메뉴 건너뛰기




Volumn 297, Issue 1, 2004, Pages 97-107

Adenylate kinase I does not affect cellular growth characteristics under normal and metabolic stress conditions

Author keywords

Adenylate kinase; Cell proliferation; Metabolic stress

Indexed keywords

ADENYLATE KINASE; GALACTOSE; GLUCOSE; ISOENZYME;

EID: 2942606509     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2004.02.025     Document Type: Article
Times cited : (6)

References (43)
  • 1
    • 0031680034 scopus 로고    scopus 로고
    • Adenylate kinase: Kinetic behavior in intact cells indicates it is integral to multiple cellular processes
    • Dzeja P.P., Zeleznikar R.J., Goldberg N.D. Adenylate kinase: kinetic behavior in intact cells indicates it is integral to multiple cellular processes. Mol. Cell. Biochem. 184:1998;169-182
    • (1998) Mol. Cell. Biochem. , vol.184 , pp. 169-182
    • Dzeja, P.P.1    Zeleznikar, R.J.2    Goldberg, N.D.3
  • 2
    • 0028930129 scopus 로고
    • Adenylate kinase-catalyzed phosphoryl transfer couples ATP utilization with its generation by glycolysis in intact muscle
    • Zeleznikar R.J., Dzeja P.P., Goldberg N.D. Adenylate kinase-catalyzed phosphoryl transfer couples ATP utilization with its generation by glycolysis in intact muscle. J. Biol. Chem. 270:1995;7311-7319
    • (1995) J. Biol. Chem. , vol.270 , pp. 7311-7319
    • Zeleznikar, R.J.1    Dzeja, P.P.2    Goldberg, N.D.3
  • 3
    • 0025191301 scopus 로고
    • Evidence for compartmentalized adenylate kinase catalysis serving a high energy phosphoryl transfer function in rat skeletal muscle
    • Zeleznikar R.J., Heyman R.A., Graeff R.M., Walseth T.F., Dawis S.M., Butz E.A., Goldberg N.D. Evidence for compartmentalized adenylate kinase catalysis serving a high energy phosphoryl transfer function in rat skeletal muscle. J. Biol. Chem. 265:1990;300-311
    • (1990) J. Biol. Chem. , vol.265 , pp. 300-311
    • Zeleznikar, R.J.1    Heyman, R.A.2    Graeff, R.M.3    Walseth, T.F.4    Dawis, S.M.5    Butz, E.A.6    Goldberg, N.D.7
  • 4
    • 0033560109 scopus 로고    scopus 로고
    • AMP-activated protein kinase: An ultrasensitive system for monitoring cellular energy charge
    • Hardie D.G., Salt I.P., Hawley S.A., Davies S.P. AMP-activated protein kinase: an ultrasensitive system for monitoring cellular energy charge. Biochem. J. 338(Pt 3):1999;717-722
    • (1999) Biochem. J. , vol.338 , Issue.3 PART , pp. 717-722
    • Hardie, D.G.1    Salt, I.P.2    Hawley, S.A.3    Davies, S.P.4
  • 5
    • 8944233359 scopus 로고    scopus 로고
    • Suppression of adenylate kinase catalyzed phosphotransfer precedes and is associated with glucose-induced insulin secretion in intact HIT-T15 cells
    • Olson L.K., Schroeder W., Robertson R.P., Goldberg N.D., Walseth T.F. Suppression of adenylate kinase catalyzed phosphotransfer precedes and is associated with glucose-induced insulin secretion in intact HIT-T15 cells. J. Biol. Chem. 271:1996;16544-16552
    • (1996) J. Biol. Chem. , vol.271 , pp. 16544-16552
    • Olson, L.K.1    Schroeder, W.2    Robertson, R.P.3    Goldberg, N.D.4    Walseth, T.F.5
  • 7
    • 0027418855 scopus 로고
    • Tissue-specific and developmentally regulated expression of the genes encoding adenylate kinase isozymes
    • Tanabe T., Yamada M., Noma T., Kajii T., Nakazawa A. Tissue-specific and developmentally regulated expression of the genes encoding adenylate kinase isozymes. J. Biochem. (Tokyo). 113:1993;200-207
