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Volumn 8, Issue 3, 1997, Pages 327-334

Effects of rottlerin, an inhibitor of calmodulin-dependent protein kinase III, on cellular proliferation, viability, and cell cycle distribution in malignant glioma cells

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN KINASE INHIBITOR;

EID: 0030980747     PISSN: 10449523     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (70)

References (53)
  • 1
    • 0028232968 scopus 로고
    • Calcium, calmodulin and cell cycle regulation
    • Means, A. R. Calcium, calmodulin and cell cycle regulation. FEBS Lett., 347: 1-4, 1984.
    • (1984) FEBS Lett. , vol.347 , pp. 1-4
    • Means, A.R.1
  • 2
    • 0027467864 scopus 로고
    • Regulation of the cell cycle by calcium and calmodulin
    • Lu, K. P., and Means, A. R. Regulation of the cell cycle by calcium and calmodulin. Endocr. Rev., 14: 40-58, 1993.
    • (1993) Endocr. Rev. , vol.14 , pp. 40-58
    • Lu, K.P.1    Means, A.R.2
  • 3
    • 0024196034 scopus 로고
    • Molecular mechanisms of action of calmodulin
    • Means, A. R. Molecular mechanisms of action of calmodulin. Recent Prog. Hormone Res., 44: 223-262, 1988.
    • (1988) Recent Prog. Hormone Res. , vol.44 , pp. 223-262
    • Means, A.R.1
  • 5
    • 0019817625 scopus 로고
    • An increase in calmodulin during growth of normal and cancerous liver in vivo
    • MacManus, J. P., Braceland, B. M., and Rixon, R. H. An increase in calmodulin during growth of normal and cancerous liver in vivo. FEBS Lett., 133: 99-102, 1981.
    • (1981) FEBS Lett. , vol.133 , pp. 99-102
    • MacManus, J.P.1    Braceland, B.M.2    Rixon, R.H.3
  • 6
    • 0021164995 scopus 로고
    • Differences in calmodulin levels of normal and transformed cells as determined by culture conditions
    • Veigl, M. L., Vanaman, T. C., Brance, M. E., and Sedwick, W. D. Differences in calmodulin levels of normal and transformed cells as determined by culture conditions. Cancer Res., 44: 3184-3189, 1984.
    • (1984) Cancer Res. , vol.44 , pp. 3184-3189
    • Veigl, M.L.1    Vanaman, T.C.2    Brance, M.E.3    Sedwick, W.D.4
  • 7
    • 0021994906 scopus 로고
    • Inhibition of the growth of C6 astrocytoma cells by inhibitors of calmodulin
    • Lee, G. L., and Hait, W. N. Inhibition of the growth of C6 astrocytoma cells by inhibitors of calmodulin. Life Sci., 36: 347-354, 1984.
    • (1984) Life Sci. , vol.36 , pp. 347-354
    • Lee, G.L.1    Hait, W.N.2
  • 8
    • 0021909418 scopus 로고
    • Inhibition of leukemic cell growth by inhibitors of calmodulin
    • Hait, W. N., Grais, L., Benz, C., and Cadman, E. Inhibition of leukemic cell growth by inhibitors of calmodulin. Cancer Chemother. Pharmacol., 14: 202-205, 1985.
    • (1985) Cancer Chemother. Pharmacol. , vol.14 , pp. 202-205
    • Hait, W.N.1    Grais, L.2    Benz, C.3    Cadman, E.4
  • 9
    • 0022343334 scopus 로고
    • Characterization of the cytotoxic effects of calmodulin inhibitors
    • Hait, W. N., and Lee, G. L. Characterization of the cytotoxic effects of calmodulin inhibitors. Biochem. Pharmacol., 34: 3973-3978, 1985.
