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Volumn 49, Issue 19, 2010, Pages 4244-4254

Identification and inhibitory properties of a novel Ca2+/ calmodulin antagonist

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL INHIBITORS; HIGH-THROUGHPUT; IN-VITRO; ISOTHERMAL TITRATION CALORIMETRY; LIVING CELL; MITOGENS; TRIFLUOPERAZINE;

EID: 77952356292     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1001213     Document Type: Article
Times cited : (17)

References (53)
  • 2
    • 0034256090 scopus 로고    scopus 로고
    • Calmodulin: A prototypical calcium sensor
    • Chin, D. and Means, A. R. (2000) Calmodulin: A prototypical calcium sensor Trends Cell Biol. 10, 322-328
    • (2000) Trends Cell Biol. , vol.10 , pp. 322-328
    • Chin, D.1    Means, A.R.2
  • 5
    • 0038199737 scopus 로고    scopus 로고
    • Management of cellular energy by the AMP-activated protein kinase system
    • Hardie, D. G., Scott, J. W., Pan, D. A., and Hudson, E. R. (2003) Management of cellular energy by the AMP-activated protein kinase system FEBS Lett. 546, 113-120
    • (2003) FEBS Lett. , vol.546 , pp. 113-120
    • Hardie, D.G.1    Scott, J.W.2    Pan, D.A.3    Hudson, E.R.4
  • 7
    • 33748747706 scopus 로고    scopus 로고
    • Mammalian TAK1 activates Snf1 protein kinase in yeast and phosphorylates AMP-activated protein kinase in vitro
    • Momcilovic, M., Hong, S. P., and Carlson, M. (2006) Mammalian TAK1 Activates Snf1 Protein Kinase in Yeast and Phosphorylates AMP-activated Protein Kinase in Vitro J. Biol. Chem. 281, 25336-25343
    • (2006) J. Biol. Chem. , vol.281 , pp. 25336-25343
    • Momcilovic, M.1    Hong, S.P.2    Carlson, M.3
  • 9
    • 0031717105 scopus 로고    scopus 로고
    • The AMP-activated/SNF1 protein kinase subfamily: Metabolic sensors of the eukaryotic cell?
    • Hardie, D. G., Carling, D., and Carlson, M. (1998) The AMP-activated/SNF1 protein kinase subfamily: Metabolic sensors of the eukaryotic cell? Annu. Rev. Biochem. 67, 821-855
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 821-855
    • Hardie, D.G.1    Carling, D.2    Carlson, M.3
  • 10
    • 0037184937 scopus 로고    scopus 로고
    • Purification and characterization of Snf1 kinase complexes containing a defined β subunit composition
    • Nath, N., McCartney, R. R., and Schmidt, M. C. (2002) Purification and characterization of Snf1 kinase complexes containing a defined β subunit composition J. Biol. Chem. 277, 50403-50408
    • (2002) J. Biol. Chem. , vol.277 , pp. 50403-50408
    • Nath, N.1    McCartney, R.R.2    Schmidt, M.C.3
  • 11
    • 31544468889 scopus 로고    scopus 로고
    • Purification and characterization of the three Snf1-activating kinases of Saccharomyces cerevisiae
    • Elbing, K., McCartney, R. R., and Schmidt, M. C. (2006) Purification and characterization of the three Snf1-activating kinases of Saccharomyces cerevisiae Biochem. J. 393, 797-805
    • (2006) Biochem. J. , vol.393 , pp. 797-805
    • Elbing, K.1    McCartney, R.R.2    Schmidt, M.C.3
  • 13
    • 20444468520 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase kinase α as Snf1-activating kinases in yeast
    • 2+/calmodulin-dependent protein kinase kinase α as Snf1-activating kinases in yeast J. Biol. Chem. 280, 21804-21809
    • (2005) J. Biol. Chem. , vol.280 , pp. 21804-21809
    • Hong, S.P.1    Momcilovic, M.2    Carlson, M.3
  • 15
    • 0023006881 scopus 로고
    • Isolation of the yeast calmodulin gene: Calmodulin is an essential protein
    • Davis, T. N., Urdea, M. S., Masiarz, F. R., and Thorner, J. (1986) Isolation of the yeast calmodulin gene: Calmodulin is an essential protein Cell 47, 423-431
    • (1986) Cell , vol.47 , pp. 423-431
    • Davis, T.N.1    Urdea, M.S.2    Masiarz, F.R.3    Thorner, J.4
  • 16
    • 0035675838 scopus 로고    scopus 로고
    • Genetic analysis of calmodulin and its targets in Saccharomyces cerevisiae
    • Cyert, M. S. (2001) Genetic analysis of calmodulin and its targets in Saccharomyces cerevisiae Annu. Rev. Genet. 35, 647-672
    • (2001) Annu. Rev. Genet. , vol.35 , pp. 647-672
    • Cyert, M.S.1
  • 18
    • 33745232336 scopus 로고    scopus 로고
    • Channeling studies in yeast: Yeast as a model for channelopathies?