    • (1993) J. Biochem. (Tokyo) , vol.113 , pp. 200-207
    • Tanabe, T.1    Yamada, M.2    Noma, T.3    Kajii, T.4    Nakazawa, A.5
  • 8
    • 0033608162 scopus 로고    scopus 로고
    • Distribution and developmental changes of adenylate kinase isozymes in the rat brain: Localization of adenylate kinase 1 in the olfactory bulb
    • Inouye S., Yamada Y., Miura K., Suzuki H., Kawata K., Shinoda K., Nakazawa A. Distribution and developmental changes of adenylate kinase isozymes in the rat brain: localization of adenylate kinase 1 in the olfactory bulb. Biochem. Biophys. Res. Commun. 254:1999;618-622
    • (1999) Biochem. Biophys. Res. Commun. , vol.254 , pp. 618-622
    • Inouye, S.1    Yamada, Y.2    Miura, K.3    Suzuki, H.4    Kawata, K.5    Shinoda, K.6    Nakazawa, A.7
  • 10
    • 0034731467 scopus 로고    scopus 로고
    • Compromised energetics in the adenylate kinase AK1 gene knockout heart under metabolic stress
    • Pucar D., Janssen E., Dzeja P.P., Juranic N., Macura S., Wieringa B., Terzic A. Compromised energetics in the adenylate kinase AK1 gene knockout heart under metabolic stress. J. Biol. Chem. 275:2000;41424-41429
    • (2000) J. Biol. Chem. , vol.275 , pp. 41424-41429
    • Pucar, D.1    Janssen, E.2    Dzeja, P.P.3    Juranic, N.4    MacUra, S.5    Wieringa, B.6    Terzic, A.7
  • 12
  • 13
    • 0036924103 scopus 로고    scopus 로고
    • Cellular characterization of adenylate kinase and its isoform: Two-photon excitation fluorescence imaging and fluorescence correlation spectroscopy
    • Ruan Q., Chen Y., Gratton E., Glaser M., Mantulin W.W. Cellular characterization of adenylate kinase and its isoform: two-photon excitation fluorescence imaging and fluorescence correlation spectroscopy. Biophys. J. 83:2002;3177-3187
    • (2002) Biophys. J. , vol.83 , pp. 3177-3187
    • Ruan, Q.1    Chen, Y.2    Gratton, E.3    Glaser, M.4    Mantulin, W.W.5
  • 14
    • 0842345405 scopus 로고    scopus 로고
    • Two structurally distinct and spatially compartmentalized adenylate kinases are expressed from the AK1 gene in mouse brain
    • Janssen E., Kuiper J., Hodgson D., Zingman L.V., Alekseev A.E., Terzic A., Wieringa B. Two structurally distinct and spatially compartmentalized adenylate kinases are expressed from the AK1 gene in mouse brain. Mol. Cell. Biochem. 256:2004;59-72
    • (2004) Mol. Cell. Biochem. , vol.256 , pp. 59-72
    • Janssen, E.1    Kuiper, J.2    Hodgson, D.3    Zingman, L.V.4    Alekseev, A.E.5    Terzic, A.6    Wieringa, B.7
  • 16
    • 0038644934 scopus 로고    scopus 로고
    • Adenylate kinase 1 deficiency induces molecular and structural adaptations to support muscle energy metabolism
    • Janssen E., de Groof A., Wijers M., Fransen J., Dzeja P.P., Terzic A., Wieringa B. Adenylate kinase 1 deficiency induces molecular and structural adaptations to support muscle energy metabolism. J. Biol. Chem. 278:2003;12937-12945
    • (2003) J. Biol. Chem. , vol.278 , pp. 12937-12945
    • Janssen, E.1    De Groof, A.2    Wijers, M.3    Fransen, J.4    Dzeja, P.P.5    Terzic, A.6    Wieringa, B.7
  • 17
    • 0031730047 scopus 로고    scopus 로고
    • Metabolic characteristics of different malignant cancer cell lines