    • (1985) Biochem. Pharmacol. , vol.34 , pp. 3973-3978
    • Hait, W.N.1    Lee, G.L.2
  • 10
    • 0024214483 scopus 로고
    • Calmodulin as a target for chemotherapeutic strategies
    • Hait, W. N., and DeRosa, W. T. Calmodulin as a target for chemotherapeutic strategies. Cancer Invest., 6: 499-511, 1988.
    • (1988) Cancer Invest. , vol.6 , pp. 499-511
    • Hait, W.N.1    DeRosa, W.T.2
  • 11
    • 0023661342 scopus 로고
    • Calmodulin is involved in regulation of cell proliferation
    • Rasmussen, C. D., and Means, A. R. Calmodulin is involved in regulation of cell proliferation. EMBO J., 6: 3961-3968, 1987.
    • (1987) EMBO J. , vol.6 , pp. 3961-3968
    • Rasmussen, C.D.1    Means, A.R.2
  • 12
    • 0023062987 scopus 로고
    • Inositol trisphosphate and diacylglycerol: Two interacting second messengers
    • Berridge, M. J. Inositol trisphosphate and diacylglycerol: two interacting second messengers. Annu. Rev. Biochem., 56: 159-193, 1987.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 159-193
    • Berridge, M.J.1
  • 13
    • 0025807509 scopus 로고
    • 2+ regulated transcription factor phosphorylated by calmodulin-dependent kinases
    • Washington DC
    • 2+ regulated transcription factor phosphorylated by calmodulin-dependent kinases. Science (Washington DC), 252: 1427-1430, 1991.
    • (1991) Science , vol.252 , pp. 1427-1430
    • Sheng, M.1    Thompson, M.A.2    Greenberg, M.E.3
  • 14
    • 1842413092 scopus 로고
    • Calcium/calmodulin-dependent binding proteins and kinase activity in murine and human glioblastoma
    • Cheng, E. H. C., Gorelick, F. S., Czernik, A. J., and Hait, W. N. Calcium/calmodulin-dependent binding proteins and kinase activity in murine and human glioblastoma. Cell Growth & Differ., 6: 1-7, 1995.
    • (1995) Cell Growth & Differ. , vol.6 , pp. 1-7
    • Cheng, E.H.C.1    Gorelick, F.S.2    Czernik, A.J.3    Hait, W.N.4
  • 15
    • 0023522187 scopus 로고
    • r 100,000 substrate for calmodulin-dependent protein kinase III in mammalian cells as elongation factor 2
    • r 100,000 substrate for calmodulin-dependent protein kinase III in mammalian cells as elongation factor 2. J. Biol. Chem., 262: 17299-17303, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17299-17303
    • Nairn, A.C.1    Palfrey, H.C.2
  • 16
    • 0023884601 scopus 로고
    • Phosphorylation of elongation factor 2 by EF-2 kinase affects rate of translation
    • Ryazanov, A. G., Shestakova, E. A., and Natapov, P. G. Phosphorylation of elongation factor 2 by EF-2 kinase affects rate of translation. Nature (Lond.), 334: 170-173, 1988.
    • (1988) Nature (Lond) , vol.334 , pp. 170-173
    • Ryazanov, A.G.1    Shestakova, E.A.2    Natapov, P.G.3
  • 17
    • 0001632984 scopus 로고
    • Phosphorylation of elongation factor 2: A mechanism to shut off protein synthesis for reprogramming gene expression
    • J. Ilan (ed.), New York: Plenum Publishing Corp.
    • Ryazanov, A. G., and Spirin, A. S. Phosphorylation of elongation factor 2: a mechanism to shut off protein synthesis for reprogramming gene expression. In: J. Ilan (ed.), Translational Regulation of Gene Expression 2, pp. 433-455. New York: Plenum Publishing Corp., 1993.