    • Wolfe, D. M. and Pearce, D. A. (2006) Channeling studies in yeast: Yeast as a model for channelopathies? NeuroMol. Med. 8, 279-306
    • (2006) NeuroMol. Med. , vol.8 , pp. 279-306
    • Wolfe, D.M.1    Pearce, D.A.2
  • 20
    • 0029994841 scopus 로고    scopus 로고
    • A new efficient gene disruption cassette for repeated use in budding yeast
    • Guldener, U., Heck, S., Fielder, T., Beinhauer, J., and Hegemann, J. H. (1996) A new efficient gene disruption cassette for repeated use in budding yeast Nucleic Acids Res. 24, 2519-2524
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2519-2524
    • Guldener, U.1    Heck, S.2    Fielder, T.3    Beinhauer, J.4    Hegemann, J.H.5
  • 21
    • 0032785638 scopus 로고    scopus 로고
    • Copper ion inducible and repressible promoter systems in yeast
    • Labbe, S. and Thiele, D. J. (1999) Copper ion inducible and repressible promoter systems in yeast Methods Enzymol. 306, 145-153
    • (1999) Methods Enzymol. , vol.306 , pp. 145-153
    • Labbe, S.1    Thiele, D.J.2
  • 23
    • 33845949733 scopus 로고    scopus 로고
    • Dissecting the role of 5′-AMP for allosteric stimulation, activation, and deactivation of AMP-activated protein kinase
    • Suter, M., Riek, U., Tuerk, R., Schlattner, U., Wallimann, T., and Neumann, D. (2006) Dissecting the role of 5′-AMP for allosteric stimulation, activation, and deactivation of AMP-activated protein kinase J. Biol. Chem. 281, 32207-32216
    • (2006) J. Biol. Chem. , vol.281 , pp. 32207-32216
    • Suter, M.1    Riek, U.2    Tuerk, R.3    Schlattner, U.4    Wallimann, T.5    Neumann, D.6
  • 25
    • 0033575222 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase i in the absence of activation loop phosphorylation
    • 2+/calmodulin-dependent protein kinase I in the absence of activation loop phosphorylation J. Biol. Chem. 274, 20215-20222
    • (1999) J. Biol. Chem. , vol.274 , pp. 20215-20222
    • Hook, S.S.1    Kemp, B.E.2    Means, A.R.3
  • 26
    • 0034463866 scopus 로고    scopus 로고
    • Chronic elevation of calmodulin in the ventricles of trasngenic mice increases the autonomous acivity of calmodulin-dependent protein kinase II, which regulates atrial natriuretic factor gene expression
    • Colomer, J. M. and Means, A. R. (2000) Chronic elevation of calmodulin in the ventricles of trasngenic mice increases the autonomous acivity of calmodulin-dependent protein kinase II, which regulates atrial natriuretic factor gene expression Mol. Endocrinol. 14, 1125-1136
    • (2000) Mol. Endocrinol. , vol.14 , pp. 1125-1136
    • Colomer, J.M.1    Means, A.R.2
  • 27
    • 0043071497 scopus 로고    scopus 로고
    • Mammalian AMP-activated protein kinase: Functional, heterotrimeric complexes by co-expression of subunits in Escherichia coli
    • Neumann, D., Woods, A., Carling, D., Wallimann, T., and Schlattner, U. (2003) Mammalian AMP-activated protein kinase: Functional, heterotrimeric complexes by co-expression of subunits in Escherichia coli Protein Expression Purif. 30, 230-237
    • (2003) Protein Expression Purif. , vol.30 , pp. 230-237
    • Neumann, D.1    Woods, A.2    Carling, D.3    Wallimann, T.4    Schlattner, U.5
  • 28
    • 0026782061 scopus 로고
    • Insulin activation of acetyl-CoA carboxylase accompanied by inhibition of the 5′-AMP-activated protein kinase