    • Mazurek S., Grimm H., Wilker S., Leib S., Eigenbrodt E. Metabolic characteristics of different malignant cancer cell lines. Anticancer Res. 18:1998;3275-3282
    • (1998) Anticancer Res. , vol.18 , pp. 3275-3282
    • Mazurek, S.1    Grimm, H.2    Wilker, S.3    Leib, S.4    Eigenbrodt, E.5
  • 18
    • 0030683603 scopus 로고    scopus 로고
    • The role of phosphometabolites in cell proliferation, energy metabolism, and tumor therapy
    • Mazurek S., Boschek C.B., Eigenbrodt E. The role of phosphometabolites in cell proliferation, energy metabolism, and tumor therapy. J. Bioenerg. Biomembr. 29:1997;315-330
    • (1997) J. Bioenerg. Biomembr. , vol.29 , pp. 315-330
    • Mazurek, S.1    Boschek, C.B.2    Eigenbrodt, E.3
  • 19
    • 0031040469 scopus 로고    scopus 로고
    • Effect of extracellular AMP on cell proliferation and metabolism of breast cancer cell lines with high and low glycolytic rates
    • Mazurek S., Michel A., Eigenbrodt E. Effect of extracellular AMP on cell proliferation and metabolism of breast cancer cell lines with high and low glycolytic rates. J. Biol. Chem. 272:1997;4941-4952
    • (1997) J. Biol. Chem. , vol.272 , pp. 4941-4952
    • Mazurek, S.1    Michel, A.2    Eigenbrodt, E.3
  • 20
    • 0024283936 scopus 로고
    • A versatile in vivo and in vitro eukaryotic expression vector for protein engineering
    • Green S., Issemann I., Sheer E. A versatile in vivo and in vitro eukaryotic expression vector for protein engineering. Nucleic Acids Res. 16:1988;369
    • (1988) Nucleic Acids Res. , vol.16 , pp. 369
    • Green, S.1    Issemann, I.2    Sheer, E.3
  • 21
    • 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. 72:1976;248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 22
    • 0033573012 scopus 로고    scopus 로고
    • The in vitro manipulation of carbohydrate metabolism: A new strategy for deciphering the cellular defence mechanisms against nitric oxide attack
    • Le Goffe C., Vallette G., Jarry A., Bou-Hanna C., Laboisse C.L. The in vitro manipulation of carbohydrate metabolism: a new strategy for deciphering the cellular defence mechanisms against nitric oxide attack. Biochem. J. 344(Pt 3):1999;643-648
    • (1999) Biochem. J. , vol.344 , Issue.3 PART , pp. 643-648
    • Le Goffe, C.1    Vallette, G.2    Jarry, A.3    Bou-Hanna, C.4    Laboisse, C.L.5
  • 23
    • 0031763886 scopus 로고    scopus 로고
    • Pyruvate kinase and the interaction of amino acid and carbohydrate metabolism in solid tumors
    • Eigenbrodt E., Kallinowski F., Ott M., Mazurek S., Vaupel P. Pyruvate kinase and the interaction of amino acid and carbohydrate metabolism in solid tumors. Anticancer Res. 18:1998;3267-3274
    • (1998) Anticancer Res. , vol.18 , pp. 3267-3274
    • Eigenbrodt, E.1    Kallinowski, F.2    Ott, M.3    Mazurek, S.4    Vaupel, P.5
  • 24
    • 0042734413 scopus 로고    scopus 로고
    • Impaired intracellular energetic communication in muscles from creatine kinase and adenylate kinase (M-CK/AK1) double knockout mice
    • Janssen E., Terzic A., Wieringa B., Dzeja P.P. Impaired intracellular energetic communication in muscles from creatine kinase and adenylate kinase (M-CK/AK1) double knockout mice. J. Biol. Chem. 278:2003;30441-30449
    • (2003) J. Biol. Chem. , vol.278 , pp. 30441-30449
    • Janssen, E.1    Terzic, A.2    Wieringa, B.3    Dzeja, P.P.4
  • 25
    • 0036510541 scopus 로고    scopus 로고
