메뉴 건너뛰기




Volumn 367, Issue 1, 2002, Pages 263-269

Origins of the difference in Ca2+ requirement for activation of μ- and m-calpain

Author keywords

EF hand; Hybrid calpain; Site directed mutagenesis

Indexed keywords

ASSAYS; PROTEINS; X RAY ANALYSIS;

EID: 0036796233     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20020485     Document Type: Article
Times cited : (30)

References (30)
  • 2
    • 0032540136 scopus 로고    scopus 로고
    • Structure and physiology of calpain, an enigmatic protease
    • Ono, Y., Sorimachi, H. and Suzuki, K. (1998) Structure and physiology of calpain, an enigmatic protease. Biochem. Biophys. Res. Commun. 245, 289-294
    • (1998) Biochem. Biophys. Res. Commun. , vol.245 , pp. 289-294
    • Ono, Y.1    Sorimachi, H.2    Suzuki, K.3
  • 3
    • 0026911137 scopus 로고
    • Is calpain activity regulated by membranes and autolysis or by calcium and calpastatin?
    • Goll, D. E., Thompson, V. F., Taylor, R. G. and Zalewska, T. (1992) Is calpain activity regulated by membranes and autolysis or by calcium and calpastatin? BioEssays 14, 549-556
    • (1992) BioEssays , vol.14 , pp. 549-556
    • Goll, D.E.1    Thompson, V.F.2    Taylor, R.G.3    Zalewska, T.4
  • 5
    • 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
  • 9
    • 0034657159 scopus 로고    scopus 로고
    • Roles of individual EF-hands in the activation of m-calpain by calcium
    • Dutt, P., Arthur, J. S., Grochulski, P., Cygler, M. and Elce, J. S. (2000) Roles of individual EF-hands in the activation of m-calpain by calcium. Biochem. J. 348, 37-43
    • (2000) Biochem. J. , vol.348 , pp. 37-43
    • Dutt, P.1    Arthur, J.S.2    Grochulski, P.3    Cygler, M.4    Elce, J.S.5
  • 10
    • 0035861569 scopus 로고    scopus 로고
    • Dissociation and aggregation of calpain in the presence of calcium
    • Pal, G. P., Elce, J. S. and Jia, Z. C. (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.C.3
  • 11
    • 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. (Tokyo) 130, 605-611
    • (2001) J. Biochem. (Tokyo) , vol.130 , pp. 605-611
    • Nakagawa, K.1    Masumoto, H.2    Sorimachi, H.3    Suzuki, K.4
  • 13
    • 0030963932 scopus 로고    scopus 로고
    • Crystal structure of calcium bound domain VI of calpain at 1.9 Å resolution and its role in enzyme assembly, regulation, and inhibitor binding
    • Lin, G. D., Chattopadhyay, D., Maki, M., Wang, K. K. W., Carson, M., Jin, L., Yuen, P.-W., Takano, E., Hatanaka, M., DeLucas, L. J. et al. (1997) Crystal structure of calcium bound domain VI of calpain at 1.9 Å resolution and its role in enzyme assembly, regulation, and inhibitor binding. Nat. Struct. Biol. 4, 539-547
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 539-547
    • Lin, G.D.1    Chattopadhyay, D.2    Maki, M.3    Wang, K.K.W.4    Carson, M.5    Jin, L.6    Yuen, P.-W.7    Takano, E.8    Hatanaka, M.9    DeLucas, L.J.10
  • 15
    • 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
  • 16
    • 0030580369 scopus 로고    scopus 로고
    • Primary sequences of rat μ-calpain large and small subunits are, respectively, moderately and highly similar to those of human
    • Sorimachi, H., Amano, S., Ishiura, S. and Suzuki, K. (1996) Primary sequences of rat μ-calpain large and small subunits are, respectively, moderately and highly similar to those of human. Biochim. Biophys. Acta 1309, 37-41
    • (1996) Biochim. Biophys. Acta , vol.1309 , pp. 37-41
    • Sorimachi, H.1    Amano, S.2    Ishiura, S.3    Suzuki, K.4
  • 17
    • 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
  • 18
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A. (1985) Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. U.S.A. 82, 488-492
