메뉴 건너뛰기




Volumn 30, Issue 6, 2010, Pages 413-423

Characterization of non-cytosolic hexokinase activity in white skeletal muscle from goldfish (Carassius auratus L.) and the effect of cold acclimation

Author keywords

Glycolysis; Goldfish; Hexokinase (HK); Mitochondria; Skeletal muscle; Thermal acclimation

Indexed keywords

ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; FRUCTOSE; GLUCOSE; GLUCOSE 6 PHOSPHATE; GUANOSINE TRIPHOSPHATE; HEXOKINASE; INOSINE TRIPHOSPHATE; MANNOSE;

EID: 78650865664     PISSN: 01448463     EISSN: None     Source Type: Journal    
DOI: 10.1042/BSR20090128     Document Type: Article
Times cited : (5)

References (70)
  • 2
    • 0020016147 scopus 로고
    • The comparative isozymology of vertebrate hexokinases
    • Ureta, T. (1982) The comparative isozymology of vertebrate hexokinases. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 71, 549-555
    • (1982) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.71 , pp. 549-555
    • Ureta, T.1
  • 3
    • 2942571813 scopus 로고    scopus 로고
    • Molecular cloning of hepatic glucose-6-phosphatase catalytic subunit from gilthead sea bream (Sparus aurata): Response of its mRNA levels and glucokinase expression to refeeding and diet composition
    • Meton, I., Caseras, A., Fernandez, F. and Baanante, I. V. (2004) Molecular cloning of hepatic glucose-6-phosphatase catalytic subunit from gilthead sea bream (Sparus aurata): response of its mRNA levels and glucokinase expression to refeeding and diet composition. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 138, 145-153
    • (2004) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.138 , pp. 145-153
    • Meton, I.1    Caseras, A.2    Fernandez, F.3    Baanante, I.V.4
  • 4
    • 0033974785 scopus 로고    scopus 로고
    • Molecular cloning, tissue distribution and sequence analysis of complete glucokinase cDNAs from gilthead seabream (Sparus aurata), rainbow trout (Oncorhynchus mykiss) and common carp (Cyprinus carpio)
    • Panserat, S., Blin, C., Medale, F., Plagnes-Juan, E., Breque, J., Krishnamoorthy, J. and Kaushik, S. (2000) Molecular cloning, tissue distribution and sequence analysis of complete glucokinase cDNAs from gilthead seabream (Sparus aurata), rainbow trout (Oncorhynchus mykiss) and common carp (Cyprinus carpio). Biochim. Biophys. Acta 1474, 61-69
    • (2000) Biochim. Biophys. Acta , vol.1474 , pp. 61-69
    • Panserat, S.1    Blin, C.2    Medale, F.3    Plagnes-Juan, E.4    Breque, J.5    Krishnamoorthy, J.6    Kaushik, S.7
  • 7
    • 0013808687 scopus 로고
    • Multiple forms of hexokinase in the rat: Tissue distribution, age dependency, and properties
    • Katzen, H. M. and Schimke, R. T. (1965) Multiple forms of hexokinase in the rat: tissue distribution, age dependency, and properties. Proc. Natl. Acad. Sci. U.S.A. 54, 1218-1225
    • (1965) Proc. Natl. Acad. Sci. U.S.A. , vol.54 , pp. 1218-1225
    • Katzen, H.M.1    Schimke, R.T.2
  • 8
    • 0014007438 scopus 로고
    • Electrophoretic properties and tissue distribution of multiple forms of hexokinase in various mammalian species
    • Grossbard, L., Weksler, M. and Schimke, R. T. (1966) Electrophoretic properties and tissue distribution of multiple forms of hexokinase in various mammalian species. Biochem. Biophys. Res. Commun. 24, 32-38
    • (1966) Biochem. Biophys. Res. Commun. , vol.24 , pp. 32-38