    • Mitochondrial binding of hexokinase II inhibits Bax-induced cytochrome c release and apoptosis
    • Pastorino J.G., Shulga N., Hoek J.B. Mitochondrial binding of hexokinase II inhibits Bax-induced cytochrome c release and apoptosis. J. Biol. Chem. 277:2002;7610-7618
    • (2002) J. Biol. Chem. , vol.277 , pp. 7610-7618
    • Pastorino, J.G.1    Shulga, N.2    Hoek, J.B.3
  • 26
    • 0041309460 scopus 로고    scopus 로고
    • Hexokinase II: The integration of energy metabolism and control of apoptosis
    • Pastorino J.G., Hoek J.B. Hexokinase II: the integration of energy metabolism and control of apoptosis. Curr. Med. Chem. 10:2003;1535-1551
    • (2003) Curr. Med. Chem. , vol.10 , pp. 1535-1551
    • Pastorino, J.G.1    Hoek, J.B.2
  • 27
    • 0042860122 scopus 로고    scopus 로고
    • Cell biology: Metabolism meets death
    • Downward J. Cell biology: metabolism meets death. Nature. 424:2003;896-897
    • (2003) Nature , vol.424 , pp. 896-897
    • Downward, J.1
  • 28
    • 0033057367 scopus 로고    scopus 로고
    • An inducible gene product for 6-phosphofructo-2-kinase with an AU-rich instability element: Role in tumor cell glycolysis and the Warburg effect
    • Chesney J., Mitchell R., Benigni F., Bacher M., Spiegel L., Al-Abed Y., Han J.H., Metz C., Bucala R. An inducible gene product for 6-phosphofructo-2- kinase with an AU-rich instability element: role in tumor cell glycolysis and the Warburg effect. Proc. Natl. Acad. Sci. U. S. A. 96:1999;3047-3052
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 3047-3052
    • Chesney, J.1    Mitchell, R.2    Benigni, F.3    Bacher, M.4    Spiegel, L.5    Al-Abed, Y.6    Han, J.H.7    Metz, C.8    Bucala, R.9
  • 29
    • 0037110975 scopus 로고    scopus 로고
    • Possible involvement of both mitochondria- and endoplasmic reticulum-dependent caspase pathways in rotenone-induced apoptosis in human neuroblastoma SH-SY5Y cells
    • Kitamura Y., Inden M., Miyamura A., Kakimura J., Taniguchi T., Shimohama S. Possible involvement of both mitochondria- and endoplasmic reticulum-dependent caspase pathways in rotenone-induced apoptosis in human neuroblastoma SH-SY5Y cells. Neurosci. Lett. 333:2002;25-28
    • (2002) Neurosci. Lett. , vol.333 , pp. 25-28
    • Kitamura, Y.1    Inden, M.2    Miyamura, A.3    Kakimura, J.4    Taniguchi, T.5    Shimohama, S.6
  • 30
    • 0035450853 scopus 로고    scopus 로고
    • Mitochondrial electron transport inhibitors cause lipid peroxidation-dependent and-independent cell death: Protective role of antioxidants
    • Zhang J.G., Tirmenstein M.A., Nicholls-Grzemski F.A., Fariss M.W. Mitochondrial electron transport inhibitors cause lipid peroxidation-dependent and-independent cell death: protective role of antioxidants. Arch. Biochem. Biophys. 393:2001;87-96
    • (2001) Arch. Biochem. Biophys. , vol.393 , pp. 87-96
    • Zhang, J.G.1    Tirmenstein, M.A.2    Nicholls-Grzemski, F.A.3    Fariss, M.W.4
  • 31
    • 0037085942 scopus 로고    scopus 로고
    • Involvement of caspase-3 and p38 mitogen-activated protein kinase in cobalt chloride-induced apoptosis in PC12 cells
    • Zou W., Zeng J., Zhuo M., Xu W., Sun L., Wang J., Liu X. Involvement of caspase-3 and p38 mitogen-activated protein kinase in cobalt chloride-induced apoptosis in PC12 cells. J. Neurosci. Res. 67:2002;837-843
    • (2002) J. Neurosci. Res. , vol.67 , pp. 837-843