    • (1993) Translational Regulation of Gene Expression , vol.2 , pp. 433-455
    • Ryazanov, A.G.1    Spirin, A.S.2
  • 18
    • 0025733261 scopus 로고
    • Regulation of protein synthesis at the elongation stage: New insights into the control of gene expression in eukaryotes
    • Ryazanov, A. G., Rudkin, B. B., and Spirin, A. S. Regulation of protein synthesis at the elongation stage: new insights into the control of gene expression in eukaryotes. FEBS Lett., 285: 170-175, 1991.
    • (1991) FEBS Lett. , vol.285 , pp. 170-175
    • Ryazanov, A.G.1    Rudkin, B.B.2    Spirin, A.S.3
  • 19
    • 0023185463 scopus 로고
    • Rapid activation of calmodulin-dependent protein kinase III in mitogen-stimulated human fibroblasts
    • Palfrey, H. C., Nairn, A. C., Muldoon, L., and Villereal, M. L. Rapid activation of calmodulin-dependent protein kinase III in mitogen-stimulated human fibroblasts. J. Biol. Chem., 262: 9785-9792, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9785-9792
    • Palfrey, H.C.1    Nairn, A.C.2    Muldoon, L.3    Villereal, M.L.4
  • 20
    • 0027172933 scopus 로고
    • Phosphorylation of elongation factor 2 in normal and malignant rat glial cells
    • Bagaglio, D. M., Cheng, E. H. C., Gorelick, F. S., Mitsui, K., Nairn, A. C., and Hait, W. N. Phosphorylation of elongation factor 2 in normal and malignant rat glial cells. Cancer Res., 53: 2260-2264, 1993.
    • (1993) Cancer Res. , vol.53 , pp. 2260-2264
    • Bagaglio, D.M.1    Cheng, E.H.C.2    Gorelick, F.S.3    Mitsui, K.4    Nairn, A.C.5    Hait, W.N.6
  • 21
    • 0028117037 scopus 로고
    • Role of calmodulin-dependent phosphorylation of elongation factor 2 in the proliferation of rat glial cells
    • Bagaglio, D. M., and Hait, W. N. Role of calmodulin-dependent phosphorylation of elongation factor 2 in the proliferation of rat glial cells. Cell Growth & Differ., 5: 1403-1408, 1994.
    • (1994) Cell Growth & Differ. , vol.5 , pp. 1403-1408
    • Bagaglio, D.M.1    Hait, W.N.2
  • 22
    • 0028012779 scopus 로고
    • Elongation factor-2 kinase: Effective inhibition by the novel protein kinase inhibitor rottlerin and relative insensitivity towards staurosporine
    • Gschwendt, M., Kittstein, W., and Marks, F. Elongation factor-2 kinase: effective inhibition by the novel protein kinase inhibitor rottlerin and relative insensitivity towards staurosporine. FEBS Lett., 338: 85-88, 1994.
    • (1994) FEBS Lett. , vol.338 , pp. 85-88
    • Gschwendt, M.1    Kittstein, W.2    Marks, F.3
  • 23
    • 0003601534 scopus 로고
    • Rahway, NJ: Merck and Co., Inc.
    • Windholz, M. (ed.), The Merck Index, p. 1192. Rahway, NJ: Merck and Co., Inc., 1989.
    • (1989) The Merck Index , pp. 1192
    • Windholz, M.1
  • 24
    • 0021839818 scopus 로고
    • Studies in cytotoxic constituents in pericarps of Mallotus japonicus, part I
    • Arisawa, M., Fujita, A., Suzuki, R., Hayashi, T., and Morita, N. Studies in cytotoxic constituents in pericarps of Mallotus japonicus, part I. J. Natl. Prod., 48: 455-459, 1985.
    • (1985) J. Natl. Prod. , vol.48 , pp. 455-459
    • Arisawa, M.1    Fujita, A.2    Suzuki, R.3    Hayashi, T.4    Morita, N.5
  • 25
    • 0030580365 scopus 로고    scopus 로고
    • Elongation factor-2 kinase: Immunological evidence for the existence of tissue-specific isoforms
    • Hait, W. N., Ward, M. D., Trakht, I. N., and Ryazanov, A. G. Elongation factor-2 kinase: immunological evidence for the existence of tissue-specific isoforms. FEBS Lett., 397: 55-60, 1996.
