calpain Inhibition by [alpha]-ketoamide and cyclic hemiacetal inhibitors revealed by X-ray crystallography
    • D. Cuerrier, T. Moldoveanu, J. Inoue, P. Davies, and R.L. Campbell Calpain Inhibition by [alpha]-ketoamide and cyclic hemiacetal inhibitors revealed by X-ray crystallography Biochemistry 45 2006 7446 7452
    • (2006) Biochemistry , vol.45 , pp. 7446-7452
    • Cuerrier, D.1    Moldoveanu, T.2    Inoue, J.3    Davies, P.4    Campbell, R.L.5
  • 35
    • 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
    • K. Nakagawa, H. Masumoto, H. Sorimachi, and K. Suzuki 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 2001 605 611
    • (2001) J. Biochem. , vol.130 , pp. 605-611
    • Nakagawa, K.1    Masumoto, H.2    Sorimachi, H.3    Suzuki, K.4
  • 38
    • 0027360303 scopus 로고
    • Studies of the active site of m-calpain and the interaction with calpastatin
    • C. Crawford, N.R. Brown, and A.C. Willis Studies of the active site of m-calpain and the interaction with calpastatin Biochem. J. 296 Pt 1 1993 135 142
    • (1993) Biochem. J. , vol.296 , Issue.1 , pp. 135-142
    • Crawford, C.1    Brown, N.R.2    Willis, A.C.3
  • 39
    • 0031787140 scopus 로고    scopus 로고
    • M-calpain subunits remain associated in the presence of calcium
    • P. Dutt, J.S. Arthur, D.E. Croall, and J.S. Elce m-calpain subunits remain associated in the presence of calcium FEBS Lett. 436 1998 367 371
    • (1998) FEBS Lett. , vol.436 , pp. 367-371
    • Dutt, P.1    Arthur, J.S.2    Croall, D.E.3    Elce, J.S.4
  • 40
    • 0030883152 scopus 로고    scopus 로고
    • The effects of truncations of the small subunit on m-calpain activity and heterodimer formation
    • J.S. Elce, P.L. Davies, C. Hegadorn, D.H. Maurice, and J.S. Arthur The effects of truncations of the small subunit on m-calpain activity and heterodimer formation Biochem. J. 326 Pt 1 1997 31 38
    • (1997) Biochem. J. , vol.326 , Issue.1 , pp. 31-38
    • Elce, J.S.1    Davies, P.L.2    Hegadorn, C.3    Maurice, D.H.4    Arthur, J.S.5
  • 41
    • 0030599354 scopus 로고    scopus 로고
    • Calpain subunits remain associated during catalysis
    • W. Zhang, and R.L. Mellgren Calpain subunits remain associated during catalysis Biochem. Biophys. Res. Commun. 227 1996 891 896
    • (1996) Biochem. Biophys. Res. Commun. , vol.227 , pp. 891-896
    • Zhang, W.1    Mellgren, R.L.2


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