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Volumn 586, Issue 20, 2012, Pages 3582-3589

Structural insights into the calcium-dependent interaction between calbindin-D28K and caspase-3

Author keywords

Calbindin D28K; Caspase 3; Isothermal titration calorimetry; Molecular docking

Indexed keywords

CALBINDIN; CALCIUM; CASPASE 3;

EID: 84867579065     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.08.032     Document Type: Article
Times cited : (12)

References (30)
  • 1
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • J.F. Kerr, A.H. Wyllie, and A.R. Currie Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics Br. J. Cancer 26 1972 239 257
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 2
    • 0036598992 scopus 로고    scopus 로고
    • Targeting death and decoy receptors of the tumour-necrosis factor superfamily
    • A. Ashkenazi Targeting death and decoy receptors of the tumour-necrosis factor superfamily Nat. Rev. Cancer 2 2002 420 430
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 420-430
    • Ashkenazi, A.1
  • 3
    • 9344261615 scopus 로고    scopus 로고
    • The cytotoxic cell protease granzyme B initiates apoptosis in a cell-free system by proteolytic processing and activation of the ICE/CED-3 family protease, CPP32, via a novel two-step mechanism
    • S.J. Martin The cytotoxic cell protease granzyme B initiates apoptosis in a cell-free system by proteolytic processing and activation of the ICE/CED-3 family protease, CPP32, via a novel two-step mechanism EMBO J. 15 1996 2407 2416
    • (1996) EMBO J. , vol.15 , pp. 2407-2416
    • Martin, S.J.1
  • 4
    • 0034283578 scopus 로고    scopus 로고
    • Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8
    • H.R. Stennicke, M. Renatus, M. Meldal, and G.S. Salvesen Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8 Biochem. J. 350 Pt 2 2000 563 568
    • (2000) Biochem. J. , vol.350 , Issue.PART 2 , pp. 563-568
    • Stennicke, H.R.1    Renatus, M.2    Meldal, M.3    Salvesen, G.S.4
  • 5
    • 26444560960 scopus 로고    scopus 로고
    • Caspases: Pharmacological manipulation of cell death
    • I.N. Lavrik, A. Golks, and P.H. Krammer Caspases: pharmacological manipulation of cell death J. Clin. Invest. 115 2005 2665 2672
    • (2005) J. Clin. Invest. , vol.115 , pp. 2665-2672
    • Lavrik, I.N.1    Golks, A.2    Krammer, P.H.3
  • 7
    • 2942748646 scopus 로고    scopus 로고
    • Prevention of glucocorticoid-induced apoptosis in osteocytes and osteoblasts by calbindin-D28K
    • Y. Liu Prevention of glucocorticoid-induced apoptosis in osteocytes and osteoblasts by calbindin-D28K J. Bone Miner. Res. 19 2004 479 490
    • (2004) J. Bone Miner. Res. , vol.19 , pp. 479-490
    • Liu, Y.1
  • 8
    • 0026504821 scopus 로고
    • Calbindin-D28K-containing neurons in animal models of neurodegeneration: Possible protection from excitotoxicity
    • A. Iacopino, S. Christakos, D. German, P.K. Sonsalla, and C.A. Altar Calbindin-D28K-containing neurons in animal models of neurodegeneration: possible protection from excitotoxicity Brain Res. Mol. Brain Res. 13 1992 251 261
    • (1992) Brain Res. Mol. Brain Res. , vol.13 , pp. 251-261
    • Iacopino, A.1    Christakos, S.2    German, D.3    Sonsalla, P.K.4    Altar, C.A.5
  • 9
    • 0034713933 scopus 로고    scopus 로고
    • Calbindin-D28K is expressed in osteoblastic cells and suppresses their apoptosis by inhibiting caspase-3 activity
    • T. Bellido, M. Huening, M. Raval-Pandya, S.C. Manolagas, and S. Christakos Calbindin-D28K is expressed in osteoblastic cells and suppresses their apoptosis by inhibiting caspase-3 activity J. Biol. Chem. 275 2000 26328 26332
    • (2000) J. Biol. Chem. , vol.275 , pp. 26328-26332