    • (1996) FEBS Lett. , vol.397 , pp. 55-60
    • Hait, W.N.1    Ward, M.D.2    Trakht, I.N.3    Ryazanov, A.G.4
  • 26
    • 0024523044 scopus 로고
    • Antimicrobial and cytotoxic activity of rottlerin-type compounds from Hypericum drummondii
    • Hayasuriya, H., McChesney, J. D., Swanson, S. M., and Pezzuto, J. M. Antimicrobial and cytotoxic activity of rottlerin-type compounds from Hypericum drummondii. J. Natl. Prod., 52: 325-331, 1989.
    • (1989) J. Natl. Prod. , vol.52 , pp. 325-331
    • Hayasuriya, H.1    McChesney, J.D.2    Swanson, S.M.3    Pezzuto, J.M.4
  • 27
    • 0019225636 scopus 로고
    • Cell death: The significance of apoptosis
    • G. H. Bourne, F. J. Danielli, and K. W. Jeon (eds.), New York: Academic Press
    • Wyllie, A. H., Kerr, J. F. R., and, Currie, A. R. Cell death: the significance of apoptosis. In: G. H. Bourne, F. J. Danielli, and K. W. Jeon (eds.), International Review of Cytology, Vol. 68, pp. 251-306. New York: Academic Press, 1980.
    • (1980) International Review of Cytology , vol.68 , pp. 251-306
    • Wyllie, A.H.1    Kerr, J.F.R.2    Currie, A.R.3
  • 28
    • 0027261147 scopus 로고
    • The cell cycle related differences in susceptibility of HL-60 cells to apoptosis induced by various antitumor agents
    • Gorczyca, W., Gong, J., Ardelt, B., Traaganos, F., and Darzynkiewicz, Z. The cell cycle related differences in susceptibility of HL-60 cells to apoptosis induced by various antitumor agents. Cancer Res., 53: 3186-3192, 1993.
    • (1993) Cancer Res. , vol.53 , pp. 3186-3192
    • Gorczyca, W.1    Gong, J.2    Ardelt, B.3    Traaganos, F.4    Darzynkiewicz, Z.5
  • 29
    • 0029145998 scopus 로고
    • Phosphorylation of eukaryotic elongation factor 2 in differentiating and proliferating HL-60 cells
    • Nilsson, A., and, Nygard, O. Phosphorylation of eukaryotic elongation factor 2 in differentiating and proliferating HL-60 cells. Biochem. Biophys. Acta, 1268: 263-266, 1995.
    • (1995) Biochem. Biophys. Acta , vol.1268 , pp. 263-266
    • Nilsson, A.1    Nygard, O.2
  • 30
    • 0024369425 scopus 로고
    • Insulin-stimulated protein tyrosine phosphorylation in intact cells evaluated by giant two-dimensional gel electrophoresis
    • Levenson, R. M., and Blackshear, P. J. Insulin-stimulated protein tyrosine phosphorylation in intact cells evaluated by giant two-dimensional gel electrophoresis. J. Biol. Chem., 264: 19984-19993, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19984-19993
    • Levenson, R.M.1    Blackshear, P.J.2
  • 34
    • 0027418816 scopus 로고
    • Overexpression of protein kinase C-δ and -∈ in NIH 3T3 cells induces opposite effects on growth, morphology, anchorage dependence, and tumorigenicity
    • Mischak, H., Goodnight, J., Kolch, W., Martiny-Baron, G., Schaechtle, C., Kazanietz, M. G., Blumberg, P. M., Pierce, J. H., and Mushinski, J. F. Overexpression of protein kinase C-δ and -∈ in NIH 3T3 cells induces opposite effects on growth, morphology, anchorage dependence, and tumorigenicity. J. Biol. Chem., 268: 6090-6096, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6090-6096
    • Mischak, H.1    Goodnight, J.2    Kolch, W.3    Martiny-Baron, G.4    Schaechtle, C.5    Kazanietz, M.G.6    Blumberg, P.M.7    Pierce, J.H.8    Mushinski, J.F.9
  • 37
    • 0017095949 scopus 로고
    • Cycloheximide elicits in human fibroblasts a response characteristic for initiation of cell proliferation
    • Pohjanpelto, P. Cycloheximide elicits in human fibroblasts a response characteristic for initiation of cell proliferation. Exp. Cell Res., 102: 138-142, 1976.
