메뉴 건너뛰기




Volumn 323, Issue 4, 2004, Pages 1131-1133

The intriguing Ca 2+ requirement of calpain activation

Author keywords

Calcium sensitivity; Calpains; Co operative calcium binding; Compartmentalization; Drosophila; Enzyme activation; Enzyme targeting

Indexed keywords

CALCIUM; CALPAIN; CYTOPLASM PROTEIN; PROTEINASE; ISOENZYME;

EID: 4644252460     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.08.194     Document Type: Short Survey
Times cited : (50)

References (30)
  • 1
    • 7044240676 scopus 로고    scopus 로고
    • The calpain system in Drosophila melanogaster: Coming of age
    • P. Friedrich, P. Tompa, and A. Farkas The calpain system in Drosophila melanogaster: coming of age BioEssays 26 2004 1 9
    • (2004) BioEssays , vol.26 , pp. 1-9
    • Friedrich, P.1    Tompa, P.2    Farkas, A.3
  • 2
    • 0029746476 scopus 로고    scopus 로고
    • Autolysis parallels activation of μ-calpain
    • A. Baki, P. Tompa, and A. Alexa Autolysis parallels activation of μ-calpain Biochem. J. 318 1996 897 901
    • (1996) Biochem. J. , vol.318 , pp. 897-901
    • Baki, A.1    Tompa, P.2    Alexa, A.3
  • 3
    • 0024340134 scopus 로고
    • 2+-dependent proteinases (mu-calpain and m-calpain)
    • 2+-dependent proteinases (mu-calpain and m-calpain) J. Biol. Chem. 264 1989 10096 10103
    • (1989) J. Biol. Chem. , vol.264 , pp. 10096-10103
    • Cong, J.1    Goll, D.E.2    Peterson, A.M.3
  • 5
    • 0039702848 scopus 로고    scopus 로고
    • Characterization of two recombinant Drosophila calpains: CALPA and a novel homolog CALPB
    • G. Jékely, and P. Friedrich Characterization of two recombinant Drosophila calpains: CALPA and a novel homolog CALPB J. Biol. Chem. 274 1999 23893 23900
    • (1999) J. Biol. Chem. , vol.274 , pp. 23893-23900
    • Jékely, G.1    Friedrich, P.2
  • 7
    • 0025096669 scopus 로고
    • Investigation of the structural basis of the interaction of calpain II with phospholipid and with carbohydrate
    • C. Crawford, N.R. Brown, and A.C. Willis Investigation of the structural basis of the interaction of calpain II with phospholipid and with carbohydrate Biochem. J. 265 1990 575 579
    • (1990) Biochem. J. , vol.265 , pp. 575-579
    • Crawford, C.1    Brown, N.R.2    Willis, A.C.3
  • 8
    • 0026542341 scopus 로고
    • Autolytic transition of μ-calpain upon activation as resolved by antibodies distinguishing between pre- and post-autolysis forms
    • T.C. Saido, S. Nagao, and M. Shiramine Autolytic transition of μ-calpain upon activation as resolved by antibodies distinguishing between pre- and post-autolysis forms J. Biochem. (Tokyo) 111 1992 81 86
    • (1992) J. Biochem. (Tokyo) , vol.111 , pp. 81-86
    • Saido, T.C.1    Nagao, S.2    Shiramine, M.3
  • 9
    • 0029922373 scopus 로고    scopus 로고
    • Investigation of the interaction of m-calpain with phospholipids: Calpain-phospholipid interactions
    • J.S.C. Arthur, and C. Crawford Investigation of the interaction of m-calpain with phospholipids: calpain-phospholipid interactions Biochim. Biophys. Acta 293 1996 201 206
    • (1996) Biochim. Biophys. Acta , vol.293 , pp. 201-206
    • Arthur, J.S.C.1    Crawford, C.2
  • 11
    • 0032557553 scopus 로고    scopus 로고
    • Molecular and functional properties of a calpain activator protein specific for μ-isoforms
    • E. Melloni, M. Michetti, and F. Salamino Molecular and functional properties of a calpain activator protein specific for μ-isoforms J. Biol. Chem. 273 1998 12827 12831
    • (1998) J. Biol. Chem. , vol.273 , pp. 12827-12831
    • Melloni, E.1    Michetti, M.2    Salamino, F.3
  • 12
    • 4644303903 scopus 로고    scopus 로고
    • DUK114, the Drosophila homolog of bovine brain calpain activator protein, is a molecular chaperone
    • in press
    • A. Farkas, G. Nardai, P. Csermely, et al., DUK114, the Drosophila homolog of bovine brain calpain activator protein, is a molecular chaperone, Biochem. J. (2004) (in press)
    • (2004) Biochem. J.
    • Farkas, A.1    Nardai, G.2    Csermely, P.3
  • 13
    • 3242761518 scopus 로고    scopus 로고
    • Calcium-mediated cellular signals: A story of failures
    • E. Carafoli Calcium-mediated cellular signals: a story of failures Trends Biochem. Sci. 29 2004 371 379
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 371-379
    • Carafoli, E.1
  • 15
    • 0842345408 scopus 로고    scopus 로고
    • On the origin of the ideas of intracellular compartmentation and organized metabolic systems
    • J. Ovádi, and V. Saks On the origin of the ideas of intracellular compartmentation and organized metabolic systems Mol. Cell. Biochem. 256 2004 5 12