    • Bellido, T.1    Huening, M.2    Raval-Pandya, M.3    Manolagas, S.C.4    Christakos, S.5
  • 10
    • 0037410215 scopus 로고    scopus 로고
    • The effects of Ca(2+) binding on the conformation of calbindin D(28K): A nuclear magnetic resonance and microelectrospray mass spectrometry study
    • R.A. Venters The effects of Ca(2+) binding on the conformation of calbindin D(28K): a nuclear magnetic resonance and microelectrospray mass spectrometry study Anal. Biochem. 317 2003 59 66
    • (2003) Anal. Biochem. , vol.317 , pp. 59-66
    • Venters, R.A.1
  • 13
    • 45549088468 scopus 로고    scopus 로고
    • Expression, purification, and characterization of caspases
    • J.B. Denault, G.S. Salvesen, Expression, purification, and characterization of caspases, Curr. Protoc. Protein Sci. 21 (2003) 13.
    • (2003) Curr. Protoc. Protein Sci. , vol.21 , pp. 13
    • Denault, J.B.1    Salvesen, G.S.2
  • 15
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: A protein-protein docking approach based on biochemical or biophysical information
    • C. Dominguez, R. Boelens, and A.M. Bonvin HADDOCK: a protein-protein docking approach based on biochemical or biophysical information J. Am. Chem. Soc. 125 2003 1731 1737
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.3
  • 18
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • R.A. Laskowski, J.A. Rullmannn, M.W. MacArthur, R. Kaptein, and J.M. Thornton AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR J. Biomol. NMR 8 1996 477 486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 19
    • 35748982413 scopus 로고    scopus 로고
    • Geometry-based sampling of conformational transitions in proteins
    • D. Seeliger, J. Haas, and B.L. de Groot Geometry-based sampling of conformational transitions in proteins Structure 15 2007 1482 1492
    • (2007) Structure , vol.15 , pp. 1482-1492
    • Seeliger, D.1    Haas, J.2    De Groot, B.L.3
  • 20
    • 33750690511 scopus 로고    scopus 로고
    • Role of loop bundle hydrogen bonds in the maturation and activity of (Pro)caspase-3
    • B. Feeney, C. Pop, P. Swartz, C. Mattos, and A.C. Clark Role of loop bundle hydrogen bonds in the maturation and activity of (Pro)caspase-3 Biochemistry 45 2006 13249 13263
    • (2006) Biochemistry , vol.45 , pp. 13249-13263
    • Feeney, B.1    Pop, C.2    Swartz, P.3    Mattos, C.4    Clark, A.C.5
  • 21
    • 79952351221 scopus 로고    scopus 로고
    • Expression of calbindin-D28K is inversely correlated with proapototic gene expression in hydrogen peroxide-induced cell death in endometrial cancer cells
    • E.M. Jung, K.C. Choi, and E.B. Jeung Expression of calbindin-D28K is inversely correlated with proapototic gene expression in hydrogen peroxide-induced cell death in endometrial cancer cells Int. J. Oncol. 38 2011 1059 1066
    • (2011) Int. J. Oncol. , vol.38 , pp. 1059-1066
    • Jung, E.M.1    Choi, K.C.2    Jeung, E.B.3
  • 22
    • 24744463641 scopus 로고    scopus 로고
    • Apoptotic signals within the basal forebrain cholinergic neurons in Alzheimer's disease
    • C.K. Wu, L. Thal, D. Pizzo, L. Hansen, E. Masliah, and C. Geula Apoptotic signals within the basal forebrain cholinergic neurons in Alzheimer's disease Exp. Neurol. 195 2005 484 496
    • (2005) Exp. Neurol. , vol.195 , pp. 484-496
    • Wu, C.K.1    Thal, L.2    Pizzo, D.3    Hansen, L.4    Masliah, E.5    Geula, C.6
  • 23
    • 33644935534 scopus 로고    scopus 로고
    • Expression of calbindin-D28K in sporadic nephroblastomas of the chicken
    • Y. Tsukamoto Expression of calbindin-D28K in sporadic nephroblastomas of the chicken Avian Dis. 50 2006 127 130
    • (2006) Avian Dis. , vol.50 , pp. 127-130
    • Tsukamoto, Y.1
  • 24
    • 77953808196 scopus 로고    scopus 로고
    • Evidence for the involvement of calbindin D28k in the presenilin 1 model of Alzheimer's disease
    • G.L. Odero Evidence for the involvement of calbindin D28k in the presenilin 1 model of Alzheimer's disease Neuroscience 169 2010 532 543
    • (2010) Neuroscience , vol.169 , pp. 532-543
    • Odero, G.L.1
  • 25
    • 83055176416 scopus 로고    scopus 로고
    • Calbindin-D28K inhibits apoptosis in dopaminergic neurons by activation of the PI3-kinase-Akt signaling pathway
    • S. Sun, F. Li, X. Gao, Y. Zhu, J. Chen, X. Zhu, H. Yuan, and D. Gao Calbindin-D28K inhibits apoptosis in dopaminergic neurons by activation of the PI3-kinase-Akt signaling pathway Neuroscience 199 2011 359 367
    • (2011) Neuroscience , vol.199 , pp. 359-367
    • Sun, S.1    Li, F.2    Gao, X.3    Zhu, Y.4    Chen, J.5    Zhu, X.6    Yuan, H.7    Gao, D.8
  • 26
    • 77956456526 scopus 로고    scopus 로고
    • Distribution patterns of calcium-binding proteins in pancreatic tissue of non-diabetic as well as type 2 diabetic rats and in rat insulinoma beta-cells (INS-1)
    • I. Bazwinsky-Wutschke, S. Wolgast, E. Muhlbauer, and E. Peschke Distribution patterns of calcium-binding proteins in pancreatic tissue of non-diabetic as well as type 2 diabetic rats and in rat insulinoma beta-cells (INS-1) Histochem. Cell Biol. 134 2010 115 127
    • (2010) Histochem. Cell Biol. , vol.134 , pp. 115-127
    • Bazwinsky-Wutschke, I.1    Wolgast, S.2    Muhlbauer, E.3    Peschke, E.4
  • 27
    • 0036668981 scopus 로고    scopus 로고
    • Intracellular calcium ion response to glucose in beta-cells of calbindin-D28K nullmutant mice and in betaHC13 cells overexpressing calbindin-D28K
    • J. Parkash, M.A. Chaudhry, A.S. Amer, S. Christakos, and W.B. Rhoten Intracellular calcium ion response to glucose in beta-cells of calbindin-D28K nullmutant mice and in betaHC13 cells overexpressing calbindin-D28K Endocrine 18 2002 221 229
    • (2002) Endocrine , vol.18 , pp. 221-229
    • Parkash, J.1    Chaudhry, M.A.2    Amer, A.S.3    Christakos, S.4    Rhoten, W.B.5
  • 28
    • 0031056634 scopus 로고    scopus 로고
    • Transfection and overexpression of the calcium binding protein calbindin-D28K results in a stimulatory effect on insulin synthesis in a rat beta cell line (RIN 1046-38)
    • D. Reddy, A.S. Pollock, S.A. Clark, K. Sooy, R.C. Vasavada, A.F. Stewart, T. Honeyman, and S. Christakos Transfection and overexpression of the calcium binding protein calbindin-D28K results in a stimulatory effect on insulin synthesis in a rat beta cell line (RIN 1046-38) Proc. Natl. Acad. Sci. U S A 94 1997 1961 1966
    • (1997) Proc. Natl. Acad. Sci. U S A , vol.94 , pp. 1961-1966
    • Reddy, D.1    Pollock, A.S.2    Clark, S.A.3    Sooy, K.4    Vasavada, R.C.5    Stewart, A.F.6    Honeyman, T.7    Christakos, S.8
  • 29
    • 79952452195 scopus 로고    scopus 로고
    • Thermodynamic, enzymatic and structural effects of removing a salt bridge at the base of loop 4 in (pro)caspase-3
    • J. Walters, P. Swartz, C. Mattos, and A.C. Clark Thermodynamic, enzymatic and structural effects of removing a salt bridge at the base of loop 4 in (pro)caspase-3 Arch. Biochem. Biophys. 508 2011 31 38
    • (2011) Arch. Biochem. Biophys. , vol.508 , pp. 31-38
    • Walters, J.1    Swartz, P.2    Mattos, C.3    Clark, A.C.4
  • 30
    • 61449175831 scopus 로고    scopus 로고
    • Structural and biochemical studies on procaspase-8: New insights on initiator caspase activation
    • N. Keller, J. Mares, O. Zerbe, and M.G. Grutter Structural and biochemical studies on procaspase-8: new insights on initiator caspase activation Structure 17 2009 438 448
    • (2009) Structure , vol.17 , pp. 438-448
    • Keller, N.1    Mares, J.2    Zerbe, O.3    Grutter, M.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.