    • (1976) Exp. Cell Res. , vol.102 , pp. 138-142
    • Pohjanpelto, P.1
  • 38
    • 0022597439 scopus 로고
    • Anisomycin and cycloheximide, like growth factors, stimulate rapidly ATP turnover in 3T3 cells
    • Talha, S., and Harel, L. Anisomycin and cycloheximide, like growth factors, stimulate rapidly ATP turnover in 3T3 cells. Cell Biol. Int. Rep., 10: 249-255, 1986.
    • (1986) Cell Biol. Int. Rep. , vol.10 , pp. 249-255
    • Talha, S.1    Harel, L.2
  • 39
    • 0021041054 scopus 로고
    • Cell-specific regulation of the c-myc gene by lymphocyte mitogens and platelet-derived growth factor
    • Kelly, K., Cochran, B. H., Stiles, C. D., and Leder, P. Cell-specific regulation of the c-myc gene by lymphocyte mitogens and platelet-derived growth factor. Cell, 35: 603-610, 1983.
    • (1983) Cell , vol.35 , pp. 603-610
    • Kelly, K.1    Cochran, B.H.2    Stiles, C.D.3    Leder, P.4
  • 40
    • 0022633687 scopus 로고
    • Effect of protein synthesis inhibitors on growth factor activation of c-fos, c-myc and actin gene transcription
    • Greenberg, M. E., Hermanowski, A. L., and Ziff, E. B. Effect of protein synthesis inhibitors on growth factor activation of c-fos, c-myc and actin gene transcription. Mol. Cell. Biol., 6: 1050-1057, 1986.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 1050-1057
    • Greenberg, M.E.1    Hermanowski, A.L.2    Ziff, E.B.3
  • 41
    • 0026093311 scopus 로고
    • Signaling and superinduction
    • Mahadevan, L. C., and Edwards, D. R. Signaling and superinduction. Nature (Lond.), 349: 747-748, 1991.
    • (1991) Nature (Lond) , vol.349 , pp. 747-748
    • Mahadevan, L.C.1    Edwards, D.R.2
  • 42
    • 0026772442 scopus 로고
    • Protein synthesis inhibitors differentially superinduce c-fos and c-jun by three distinct mechanisms: Lack of evidence for labile repressors
    • Edwards, D. R., and Mahadevan, L. C. Protein synthesis inhibitors differentially superinduce c-fos and c-jun by three distinct mechanisms: lack of evidence for labile repressors. EMBO J., 11: 2415-2423, 1992.
    • (1992) EMBO J. , vol.11 , pp. 2415-2423
    • Edwards, D.R.1    Mahadevan, L.C.2
  • 43
    • 0016175608 scopus 로고
    • The stimulation of the phosphorylation of ribosomal protein S6 by cycloheximide and puromycin
    • Gressner, A. M., and Wool, I. G. The stimulation of the phosphorylation of ribosomal protein S6 by cycloheximide and puromycin. Biochem. Biophys. Res. Commun., 60: 1482-1490, 1974.