    • Witters, L. A. and Kemp, B. E. (1992) Insulin activation of acetyl-CoA carboxylase accompanied by inhibition of the 5′-AMP-activated protein kinase J. Biol. Chem. 267, 2864-2867
    • (1992) J. Biol. Chem. , vol.267 , pp. 2864-2867
    • Witters, L.A.1    Kemp, B.E.2
  • 29
    • 14744268745 scopus 로고    scopus 로고
    • Heat capacity effects in protein folding and ligand binding: A re-evaluation of the role of water in biomolecular thermodynamics
    • Cooper, A. (2005) Heat capacity effects in protein folding and ligand binding: A re-evaluation of the role of water in biomolecular thermodynamics Biophys. Chem. 115, 89-97
    • (2005) Biophys. Chem. , vol.115 , pp. 89-97
    • Cooper, A.1
  • 30
    • 0032901515 scopus 로고    scopus 로고
    • Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition
    • Jelesarov, I. and Bosshard, H. R. (1999) Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition J. Mol. Recognit. 12, 3-18
    • (1999) J. Mol. Recognit. , vol.12 , pp. 3-18
    • Jelesarov, I.1    Bosshard, H.R.2
  • 31
    • 2442468051 scopus 로고    scopus 로고
    • Regulation of cyclin D1/Cdk4 complexes by calcium/calmodulin-dependent protein kinase i
    • Kahl, C. R. and Means, A. R. (2004) Regulation of cyclin D1/Cdk4 complexes by calcium/calmodulin-dependent protein kinase I J. Biol. Chem. 279, 15411-15419
    • (2004) J. Biol. Chem. , vol.279 , pp. 15411-15419
    • Kahl, C.R.1    Means, A.R.2
  • 32
    • 0024505761 scopus 로고
    • Points of action of estrogen antagonists and a calmodulin antagonist within the MCF-7 human breast cancer cell cycle
    • Musgrove, E. A., Wakeling, A. E., and Sutherland, R. L. (1989) Points of action of estrogen antagonists and a calmodulin antagonist within the MCF-7 human breast cancer cell cycle Cancer Res. 49, 2398-2404
    • (1989) Cancer Res. , vol.49 , pp. 2398-2404
    • Musgrove, E.A.1    Wakeling, A.E.2    Sutherland, R.L.3
  • 33
    • 0023036064 scopus 로고
    • 2+/calmodulin-dependent protein kinase by autophosphorylation: ATP modulates production of an autonomous enzyme
    • 2+/calmodulin-dependent protein kinase by autophosphorylation: ATP modulates production of an autonomous enzyme Proc. Natl. Acad. Sci. U.S.A. 83, 9497-9501
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 9497-9501
    • Lou, L.L.1    Lloyd, S.J.2    Schulman, H.3
  • 34
    • 37349081963 scopus 로고    scopus 로고
    • Vinflunine, a novel microtubule inhibitor, suppresses calmodulin interaction with the microtubule-associated protein STOP
    • Makarov, A. A., Tsvetkov, P. O., Villard, C., Esquieu, D., Pourroy, B., Fahy, J., Braguer, D., Peyrot, V., and Lafitte, D. (2007) Vinflunine, a novel microtubule inhibitor, suppresses calmodulin interaction with the microtubule-associated protein STOP Biochemistry 46, 14899-14906
    • (2007) Biochemistry , vol.46 , pp. 14899-14906
    • Makarov, A.A.1    Tsvetkov, P.O.2    Villard, C.3    Esquieu, D.4    Pourroy, B.5    Fahy, J.6    Braguer, D.7    Peyrot, V.8    Lafitte, D.9
  • 37
    • 0347949547 scopus 로고    scopus 로고
    • Regulation of cell cycle progression by calcium/calmodulin-dependent pathways
    • Kahl, C. R. and Means, A. R. (2003) Regulation of cell cycle progression by calcium/calmodulin-dependent pathways Endocr. Rev. 24, 719-736
    • (2003) Endocr. Rev. , vol.24 , pp. 719-736
    • Kahl, C.R.1    Means, A.R.2
  • 38
    • 0024494439 scopus 로고
    • The effect of trifluoperazine, a calmodulin antagonist, on the growth of normal and malignant epidermal keratinocytes in culture
    • Grief, F., Soroff, H. S., Albers, K. M., and Taichman, L. B. (1989) The effect of trifluoperazine, a calmodulin antagonist, on the growth of normal and malignant epidermal keratinocytes in culture Eur. J. Cancer Clin. Oncol. 25, 19-26
    • (1989) Eur. J. Cancer Clin. Oncol. , vol.25 , pp. 19-26
    • Grief, F.1    Soroff, H.S.2    Albers, K.M.3    Taichman, L.B.4
  • 39
    • 0020062918 scopus 로고
    • Calmodulin and the cell cycle: Involvement in regulation of cell-cycle progression
    • Chafouleas, J. G., Bolton, W. E., Hidaka, H., Boyd, A. E., and Means, A. R. (1982) Calmodulin and the cell cycle: Involvement in regulation of cell-cycle progression Cell 28, 41-50
    • (1982) Cell , vol.28 , pp. 41-50
    • Chafouleas, J.G.1    Bolton, W.E.2    Hidaka, H.3    Boyd, A.E.4    Means, A.R.5
  • 40
    • 0028923306 scopus 로고
    • Radicicol, a protein tyrosine kinase inhibitor, suppresses the expression of mitogen-inducible cyclooxygenase in macrophages stimulated with lipopolysaccharide and in experimental glomerulonephritis
    • Chanmugam, P., Feng, L., Liou, S., Jang, B. C., Boudreau, M., Yu, G., Lee, J. H., Kwon, H. J., Beppu, T., and Yoshida, M. (1995) Radicicol, a protein tyrosine kinase inhibitor, suppresses the expression of mitogen-inducible cyclooxygenase in macrophages stimulated with lipopolysaccharide and in experimental glomerulonephritis J. Biol. Chem. 270, 5418-5426
    • (1995) J. Biol. Chem. , vol.270 , pp. 5418-5426
    • Chanmugam, P.1    Feng, L.2    Liou, S.3    Jang, B.C.4    Boudreau, M.5    Yu, G.6    Lee, J.H.7    Kwon, H.J.8    Beppu, T.9    Yoshida, M.10
  • 41
    • 77952384971 scopus 로고    scopus 로고
    • Aptamers as artificial gene regulation elements
    • Suess, B. and Weigand, J. E. (2009) Aptamers as artificial gene regulation elements Methods Mol. Biol. 535, 201-208
    • (2009) Methods Mol. Biol. , vol.535 , pp. 201-208
    • Suess, B.1    Weigand, J.E.2
  • 42
    • 0031567108 scopus 로고    scopus 로고
    • Energetics of target peptide recognition by calmodulin: A calorimetric study
    • Wintrode, P. L. and Privalov, P. L. (1997) Energetics of target peptide recognition by calmodulin: A calorimetric study J. Mol. Biol. 266, 1050-1062
    • (1997) J. Mol. Biol. , vol.266 , pp. 1050-1062
    • Wintrode, P.L.1    Privalov, P.L.2
  • 43
    • 0023664031 scopus 로고
    • Microcalorimetric investigation of the interactions in the ternary complex calmodulin-calcium-melittin
    • Milos, M., Schaer, J. J., Comte, M., and Cox, J. A. (1987) Microcalorimetric investigation of the interactions in the ternary complex calmodulin-calcium-melittin J. Biol. Chem. 262, 2746-2749
    • (1987) J. Biol. Chem. , vol.262 , pp. 2746-2749
    • Milos, M.1    Schaer, J.J.2    Comte, M.3    Cox, J.A.4
  • 44
    • 34047237831 scopus 로고    scopus 로고
    • 2+/calmodulin- dependent protein kinase II: Subpicomolar Kd determined using competition titration calorimetry
    • 2+/calmodulin-dependent protein kinase II: Subpicomolar Kd determined using competition titration calorimetry Biochemistry 46, 4017-4027
    • (2007) Biochemistry , vol.46 , pp. 4017-4027
    • Tse, J.K.1    Giannetti, A.M.2    Bradshaw, J.M.3
  • 45
    • 0035958004 scopus 로고    scopus 로고
    • Energetics of target peptide binding by calmodulin reveals different modes of binding
    • Brokx, R. D., Lopez, M. M., Vogel, H. J., and Makhatadze, G. I. (2001) Energetics of target peptide binding by calmodulin reveals different modes of binding J. Biol. Chem. 276, 14083-14091
    • (2001) J. Biol. Chem. , vol.276 , pp. 14083-14091
    • Brokx, R.D.1    Lopez, M.M.2    Vogel, H.J.3    Makhatadze, G.I.4
  • 46
    • 0032512626 scopus 로고    scopus 로고
    • Solution structure of calmodulin-W-7 complex: The basis of diversity in molecular recognition
    • Osawa, M., Swindells, M. B., Tanikawa, J., Tanaka, T., Mase, T., Furuya, T., and Ikura, M. (1998) Solution structure of calmodulin-W-7 complex: The basis of diversity in molecular recognition J. Mol. Biol. 276, 165-176
    • (1998) J. Mol. Biol. , vol.276 , pp. 165-176
    • Osawa, M.1    Swindells, M.B.2    Tanikawa, J.3    Tanaka, T.4    Mase, T.5    Furuya, T.6    Ikura, M.7
  • 48
    • 0020643734 scopus 로고
    • Naphthalenesulfonamides as calmodulin antagonists
    • Hidaka, H. and Tanaka, T. (1983) Naphthalenesulfonamides as calmodulin antagonists Methods Enzymol. 102, 185-194
    • (1983) Methods Enzymol. , vol.102 , pp. 185-194
    • Hidaka, H.1    Tanaka, T.2
  • 49
    • 0019947482 scopus 로고
    • Interaction of drugs with calmodulin: Biochemical, pharmacological and clinical implications
    • Weiss, B., Prozialick, W. C., and Wallace, T. L. (1982) Interaction of drugs with calmodulin: Biochemical, pharmacological and clinical implications Biochem. Pharmacol. 31, 2217-2226
    • (1982) Biochem. Pharmacol. , vol.31 , pp. 2217-2226
    • Weiss, B.1    Prozialick, W.C.2    Wallace, T.L.3
  • 50
    • 0028558882 scopus 로고
    • Drug binding by calmodulin: Crystal structure of a calmodulin- trifluoperazine complex
    • Cook, W. J., Walter, L. J., and Walter, M. R. (1994) Drug binding by calmodulin: Crystal structure of a calmodulin-trifluoperazine complex Biochemistry 33, 15259-15265
    • (1994) Biochemistry , vol.33 , pp. 15259-15265
    • Cook, W.J.1    Walter, L.J.2    Walter, M.R.3
  • 51
    • 0022653767 scopus 로고
    • Calcium, calmodulin, and protein content of adriamycin-resistant and -sensitive murine leukemic cells
    • Nair, S., Samy, T. S. A., and Krishan, A. (1986) Calcium, calmodulin, and protein content of adriamycin-resistant and -sensitive murine leukemic cells Cancer Res. 46, 229-232
    • (1986) Cancer Res. , vol.46 , pp. 229-232
    • Nair, S.1    Samy, T.S.A.2    Krishan, A.3
  • 52
    • 0022972654 scopus 로고
    • Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug-resistant human cells
    • Chen, C. J., Chin, J. E., Ueda, K., Clark, D. P., Pastan, I., Gottesman, M. M., and Roninson, I. B. (1986) Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug-resistant human cells Cell 47, 381-389
    • (1986) Cell , vol.47 , pp. 381-389
    • Chen, C.J.1    Chin, J.E.2    Ueda, K.3    Clark, D.P.4    Pastan, I.5    Gottesman, M.M.6    Roninson, I.B.7
  • 53
    • 33845386823 scopus 로고    scopus 로고
    • Targeting calmodulin in reversing multi drug resistance in cancer cells
    • Mayur, Y. C., Jagadeesh, S., and Thimmaiah, K. N. (2006) Targeting calmodulin in reversing multi drug resistance in cancer cells Mini Rev. Med. Chem. 6, 1383-1389
    • (2006) Mini Rev. Med. Chem. , vol.6 , pp. 1383-1389
    • Mayur, Y.C.1    Jagadeesh, S.2    Thimmaiah, K.N.3


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