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 19
    • 0029048989 scopus 로고
    • Casein zymography: A method to study μ-calpain, m-calpain, and their inhibitory agents
    • Raser, K. J., Posner, A. and Wang, K. K. W. (1995) Casein zymography: a method to study μ-calpain, m-calpain, and their inhibitory agents. Arch. Biochem. Biophys. 319, 211-216
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 211-216
    • Raser, K.J.1    Posner, A.2    Wang, K.K.W.3
  • 20
    • 0033650175 scopus 로고    scopus 로고
    • Calpain zymography with casein or fluorescein isothiocyanate casein
    • Arthur, J. S. and Mykles, D. L. (2000) Calpain zymography with casein or fluorescein isothiocyanate casein. Methods Mol. Biol. 144, 109-116
    • (2000) Methods Mol. Biol. , vol.144 , pp. 109-116
    • Arthur, J.S.1    Mykles, D.L.2
  • 21
  • 22
    • 0023943527 scopus 로고
    • Molecular and catalytic characterization of intact heterodimeric and derived monomeric calpains isolated under different conditions from pig polymorphonuclear leukocytes
    • Fukui, I., Toyohara, H., Ito, K., Hamakubo, T. and Murachi, T. (1988) Molecular and catalytic characterization of intact heterodimeric and derived monomeric calpains isolated under different conditions from pig polymorphonuclear leukocytes. Biochemistry 27, 3260-3267
    • (1988) Biochemistry , vol.27 , pp. 3260-3267
    • Fukui, I.1    Toyohara, H.2    Ito, K.3    Hamakubo, T.4    Murachi, T.5
  • 23
    • 0035940513 scopus 로고    scopus 로고
    • Long-range effects on calcium binding and conformational change in the N-domain of calmodulin
    • Ababou, A., Shenvi, R. A. and Desjarlais, J. R. (2001) Long-range effects on calcium binding and conformational change in the N-domain of calmodulin. Biochemistry 40, 12719-12726.
    • (2001) Biochemistry , vol.40 , pp. 12719-12726
    • Ababou, A.1    Shenvi, R.A.2    Desjarlais, J.R.3
  • 24
    • 0035107931 scopus 로고    scopus 로고
    • Solvation energetics and conformational change in EF-hand proteins
    • Ababou, A. and Desjarlais, J. R. (2001) Solvation energetics and conformational change in EF-hand proteins. Protein Sci. 10, 301-312
    • (2001) Protein Sci. , vol.10 , pp. 301-312
    • Ababou, A.1    Desjarlais, J.R.2
  • 26
  • 27
    • 0032708680 scopus 로고    scopus 로고
    • Diversity of conformational states and changes within the EF-hand protein superfamily
    • Yap, K. L., Ames, J. B, Swindells, M. B. and Ikura, M. (1999) Diversity of conformational states and changes within the EF-hand protein superfamily. Proteins: Struct. Funct. Genet. 37, 499-507
    • (1999) Proteins: Struct. Funct. Genet. , vol.37 , pp. 499-507
    • Yap, K.L.1    Ames, J.B.2    Swindells, M.B.3    Ikura, M.4
  • 28
    • 0030032040 scopus 로고    scopus 로고
    • Calcium binding and conformational response in EF-hand proteins
    • Ikura, M. (1996) Calcium binding and conformational response in EF-hand proteins. Trends Biochem. Sci. 21, 14-17
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 14-17
    • Ikura, M.1
  • 30
    • 0030774905 scopus 로고    scopus 로고
    • Functional properties of recombinant calpain I and of mutants lacking domains III and IV of the catalytic subunit
    • Vilei, E. M., Caiderara, S., Anagli, J., Berardi, S., Hitomi, K., Maki, M. and Carafoli, E. (1997) Functional properties of recombinant calpain I and of mutants lacking domains III and IV of the catalytic subunit. J. Biol. Chem. 272, 25802-25808
    • (1997) J. Biol. Chem. , vol.272 , pp. 25802-25808
    • Vilei, E.M.1    Caiderara, S.2    Anagli, J.3    Berardi, S.4    Hitomi, K.5    Maki, M.6    Carafoli, E.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.