    • Grossbard, L.1    Weksler, M.2    Schimke, R.T.3
  • 9
    • 0027186032 scopus 로고
    • Mammalian glucokinase and its gene
    • lynedjian, P. B. (1993) Mammalian glucokinase and its gene. Biochem. J. 293, 1-13
    • (1993) Biochem. J. , vol.293 , pp. 1-13
    • Lynedjian, P.B.1
  • 11
    • 0001477074 scopus 로고
    • Substrate specificity of brain hexokinase
    • Sols, A. and Crane, R. K. (1954) Substrate specificity of brain hexokinase. J. Biol. Chem. 210, 581-595
    • (1954) J. Biol. Chem. , vol.210 , pp. 581-595
    • Sols, A.1    Crane, R.K.2
  • 12
    • 0014010968 scopus 로고
    • Multiple hexokinases of rat tissues. Purification and comparison of soluble forms
    • Grossbard, L. and Schimke, R. T. (1966) Multiple hexokinases of rat tissues. Purification and comparison of soluble forms. J. Biol. Chem. 241, 3546-3560
    • (1966) J. Biol. Chem. , vol.241 , pp. 3546-3560
    • Grossbard, L.1    Schimke, R.T.2
  • 13
    • 0014197795 scopus 로고
    • Rat skeletal muscle hexokinase. II. Kinetic evidence for a second hexokinase in muscle tissue
    • Hanson, T. L. and Fromm, H. J. (1967) Rat skeletal muscle hexokinase. II. Kinetic evidence for a second hexokinase in muscle tissue. J. Biol. Chem. 242, 501-508
    • (1967) J. Biol. Chem. , vol.242 , pp. 501-508
    • Hanson, T.L.1    Fromm, H.J.2
  • 14
    • 0038714272 scopus 로고    scopus 로고
    • Isozymes of mammalian hexokinase: Structure, subcellular localization and metabolic function
    • Wilson, J. E. (2003) Isozymes of mammalian hexokinase: structure, subcellular localization and metabolic function. J. Exp. Biol. 206, 2049-2057
    • (2003) J. Exp. Biol. , vol.206 , pp. 2049-2057
    • Wilson, J.E.1
  • 15
    • 0037056002 scopus 로고    scopus 로고
    • Mitochondrial bound type II hexokinase: A key player in the growth and survival of many cancers and an ideal prospect for therapeutic intervention
    • Pedersen, P. L., Mathupala, S., Rempel, A., Geschwind, J. F. and Ko, Y. H. (2002) Mitochondrial bound type II hexokinase: a key player in the growth and survival of many cancers and an ideal prospect for therapeutic intervention. Biochim. Biophys. Acta 1555, 14-20
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 14-20
    • Pedersen, P.L.1    Mathupala, S.2    Rempel, A.3    Geschwind, J.F.4    Ko, Y.H.5
  • 16
    • 0006857425 scopus 로고
    • The association of hexokinase with particulate fractions of brain and other tissue homogenates
    • Crane, R. K. and Sols, A. (1953) The association of hexokinase with particulate fractions of brain and other tissue homogenates. J. Biol. Chem. 203, 273-292
    • (1953) J. Biol. Chem. , vol.203 , pp. 273-292
    • Crane, R.K.1    Sols, A.2
  • 17
    • 0014962558 scopus 로고
    • Multiple forms of hexokinase. Activities associated with subcellular particulate and soluble fractions of normal and streptozotocin diabetic rat tissues
    • Katzen, H. M., Soderman, D. D. and Wiley, C. E. (1970) Multiple forms of hexokinase. Activities associated with subcellular particulate and soluble fractions of normal and streptozotocin diabetic rat tissues. J. Biol. Chem. 245, 4081-4096
    • (1970) J. Biol. Chem. , vol.245 , pp. 4081-4096
    • Katzen, H.M.1    Soderman, D.D.2    Wiley, C.E.3
  • 18
    • 0022595453 scopus 로고