    • Zou, W.1    Zeng, J.2    Zhuo, M.3    Xu, W.4    Sun, L.5    Wang, J.6    Liu, X.7
  • 34
    • 0037163688 scopus 로고    scopus 로고
    • Evaluation of 2-deoxy-D-glucose as a chemotherapeutic agent: Mechanism of cell death
    • Aft R.L., Zhang F.W., Gius D. Evaluation of 2-deoxy-D-glucose as a chemotherapeutic agent: mechanism of cell death. Br. J. Cancer. 87:2002;805-812
    • (2002) Br. J. Cancer , vol.87 , pp. 805-812
    • Aft, R.L.1    Zhang, F.W.2    Gius, D.3
  • 35
    • 0032774329 scopus 로고    scopus 로고
    • Bcl-2 protects against FCCP-induced apoptosis and mitochondrial membrane potential depolarization in PC12 cells
    • Dispersyn G., Nuydens R., Connors R., Borgers M., Geerts H. Bcl-2 protects against FCCP-induced apoptosis and mitochondrial membrane potential depolarization in PC12 cells. Biochim. Biophys. Acta. 1428:1999;357-371
    • (1999) Biochim. Biophys. Acta , vol.1428 , pp. 357-371
    • Dispersyn, G.1    Nuydens, R.2    Connors, R.3    Borgers, M.4    Geerts, H.5
  • 37
    • 0030612749 scopus 로고    scopus 로고
    • JC-1, but not DiOC6(3) or rhodamine 123, is a reliable fluorescent probe to assess delta psi changes in intact cells: Implications for studies on mitochondrial functionality during apoptosis
    • Salvioli S., Ardizzoni A., Franceschi C., Cossarizza A. JC-1, but not DiOC6(3) or rhodamine 123, is a reliable fluorescent probe to assess delta psi changes in intact cells: implications for studies on mitochondrial functionality during apoptosis. FEBS Lett. 411:1997;77-82
    • (1997) FEBS Lett. , vol.411 , pp. 77-82
    • Salvioli, S.1    Ardizzoni, A.2    Franceschi, C.3    Cossarizza, A.4
  • 39
    • 0036468514 scopus 로고    scopus 로고
    • Effects of ambient oxygen concentration on the growth and antioxidant defenses of human cell cultures established from fetal and postnatal skin
    • Balin A.K., Pratt L., Allen R.G. Effects of ambient oxygen concentration on the growth and antioxidant defenses of human cell cultures established from fetal and postnatal skin. Free Radical Biol. Med. 32:2002;257-267
    • (2002) Free Radical Biol. Med. , vol.32 , pp. 257-267
    • Balin, A.K.1    Pratt, L.2    Allen, R.G.3
  • 40
    • 0036682009 scopus 로고    scopus 로고
    • Lowered oxygen tension induces expression of the hypoxia marker MN/carbonic anhydrase IX in the absence of hypoxia-inducible factor 1 alpha stabilization: A role for phosphatidylinositol 3′-kinase
    • Kaluz S., Kaluzova M., Chrastina A., Olive P.L., Pastorekova S., Pastorek J., Lerman M.I., Stanbridge E.J. Lowered oxygen tension induces expression of the hypoxia marker MN/carbonic anhydrase IX in the absence of hypoxia-inducible factor 1 alpha stabilization: a role for phosphatidylinositol 3′-kinase. Cancer Res. 62:2002;4469-4477
    • (2002) Cancer Res. , vol.62 , pp. 4469-4477
    • Kaluz, S.1    Kaluzova, M.2    Chrastina, A.3    Olive, P.L.4    Pastorekova, S.5    Pastorek, J.6    Lerman, M.I.7    Stanbridge, E.J.8
  • 42
    • 0037184909 scopus 로고    scopus 로고
    • Taking the study of cancer cell survival to a new dimension
    • Jacks T., Weinberg R.A. Taking the study of cancer cell survival to a new dimension. Cell. 111:2002;923-925
    • (2002) Cell , vol.111 , pp. 923-925
    • Jacks, T.1    Weinberg, R.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.