    • (2004) Mol. Cell. Biochem. , vol.256 , pp. 5-12
    • Ovádi, J.1    Saks, V.2
  • 16
    • 0028274544 scopus 로고
    • Anchoring of protein kinase a is required for modulation of AMPA/kainate receptors on hippocampal neurons
    • C. Rosenmund, D.W. Carr, and S.E. Bergeson Anchoring of protein kinase A is required for modulation of AMPA/kainate receptors on hippocampal neurons Nature 368 1994 853 856
    • (1994) Nature , vol.368 , pp. 853-856
    • Rosenmund, C.1    Carr, D.W.2    Bergeson, S.E.3
  • 17
    • 0037447227 scopus 로고    scopus 로고
    • Bioinformatic design of A-kinase anchoring protein-in silico: Potent and selective peptide antagonist of type II protein kinase a anchoring
    • N.M. Alto, S.H. Soderling, and N. Hoshi Bioinformatic design of A-kinase anchoring protein-in silico: potent and selective peptide antagonist of type II protein kinase A anchoring Proc. Natl. Acad. Sci. USA 8 2003 4445 4450
    • (2003) Proc. Natl. Acad. Sci. USA , vol.8 , pp. 4445-4450
    • Alto, N.M.1    Soderling, S.H.2    Hoshi, N.3
  • 18
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • P. Tompa Intrinsically unstructured proteins Trends Biochem. Sci. 27 2002 527 533
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 527-533
    • Tompa, P.1
  • 19
    • 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
  • 20
    • 12944300453 scopus 로고    scopus 로고
    • The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium
    • S. Strobl, C. Fernandez-Catalan, and M. Braun The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium Proc. Natl. Acad. Sci. USA 97 2000 588 592
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 588-592
    • Strobl, S.1    Fernandez-Catalan, C.2    Braun, M.3
  • 24
    • 0034657159 scopus 로고    scopus 로고
    • Roles of individual EF-hands in the activation of m-calpain by calcium
    • P. Dutt, J.S.C. Arthur, and P. Grochulski Roles of individual EF-hands in the activation of m-calpain by calcium Biochem. J. 348 2000 37 43
    • (2000) Biochem. J. , vol.348 , pp. 37-43
    • Dutt, P.1    Arthur, J.S.C.2    Grochulski, P.3
  • 25
    • 4544368685 scopus 로고    scopus 로고
    • Electrostatic interactions of domain III stabilize the inactive conformation of μ-calpain
    • A. Fernández-Montalván, I. Assfalg-Machleidt, and D. Pfeiler Electrostatic interactions of domain III stabilize the inactive conformation of μ-calpain Biochem. J. 382 2004 9022 9026
    • (2004) Biochem. J. , vol.382 , pp. 9022-9026
    • Fernández-Montalván, A.1    Assfalg-Machleidt, I.2    Pfeiler, D.3
  • 26
    • 0035119650 scopus 로고    scopus 로고
    • Frequency decoding of fast calcium oscillations by calpain
    • P. Tompa, R. Toth-Boconadi, and P. Friedrich Frequency decoding of fast calcium oscillations by calpain Cell Calcium 29 2001 161 170
    • (2001) Cell Calcium , vol.29 , pp. 161-170
    • Tompa, P.1    Toth-Boconadi, R.2    Friedrich, P.3
  • 27
    • 0037088661 scopus 로고    scopus 로고
    • Calpastatin subdomains a and C are activators of calpain
    • P. Tompa, Z. Mucsi, and Gy. Orosz Calpastatin subdomains A and C are activators of calpain J. Biol. Chem. 277 2002 9022 9026
    • (2002) J. Biol. Chem. , vol.277 , pp. 9022-9026
    • Tompa, P.1    Mucsi, Z.2    Orosz, Gy.3
  • 28
    • 0024844775 scopus 로고
    • Inhibition of calpain by a synthetic oligopeptide corresponding to an exon of the human calpastatin gene
    • M. Maki, H. Bagci, and K. Hamaguchi Inhibition of calpain by a synthetic oligopeptide corresponding to an exon of the human calpastatin gene J. Biol. Chem. 264 1989 18866 18869
    • (1989) J. Biol. Chem. , vol.264 , pp. 18866-18869
    • Maki, M.1    Bagci, H.2    Hamaguchi, K.3
  • 29
    • 0037470789 scopus 로고    scopus 로고
    • Molecular cloning and RNA expression of a novel Drosophila calpain, Calpain C
    • C. Spadoni, A. Farkas, and R. Sinka Molecular cloning and RNA expression of a novel Drosophila calpain, Calpain C Biochem. Biophys. Res. Commun. 303 2003 343 349
    • (2003) Biochem. Biophys. Res. Commun. , vol.303 , pp. 343-349
    • Spadoni, C.1    Farkas, A.2    Sinka, R.3
  • 30
    • 2942700177 scopus 로고    scopus 로고
    • Inactive enzyme-homologues find new function in regulatory processes
    • B. Pils, and J. Schultz Inactive enzyme-homologues find new function in regulatory processes J. Mol. Biol. 340 2004 399 404
    • (2004) J. Mol. Biol. , vol.340 , pp. 399-404
    • Pils, B.1    Schultz, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.