    • Hexokinase receptor complex in hepatoma mitochondria: Evidence from N,N′-dicyclohexylcarbodiimide-labeling studies for the involvement of the pore-forming protein VDAC
    • Nakashima, R. A., Mangan, P. S., Colombini, M. and Pedersen, P. L. (1986) Hexokinase receptor complex in hepatoma mitochondria: evidence from N,N′-dicyclohexylcarbodiimide-labeling studies for the involvement of the pore-forming protein VDAC. Biochemistry 25, 1015-1021
    • (1986) Biochemistry , vol.25 , pp. 1015-1021
    • Nakashima, R.A.1    Mangan, P.S.2    Colombini, M.3    Pedersen, P.L.4
  • 19
    • 0842305105 scopus 로고    scopus 로고
    • All three isoforms of the voltage-dependent anion channel (VDAC1, VDAC2, and VDAC3) are present in mitochondria from bovine, rabbit, and rat brain
    • Cesar Mde, C. and Wilson, J. E. (2004) All three isoforms of the voltage-dependent anion channel (VDAC1, VDAC2, and VDAC3) are present in mitochondria from bovine, rabbit, and rat brain. Arch. Biochem. Biophys. 422, 191-196
    • (2004) Arch. Biochem. Biophys. , vol.422 , pp. 191-196
    • Cesar Mde, C.1    Wilson, J.E.2
  • 20
    • 0031238860 scopus 로고    scopus 로고
    • Structural determinants for the intracellular localization of the isozymes of mammalian hexokinase: Intracellular localization of fusion constructs incorporating structural elements from the hexokinase isozymes and the green fluorescent protein
    • Sui, D. and Wilson, J. E. (1997) Structural determinants for the intracellular localization of the isozymes of mammalian hexokinase: intracellular localization of fusion constructs incorporating structural elements from the hexokinase isozymes and the green fluorescent protein. Arch. Biochem. Biophys. 345, 111-125
    • (1997) Arch. Biochem. Biophys. , vol.345 , pp. 111-125
    • Sui, D.1    Wilson, J.E.2
  • 21
    • 0026151278 scopus 로고
    • The effect of insulin on the catalytic efficacy of rat skeletal muscle hexokinase isoenzyme II
    • Goncharova, N. and Zelenina, E. V. (1991) The effect of insulin on the catalytic efficacy of rat skeletal muscle hexokinase isoenzyme II. Biokhimiia 56, 913-922
    • (1991) Biokhimiia , vol.56 , pp. 913-922
    • Goncharova, N.1    Zelenina, E.V.2
  • 22
    • 0042575733 scopus 로고
    • High aerobic glycolysis of rat hepatoma cells in culture: Role of mitochondrial hexokinase
    • Bustamante, E. and Pedersen, P. L. (1977) High aerobic glycolysis of rat hepatoma cells in culture: role of mitochondrial hexokinase. Proc. Natl. Acad. Sci. U.S.A. 74, 3735-3739
    • (1977) Proc. Natl. Acad. Sci. U.S.A. , vol.74 , pp. 3735-3739
    • Bustamante, E.1    Pedersen, P.L.2
  • 23
    • 0020079964 scopus 로고
    • Stability of hexokinase II in vitro and in ascites tumor cells
    • Rose, I. A. and Warms, J. V. (1982) Stability of hexokinase II in vitro and in ascites tumor cells. Arch. Biochem. Biophys. 213, 625-634
    • (1982) Arch. Biochem. Biophys. , vol.213 , pp. 625-634
    • Rose, I.A.1    Warms, J.V.2
  • 24
    • 0024237766 scopus 로고
    • Functional significance of mitochondrial bound hexokinase in tumor cell metabolism. Evidence for preferential phosphorylation of glucose by intramitochondrially generated ATP
    • Arora, K. K. and Pedersen, P. L. (1988) Functional significance of mitochondrial bound hexokinase in tumor cell metabolism. Evidence for preferential phosphorylation of glucose by intramitochondrially generated ATP. J. Biol. Chem. 263, 17422-17428
    • (1988) J. Biol. Chem. , vol.263 , pp. 17422-17428
    • Arora, K.K.1    Pedersen, P.L.2
  • 25
    • 0034983918 scopus 로고    scopus 로고
    • Inhibition of early apoptotic events by Akt/PKB is dependent on the first committed step of glycolysis and mitochondrial hexokinase
    • Gottlob, K., Majewski, N., Kennedy, S., Kandel, E., Robey, R. B. and Hay, N. (2001) Inhibition of early apoptotic events by Akt/PKB is dependent on the first committed step of glycolysis and mitochondrial hexokinase. Genes Dev. 15, 1406-1418
    • (2001) Genes Dev. , vol.15 , pp. 1406-1418
    • Gottlob, K.1    Majewski, N.2    Kennedy, S.3    Kandel, E.4    Robey, R.B.5    Hay, N.6
  • 26
    • 0036510541 scopus 로고    scopus 로고
    • Mitochondrial binding of hexokinase II inhibits Bax-induced cytochrome c release and apoptosis
    • Pastorino, J. G., Shulga, N. and Hoek, J. B. (2002) Mitochondrial binding of hexokinase II inhibits Bax-induced cytochrome c release and apoptosis. J. Biol. Chem. 277, 7610-7618
    • (2002) J. Biol. Chem. , vol.277 , pp. 7610-7618
    • Pastorino, J.G.1    Shulga, N.2    Hoek, J.B.3
  • 27
    • 4544355934 scopus 로고    scopus 로고
    • Mitochondrial bound hexokinase activity as a preventive antioxidant defense: Steady-state ADP formation as a regulatory mechanism of membrane potential and reactive oxygen species generation in mitochondria
    • da-Silva, W. S., Gomez-Puyou, A., de Gomez-Puyou, M. T., Moreno-Sanchez, R., De Felice, F. G., de Meis, L., Oliveira, M. F. and Galina, A. (2004) Mitochondrial bound hexokinase activity as a preventive antioxidant defense: steady-state ADP formation as a regulatory mechanism of membrane potential and reactive oxygen species generation in mitochondria. J. Biol. Chem. 279, 39846-39855
    • (2004) J. Biol. Chem. , vol.279 , pp. 39846-39855
    • Da-Silva, W.S.1    Gomez-Puyou, A.2    De Gomez-Puyou, M.T.3    Moreno-Sanchez, R.4    De Felice, F.G.5    De Meis, L.6    Oliveira, M.F.7    Galina, A.8
  • 28
    • 33846001693 scopus 로고    scopus 로고
    • Mitochondrial creatine kinase activity prevents reactive oxygen species generation: Antioxidant role of mitochondrial kinase-dependent ADP re-cycling activity
    • Meyer, L. E., Machado, L. B., Santiago, A. P., da-Silva, W. S., De Felice, F. G., Holub, O., Oliveira, M. F. and Galina, A. (2006) Mitochondrial creatine kinase activity prevents reactive oxygen species generation: antioxidant role of mitochondrial kinase-dependent ADP re-cycling activity. J. Biol. Chem. 281, 37361-37371
    • (2006) J. Biol. Chem. , vol.281 , pp. 37361-37371
    • Meyer, L.E.1    Machado, L.B.2    Santiago, A.P.3    Da-Silva, W.S.4    De Felice, F.G.5    Holub, O.6    Oliveira, M.F.7    Galina, A.8
  • 29
    • 0034618685 scopus 로고    scopus 로고
    • Glucokinase gene expression is nutritionally regulated in liver of gilthead sea bream (Sparus aurata)
    • Caseras, A., Meton, I., Fernandez, F. and Baanante, I. V. (2000) Glucokinase gene expression is nutritionally regulated in liver of gilthead sea bream (Sparus aurata). Biochim. Biophys. Acta 1493, 135-141
    • (2000) Biochim. Biophys. Acta , vol.1493 , pp. 135-141
    • Caseras, A.1    Meton, I.2    Fernandez, F.3    Baanante, I.V.4
  • 30
    • 37049035363 scopus 로고    scopus 로고
    • Hepatic glucokinase and glucose-6-phosphatase responses to dietary glucose and starch in gilthead sea bream (Sparus aurata) juveniles reared at two temperatures
    • Enes, P., Panserat, S., Kaushik, S. and Oliva-Teles, A. (2008) Hepatic glucokinase and glucose-6-phosphatase responses to dietary glucose and starch in gilthead sea bream (Sparus aurata) juveniles reared at two temperatures. Comp. Biochem. Physiol. A Mol. Integr. Physiol. 149, 80-86
    • (2008) Comp. Biochem. Physiol. A Mol. Integr. Physiol. , vol.149 , pp. 80-86
    • Enes, P.1    Panserat, S.2    Kaushik, S.3    Oliva-Teles, A.4
  • 33
    • 0035045712 scopus 로고    scopus 로고
    • Glucose tolerance and peripheral glucose utilization in rainbow trout (Oncorhynchus mykiss), American eel (Anguilla rostrata), and black bullhead catfish (Ameiurus melas)
    • Legate, N. J., Bonen, A. and Moon, T. W. (2001) Glucose tolerance and peripheral glucose utilization in rainbow trout (Oncorhynchus mykiss), American eel (Anguilla rostrata), and black bullhead catfish (Ameiurus melas). Gen. Comp. Endocrinol. 122, 48-59
    • (2001) Gen. Comp. Endocrinol. , vol.122 , pp. 48-59
    • Legate, N.J.1    Bonen, A.2    Moon, T.W.3
  • 34
    • 0035434641 scopus 로고    scopus 로고
    • Influence of exercise on the activity and the distribution between free and bound forms of glycolytic and associated enzymes in tissues of horse mackerel
    • Lushchak, V. I., Bagnyukova, T. V., Storey, J. M. and Storey, K. B. (2001) Influence of exercise on the activity and the distribution between free and bound forms of glycolytic and associated enzymes in tissues of horse mackerel. Braz. J. Med. Biol. Res. 34, 1055-1064
    • (2001) Braz. J. Med. Biol. Res. , Issue.34 , pp. 1055-1064
    • Lushchak, V.I.1    Bagnyukova, T.V.2    Storey, J.M.3    Storey, K.B.4
  • 35
    • 0002728509 scopus 로고
    • Changes in mitochondrial distribution and diffusion distances in muscle of goldfish upon acclimation to warm and cold temperatures
    • Tyler, S. and Sidell, B. D. (1984) Changes in mitochondrial distribution and diffusion distances in muscle of goldfish upon acclimation to warm and cold temperatures. J. Exp. Zool. 232, 1-9
    • (1984) J. Exp. Zool. , Issue.232 , pp. 1-9
    • Tyler, S.1    Sidell, B.D.2
  • 36
    • 0015511909 scopus 로고
    • The effect of temperature acclimation upon succinic dehydrogenase activity from the epaxial muscle of the common goldfish (Carassius auratus L.) - II. Lipid reactivation of the soluble enzyme
    • Hazel, J. R. (1972) The effect of temperature acclimation upon succinic dehydrogenase activity from the epaxial muscle of the common goldfish (Carassius auratus L.) - II. Lipid reactivation of the soluble enzyme. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 43, 863-882
    • (1972) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.43 , pp. 863-882
    • Hazel, J.R.1
  • 37
    • 0015511691 scopus 로고
    • The effect of temperature acclimation upon succinic dehydrogenase activity from the epaxial muscle of the common goldfish (Carassius auratus L.) - I. Properties of the enzyme and the effect of lipid extraction
    • Hazel, J. R. (1972) The effect of temperature acclimation upon succinic dehydrogenase activity from the epaxial muscle of the common goldfish (Carassius auratus L.) - I. Properties of the enzyme and the effect of lipid extraction. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 43, 837-861
    • (1972) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.43 , pp. 837-861
    • Hazel, J.R.1
  • 38
    • 0018146990 scopus 로고
    • The effect of acclimation temperature on the activation energies of state III respiration and on the unsaturation of membrane lipids of goldfish mitochondria
    • van den Thillart, G. and Modderkolk, J. (1978) The effect of acclimation temperature on the activation energies of state III respiration and on the unsaturation of membrane lipids of goldfish mitochondria. Biochim. Biophys. Acta 510, 38-51
    • (1978) Biochim. Biophys. Acta , vol.510 , pp. 38-51
    • Van Den Thillart, G.1    Modderkolk, J.2
  • 39
    • 0001955487 scopus 로고
    • Responses of goldfish (Carassius auratus L.) muscle to acclimation temperature: Alteration in biochemistry and proportions of different fiber types
    • Sidell, B. D. (1980) Responses of goldfish (Carassius auratus L.) muscle to acclimation temperature: alteration in biochemistry and proportions of different fiber types. Physiol. Zool. 53, 98-107
    • (1980) Physiol. Zool. , vol.53 , pp. 98-107
    • Sidell, B.D.1
  • 40
    • 51249185742 scopus 로고
    • Carbohydrate metabolism of goldfish (Carassius auratus L.). Effects of long term hypoxia-acclimation on enzyme patterns of red muscle, white muscle and liver
    • van den Thillart, G. and Smit, H. (1984) Carbohydrate metabolism of goldfish (Carassius auratus L.). Effects of long term hypoxia-acclimation on enzyme patterns of red muscle, white muscle and liver. J. Comp. Physiol. 154, 477-486
    • (1984) J. Comp. Physiol. , vol.154 , pp. 477-486
    • Van Den Thillart, G.1    Smit, H.2
  • 41
    • 0008307784 scopus 로고    scopus 로고
    • Teleost liver hexokinase- and glucokinase-like enzymes: Partial cDNA cloning and phylogenetic studies in rainbow trout (Oncorhynchus mykiss), common carp (Cyprinus carpio) and gilthead seabream (Sparus aurata)
    • Blin, C., Panserat, S., Medale, F., Gomes, E., Breque, J., Kaushik, S. and Krishnamoorthy, R. (1999) Teleost liver hexokinase- and glucokinase-like enzymes: partial cDNA cloning and phylogenetic studies in rainbow trout (Oncorhyncnus mykiss), common carp (Cyprinus carpio) and gilthead seabream (Sparus aurata). Fish Physiol. Biochem. 21, 93-102 (Pubitemid 129644330)
    • (1999) Fish Physiology and Biochemistry , vol.21 , Issue.2 , pp. 93-102
    • Blin, C.1    Panserat, S.2    Medale, F.3    Gomes, E.4    Breque, J.5    Kaushik, S.6    Krishnamoorthy, R.7
  • 42
    • 0033857109 scopus 로고    scopus 로고
    • Partial molecular cloning and tissue distribution of hexokinase I cDNA in common carp
    • Blin, C., Panserat, S., Kaushik, S. and Krisnamoorthy, R. (2000) Partial molecular cloning and tissue distribution of hexokinase I cDNA in common carp. J. Fish Biol. 56, 1558-1561
    • (2000) J. Fish Biol. , vol.56 , pp. 1558-1561
    • Blin, C.1    Panserat, S.2    Kaushik, S.3    Krisnamoorthy, R.4
  • 43
    • 0034954369 scopus 로고    scopus 로고
    • Ontogenesis of hexokinase I and hexokinase IV (glucokinase) gene expressions in common carp (Cyprinus carpio) related to diet
    • Panserat, S., Fontagne, S., Bergot, P. and Kaushik, S. (2001) Ontogenesis of hexokinase I and hexokinase IV (glucokinase) gene expressions in common carp (Cyprinus carpio) related to diet. Br. J. Nutr. 85, 649-651
    • (2001) Br. J. Nutr. , vol.85 , pp. 649-651
    • Panserat, S.1    Fontagne, S.2    Bergot, P.3    Kaushik, S.4
  • 45
    • 49449120800 scopus 로고
    • A comparative study of glycolysis in red and white muscles of the trout (Salmo gairdneri) and mirror carp (Cyprinus carpio)
    • Johnston, I. A. (1977) A comparative study of glycolysis in red and white muscles of the trout (Salmo gairdneri) and mirror carp (Cyprinus carpio). J. Fish Biol. 11, 575-588
    • (1977) J. Fish Biol. , vol.11 , pp. 575-588
    • Johnston, I.A.1
  • 46
    • 0022272285 scopus 로고
    • Force-velocity characteristics and metabolism in carp muscle fibres following temperature acclimation
    • Johnston, I. A., Sidell, B. D. and Driedzic, W. R. (1985) Force-velocity characteristics and metabolism in carp muscle fibres following temperature acclimation. J. Exp. Biol. 119, 239-249
    • (1985) J. Exp. Biol. , vol.119 , pp. 239-249
    • Johnston, I.A.1    Sidell, B.D.2    Driedzic, W.R.3
  • 47
    • 0013604875 scopus 로고
    • Role of enzyme binding in muscle metabolism of the goldfish
    • Duncan, J. A. and Storey, K. B. (1991) Role of enzyme binding in muscle metabolism of the goldfish. Can. J. Zool. 69, 1571-1576
    • (1991) Can. J. Zool. , vol.69 , pp. 1571-1576
    • Duncan, J.A.1    Storey, K.B.2
  • 48
    • 0022614213 scopus 로고
    • Effects of temperature and thermal acclimation on contractile properties and metabolism of skeletal muscle in the flounder (Platichthys flesus L.)
    • Johnston, I. A. and Wokoma, A. (1986) Effects of temperature and thermal acclimation on contractile properties and metabolism of skeletal muscle in the flounder (Platichthys flesus L.). J. Exp. Biol. 120, 119-130
    • (1986) J. Exp. Biol. , vol.120 , pp. 119-130
    • Johnston, I.A.1    Wokoma, A.2
  • 49
    • 0030832284 scopus 로고    scopus 로고
    • Structural and biochemical analyses of cardiac ventricular enlargement in cold-acclimated striped bass
    • Rodnick, K. J. and Sidell, B. D. (1997) Structural and biochemical analyses of cardiac ventricular enlargement in cold-acclimated striped bass. Am. J. Physiol. Regul. Integr. Comp. Physiol. 273, R252-R258
    • (1997) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.273
    • Rodnick, K.J.1    Sidell, B.D.2
  • 50
    • 0025981250 scopus 로고
    • The effect of acclimation temperature on enzyme activity in Drosophila melanogaster
    • Burnell, A. M., Reaper, C. and Doherty, J. (1991) The effect of acclimation temperature on enzyme activity in Drosophila melanogaster. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 98, 609-614
    • (1991) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.98 , pp. 609-614
    • Burnell, A.M.1    Reaper, C.2    Doherty, J.3
  • 51
    • 0016752950 scopus 로고
    • Comparison of the effects of physical exercise, cold acclimation and repeated injections of isoprenaline on rat muscle enzymes
    • Harri, M. N. and Valtola, J. (1975) Comparison of the effects of physical exercise, cold acclimation and repeated injections of isoprenaline on rat muscle enzymes. Acta Physiol. Scand. 95, 391-399
    • (1975) Acta Physiol. Scand. , vol.95 , pp. 391-399
    • Harri, M.N.1    Valtola, J.2
  • 52
    • 0023481961 scopus 로고
    • Significance of increase in glucose 6-phosphatase activity in brown adipose cells of cold-exposed and starved mice
    • Watanabe, J., Kanamura, S., Tokunaga, H., Sakaida, M. and Kanai, K. (1987) Significance of increase in glucose 6-phosphatase activity in brown adipose cells of cold-exposed and starved mice. Anat. Rec. 219, 39-44
    • (1987) Anat. Rec. , vol.219 , pp. 39-44
    • Watanabe, J.1    Kanamura, S.2    Tokunaga, H.3    Sakaida, M.4    Kanai, K.5
  • 53
    • 0025347236 scopus 로고
    • Neuronal regulation of substrate cycle between glucose 6-phosphate and glucose in brown adipose tissues of cold-exposed mice
    • Suzuki, H., Watanabe, J., Itani, T., Ogawa, R. and Kanamura, S. (1990) Neuronal regulation of substrate cycle between glucose 6-phosphate and glucose in brown adipose tissues of cold-exposed mice. Anat. Rec. 226, 314-319
    • (1990) Anat. Rec. , vol.226 , pp. 314-319
    • Suzuki, H.1    Watanabe, J.2    Itani, T.3    Ogawa, R.4    Kanamura, S.5
  • 54
    • 0025330906 scopus 로고
    • Changes in free and bound forms and total amount of hexokinase isozyme II of rat muscle in response to contractile activity
    • Weber, F. E. and Pette, D. (1990) Changes in free and bound forms and total amount of hexokinase isozyme II of rat muscle in response to contractile activity. Eur. J. Biochem. 191, 85-90
    • (1990) Eur. J. Biochem. , vol.191 , pp. 85-90
    • Weber, F.E.1    Pette, D.2
  • 55
    • 0034932121 scopus 로고    scopus 로고
    • Subcellular distribution and kinetic properties of cytosolic and non-cytosolic hexokinases in maize seedling roots: Implications for hexose phosphorylation
    • da-Silva, W. S., Rezende, G. L. and Galina, A. (2001) Subcellular distribution and kinetic properties of cytosolic and non-cytosolic hexokinases in maize seedling roots: implications for hexose phosphorylation. J. Exp. Bot. 52, 1191-1201
    • (2001) J. Exp. Bot. , vol.52 , pp. 1191-1201
    • Da-Silva, W.S.1    Rezende, G.L.2    Galina, A.3
  • 57
    • 0015276570 scopus 로고
    • The activities of Phosphorylase, hexokinase, phosphofructokinase, lactate dehydrogenase and the glycerol 3-phosphate dehydrogenases in muscles from vertebrates and invertebrates
    • Crabtree, B. and Newsholme, E. A. (1972) The activities of Phosphorylase, hexokinase, phosphofructokinase, lactate dehydrogenase and the glycerol 3-phosphate dehydrogenases in muscles from vertebrates and invertebrates. Biochem. J. 126, 49-58
    • (1972) Biochem. J. , vol.126 , pp. 49-58
    • Crabtree, B.1    Newsholme, E.A.2
  • 58
    • 0021709960 scopus 로고
    • Activities of glucokinase and hexokinase in mammalian and avian livers
    • Stanley, J. C., Dohm, G. L., McManus, B. S. and Newsholme, E. A. (1984) Activities of glucokinase and hexokinase in mammalian and avian livers. Biochem. J. 224, 667-671
    • (1984) Biochem. J. , vol.224 , pp. 667-671
    • Stanley, J.C.1    Dohm, G.L.2    McManus, B.S.3    Newsholme, E.A.4
  • 60
    • 0000154206 scopus 로고
    • The colorimetric determination of phosphorus
    • Fiske, C. H. and Subbarow, Y. (1925) The colorimetric determination of phosphorus. J. Biol. Chem. 66, 375-400
    • (1925) J. Biol. Chem. , vol.66 , pp. 375-400
    • Fiske, C.H.1    Subbarow, Y.2
  • 61
    • 0014413649 scopus 로고
    • Studies on isozymes of hexokinase in animal tissues
    • Schimke, R. T. and Grossbard, L. (1968) Studies on isozymes of hexokinase in animal tissues. Ann. N.Y. Acad. Sci. 151, 332-350
    • (1968) Ann. N.Y. