메뉴 건너뛰기




Volumn 276, Issue 4, 2009, Pages 973-982

Distinguishing between calpain heterodimerization and homodimerization

Author keywords

Calcium; Calpain; Dimerization; EF hand protease

Indexed keywords

CALPAIN; CALPAIN 1; CALPAIN 13; CALPAIN 3; CALPAIN 9; CALPASTATIN; HETERODIMER; HOMODIMER; UNCLASSIFIED DRUG;

EID: 58849161891     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06833.x     Document Type: Article
Times cited : (18)

References (51)
  • 2
    • 0026779059 scopus 로고
    • Purification and characterization of a Ca(2+)-activated thiol protease from Drosophila melanogaster
    • Pinter M, Stierandova A Friedrich P (1992) Purification and characterization of a Ca(2+)-activated thiol protease from Drosophila melanogaster. Biochemistry 31, 8201 8206.
    • (1992) Biochemistry , vol.31 , pp. 8201-8206
    • Pinter, M.1    Stierandova, A.2    Friedrich, P.3
  • 3
    • 0029834118 scopus 로고    scopus 로고
    • The tra-3 sex determination gene of Caenorhabditis elegans encodes a member of the calpain regulatory protease family
    • Barnes TM Hodgkin J (1996) The tra-3 sex determination gene of Caenorhabditis elegans encodes a member of the calpain regulatory protease family. EMBO J 15, 4477 4484.
    • (1996) EMBO J , vol.15 , pp. 4477-4484
    • Barnes, T.M.1    Hodgkin, J.2
  • 4
    • 0037452506 scopus 로고    scopus 로고
    • Purification and properties of the Dictyostelium calpain-like protein, Cpl
    • Huang X, Czerwinski E Mellgren RL (2003) Purification and properties of the Dictyostelium calpain-like protein, Cpl. Biochemistry 42, 1789 1795.
    • (2003) Biochemistry , vol.42 , pp. 1789-1795
    • Huang, X.1    Czerwinski, E.2    Mellgren, R.L.3
  • 5
    • 0038274765 scopus 로고    scopus 로고
    • Phytocalpains: Orthologous calcium-dependent cysteine proteinases
    • Margis R Margis-Pinheiro M (2003) Phytocalpains: orthologous calcium-dependent cysteine proteinases. Trends Plant Sci 8, 58 62.
    • (2003) Trends Plant Sci , vol.8 , pp. 58-62
    • Margis, R.1    Margis-Pinheiro, M.2
  • 6
    • 0031259933 scopus 로고    scopus 로고
    • A new subfamily of vertebrate calpains lacking a calmodulin-like domain: Implications for calpain regulation and evolution
    • Dear N, Matena K, Vingron M Boehm T (1997) A new subfamily of vertebrate calpains lacking a calmodulin-like domain: implications for calpain regulation and evolution. Genomics 45, 175 184.
    • (1997) Genomics , vol.45 , pp. 175-184
    • Dear, N.1    Matena, K.2    Vingron, M.3    Boehm, T.4
  • 7
    • 28244461606 scopus 로고    scopus 로고
    • Evolutionary relationships and protein domain architecture in an expanded calpain superfamily in kinetoplastid parasites
    • Ersfeld K, Barraclough H Gull K (2005) Evolutionary relationships and protein domain architecture in an expanded calpain superfamily in kinetoplastid parasites. J Mol Evol 61, 742 757.
    • (2005) J Mol Evol , vol.61 , pp. 742-757
    • Ersfeld, K.1    Barraclough, H.2    Gull, K.3
  • 8
    • 0037810356 scopus 로고    scopus 로고
    • Revisiting ubiquity and tissue specificity of human calpains
    • Farkas A, Tompa P Friedrich P (2003) Revisiting ubiquity and tissue specificity of human calpains. Biol Chem 384, 945 949.
    • (2003) Biol Chem , vol.384 , pp. 945-949
    • Farkas, A.1    Tompa, P.2    Friedrich, P.3
  • 9
    • 0036168356 scopus 로고    scopus 로고
    • Cutting to the chase: Calpain proteases in cell motility
    • Glading A, Lauffenburger DA Wells A (2002) Cutting to the chase: calpain proteases in cell motility. Trends Cell Biol 12, 46 54.
    • (2002) Trends Cell Biol , vol.12 , pp. 46-54
    • Glading, A.1    Lauffenburger, D.A.2    Wells, A.3
  • 10
    • 0037648485 scopus 로고    scopus 로고
    • Cross-talk between calpain and caspase proteolytic systems during neuronal apoptosis
    • Neumar RW, Xu YA, Gada H, Guttmann RP Siman R (2003) Cross-talk between calpain and caspase proteolytic systems during neuronal apoptosis. J Biol Chem 278, 14162 14167.
    • (2003) J Biol Chem , vol.278 , pp. 14162-14167
    • Neumar, R.W.1    Xu, Y.A.2    Gada, H.3    Guttmann, R.P.4    Siman, R.5
  • 13
    • 0842263992 scopus 로고    scopus 로고
    • Linkage of calpain 10 to type 2 diabetes: The biological rationale
    • Cox NJ, Hayes MG, Roe CA, Tsuchiya T Bell GI (2004) Linkage of calpain 10 to type 2 diabetes: the biological rationale. Diabetes 53 (Suppl. 1 S19 S25.
    • (2004) Diabetes , vol.53 , Issue.1
    • Cox, N.J.1    Hayes, M.G.2    Roe, C.A.3    Tsuchiya, T.4    Bell, G.I.5
  • 14
    • 0037112117 scopus 로고    scopus 로고
    • Activation of calpain in cultured neurons overexpressing Alzheimer amyloid precursor protein
    • Kuwako K, Nishimura I, Uetsuki T, Saido TC Yoshikawa K (2002) Activation of calpain in cultured neurons overexpressing Alzheimer amyloid precursor protein. Brain Res Mol Brain Res 107, 166 175.
    • (2002) Brain Res Mol Brain Res , vol.107 , pp. 166-175
    • Kuwako, K.1    Nishimura, I.2    Uetsuki, T.3    Saido, T.C.4    Yoshikawa, K.5
  • 17
    • 0034079985 scopus 로고    scopus 로고
    • Isolation of two novel genes, down-regulated in gastric cancer
    • Yoshikawa Y, Mukai H, Hino F, Asada K Kato I (2000) Isolation of two novel genes, down-regulated in gastric cancer. Jpn J Cancer Res 91, 459 463.
    • (2000) Jpn J Cancer Res , vol.91 , pp. 459-463
    • Yoshikawa, Y.1    Mukai, H.2    Hino, F.3    Asada, K.4    Kato, I.5
  • 18
    • 0027988820 scopus 로고
    • Calpain inhibition: An overview of its therapeutic potential
    • Wang KK Yuen PW (1994) Calpain inhibition: an overview of its therapeutic potential. Trends Pharmacol Sci 15, 412 419.
    • (1994) Trends Pharmacol Sci , vol.15 , pp. 412-419
    • Wang, K.K.1    Yuen, P.W.2
  • 19
    • 0033573028 scopus 로고    scopus 로고
    • Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation
    • Hosfield CM, Elce JS, Davies PL Jia Z (1999) Crystal structure of calpain reveals the structural basis for Ca(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
  • 25
    • 0842328803 scopus 로고    scopus 로고
    • Structure, activation, and biology of calpain
    • Suzuki K, Hata S, Kawabata Y Sorimachi H (2004) Structure, activation, and biology of calpain. Diabetes 53 (Suppl. 1 S12 S18.
    • (2004) Diabetes , vol.53 , Issue.1
    • Suzuki, K.1    Hata, S.2    Kawabata, Y.3    Sorimachi, H.4
  • 28
    • 46349101338 scopus 로고    scopus 로고
    • Human calpain 7/PalBH associates with a subset of ESCRT-III-related proteins in its N-terminal region and partly localizes to endocytic membrane compartments
    • Yorikawa C, Takaya E, Osako Y, Tanaka R, Terasawa Y, Hamakubo T, Mochizuki Y, Iwanari H, Kodama T, Maeda T et al. (2008) Human calpain 7/PalBH associates with a subset of ESCRT-III-related proteins in its N-terminal region and partly localizes to endocytic membrane compartments. J Biochem 143, 731 745.
    • (2008) J Biochem , vol.143 , pp. 731-745
    • Yorikawa, C.1    Takaya, E.2    Osako, Y.3    Tanaka, R.4    Terasawa, Y.5    Hamakubo, T.6    Mochizuki, Y.7    Iwanari, H.8    Kodama, T.9    Maeda, T.10
  • 29
    • 47749115368 scopus 로고    scopus 로고
    • Characterization of endogenous and recombinant human calpain-10
    • Dong B Liu R (2008) Characterization of endogenous and recombinant human calpain-10. Biochimie 90, 1362 1371.
    • (2008) Biochimie , vol.90 , pp. 1362-1371
    • Dong, B.1    Liu, R.2
  • 32
    • 3242798339 scopus 로고    scopus 로고
    • Interaction of calpastatin with calpain: A review
    • Wendt A, Thompson VF Goll DE (2004) Interaction of calpastatin with calpain: a review. Biol Chem 385, 465 472.
    • (2004) Biol Chem , vol.385 , pp. 465-472
    • Wendt, A.1    Thompson, V.F.2    Goll, D.E.3
  • 33
    • 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
    • Todd B, Moore D, Deivanayagam CC, Lin GD, Chattopadhyay D, Maki M, Wang KK Narayana SV (2003) 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, 131 146.
    • (2003) J Mol Biol , vol.328 , pp. 131-146
    • Todd, B.1    Moore, D.2    Deivanayagam, C.C.3    Lin, G.D.4    Chattopadhyay, D.5    Maki, M.6    Wang, K.K.7    Narayana, S.V.8
  • 34
    • 56749172400 scopus 로고    scopus 로고
    • Calcium-bound structure of calpain and its mechanism of inhibition by calpastatin
    • Hanna RA, Campbell RL Davies PL (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
  • 35
    • 0029856558 scopus 로고    scopus 로고
    • Structural basis for the binding of a globular antifreeze protein to ice
    • Jia Z, DeLuca CI, Chao H Davies PL (1996) Structural basis for the binding of a globular antifreeze protein to ice. Nature 384, 285 288.
    • (1996) Nature , vol.384 , pp. 285-288
    • Jia, Z.1    Deluca, C.I.2    Chao, H.3    Davies, P.L.4
  • 38
    • 0030998285 scopus 로고    scopus 로고
    • Structure of a calpain Ca(2+)-binding domain reveals a novel EF-hand and Ca(2+)-induced conformational changes
    • Blanchard H, Grochulski P, Li Y, Arthur JS, Davies PL, Elce JS Cygler M (1997) Structure of a calpain Ca(2+)-binding domain reveals a novel EF-hand and Ca(2+)-induced conformational changes. Nat Struct Biol 4, 532 538.
    • (1997) Nat Struct Biol , vol.4 , pp. 532-538
    • Blanchard, H.1    Grochulski, P.2    Li, Y.3    Arthur, J.S.4    Davies, P.L.5    Elce, J.S.6    Cygler, M.7
  • 40
    • 1242351264 scopus 로고    scopus 로고
    • Structures, functions and molecular evolution of the penta-EF-hand Ca2+-binding proteins
    • Maki M, Kitaura Y, Satoh H, Ohkouchi S Shibata H (2002) Structures, functions and molecular evolution of the penta-EF-hand Ca2+-binding proteins. Biochim Biophys Acta 1600, 51 60.
    • (2002) Biochim Biophys Acta , vol.1600 , pp. 51-60
    • Maki, M.1    Kitaura, Y.2    Satoh, H.3    Ohkouchi, S.4    Shibata, H.5
  • 41
    • 0034725530 scopus 로고    scopus 로고
    • Crystal structure of human grancalcin, a member of the penta-EF-hand protein family
    • Jia J, Han Q, Borregaard N, Lollike K Cygler M (2000) Crystal structure of human grancalcin, a member of the penta-EF-hand protein family. J Mol Biol 300, 1271 1281.
    • (2000) J Mol Biol , vol.300 , pp. 1271-1281
    • Jia, J.1    Han, Q.2    Borregaard, N.3    Lollike, K.4    Cygler, M.5
  • 42
    • 0029670455 scopus 로고    scopus 로고
    • Ca(2+)-binding domain VI of rat calpain is a homodimer in solution: Hydrodynamic, crystallization and preliminary X-ray diffraction studies
    • Blanchard H, Li Y, Cygler M, Kay CM, Simon J, Arthur C, Davies PL Elce JS (1996) Ca(2+)-binding domain VI of rat calpain is a homodimer in solution: hydrodynamic, crystallization and preliminary X-ray diffraction studies. Protein Sci 5, 535 537.
    • (1996) Protein Sci , vol.5 , pp. 535-537
    • Blanchard, H.1    Li, Y.2    Cygler, M.3    Kay, C.M.4    Simon, J.5    Arthur, C.6    Davies, P.L.7    Elce, J.S.8
  • 44
    • 28844450410 scopus 로고    scopus 로고
    • An improved method for fast, robust, and seamless integration of DNA fragments into multiple plasmids
    • Benoit RM, Wilhelm RN, Scherer-Becker D Ostermeier C (2006) An improved method for fast, robust, and seamless integration of DNA fragments into multiple plasmids. Protein Expr Purif 45, 66 71.
    • (2006) Protein Expr Purif , vol.45 , pp. 66-71
    • Benoit, R.M.1    Wilhelm, R.N.2    Scherer-Becker, D.3    Ostermeier, C.4
  • 45
    • 0028880896 scopus 로고
    • Recombinant calpain II: Improved expression systems and production of a C105A active-site mutant for crystallography
    • Elce JS, Hegadorn C, Gauthier S, Vince JW Davies PL (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
  • 46
    • 0027270959 scopus 로고
    • Use of proline mutants to help solve the NMR solution structure of type III antifreeze protein
    • Chao H, Davies PL, Sykes BD Sonnichsen FD (1993) Use of proline mutants to help solve the NMR solution structure of type III antifreeze protein. Protein Sci 2, 1411 1428.
    • (1993) Protein Sci , vol.2 , pp. 1411-1428
    • Chao, H.1    Davies, P.L.2    Sykes, B.D.3    Sonnichsen, F.D.4
  • 48
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4 (
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50, 760 763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 49
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A Blundell TL (1993) Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 234, 779 815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.