    • (1974) Biochem. Biophys. Res. Commun. , vol.60 , pp. 1482-1490
    • Gressner, A.M.1    Wool, I.G.2
  • 44
    • 0027358722 scopus 로고
    • MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo
    • Sun, H., Charles, C. H., Lau, L. F., and Tonks, N. K. MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo. Cell, 75: 487-493, 1993.
    • (1993) Cell , vol.75 , pp. 487-493
    • Sun, H.1    Charles, C.H.2    Lau, L.F.3    Tonks, N.K.4
  • 45
    • 0029147738 scopus 로고
    • Protein synthesis inhibitors reveal differential regulation of mitogen activated protein kinase and stress-activated protein kinase pathways that converge on E1K-1
    • Zinck, R., Cahill, M. A., Kracht, M., Sachsenmaier, C., Hipskind, R. R., and Nordhei, A. Protein synthesis inhibitors reveal differential regulation of mitogen activated protein kinase and stress-activated protein kinase pathways that converge on E1K-1. Mol. Cell. Biol., 15: 4930-4938, 1995.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4930-4938
    • Zinck, R.1    Cahill, M.A.2    Kracht, M.3    Sachsenmaier, C.4    Hipskind, R.R.5    Nordhei, A.6
  • 47
    • 0028052255 scopus 로고
    • 55 but not mitogen-activated protein kinases ERK-1 and -2 are implicated in the induction of c-fos and c-jun
    • 55 but not mitogen-activated protein kinases ERK-1 and -2 are implicated in the induction of c-fos and c-jun. Mol. Cell. Biol., 14: 7352-7362, 1994.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7352-7362
    • Cano, E.1    Hazzalin, C.A.2    Mahadevan, L.C.3
  • 48
    • 0022612456 scopus 로고
    • Cycloheximide or puromycin can substitute for PDGF in inducing cellular DNA synthesis in quiescent 3T3 cells
    • Kaczmarek, L., Surmacz, E., and Baserga, R. Cycloheximide or puromycin can substitute for PDGF in inducing cellular DNA synthesis in quiescent 3T3 cells. Cell Biol. Int. Rep., 10: 455-463, 1986.
    • (1986) Cell Biol. Int. Rep. , vol.10 , pp. 455-463
    • Kaczmarek, L.1    Surmacz, E.2    Baserga, R.3
  • 49
    • 0030016110 scopus 로고    scopus 로고
    • Cloning and expression of cDNA encoding protein synthesis elongation factor-2 kinase
    • Redpath, N. T., Price, N. T., and Proud, C. G. Cloning and expression of cDNA encoding protein synthesis elongation factor-2 kinase. J. Biol. Chem., 271: 17547-17554, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17547-17554
    • Redpath, N.T.1    Price, N.T.2    Proud, C.G.3
  • 50
    • 0004252445 scopus 로고
    • Englewood Cliffs, NJ: Prentice-Hall, Inc.
    • Zar, J. H. Biostatistical Analysis, pp. 180-183. Englewood Cliffs, NJ: Prentice-Hall, Inc., 1992.
    • (1992) Biostatistical Analysis , pp. 180-183
    • Zar, J.H.1
  • 51
    • 0024492086 scopus 로고
    • Antibodies to CD3-T cell receptor complex induce death by apoptosis in immature T cells in thymic cultures
    • Smith, C. A., Williams, G. T., Kingston, R., Jenkinson, E. J., and Owen, J. J. T. Antibodies to CD3-T cell receptor complex induce death by apoptosis in immature T cells in thymic cultures. Nature (Lond.), 337: 181-184, 1989.
    • (1989) Nature (Lond) , vol.337 , pp. 181-184
    • Smith, C.A.1    Williams, G.T.2    Kingston, R.3    Jenkinson, E.J.4    Owen, J.J.T.5
  • 52
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72: 248-254, 1976.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 53
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.), 227: 680-685, 1970.
    • (1970) Nature (Lond) , vol.227 , pp. 680-685
    • Laemmli, U.K.1


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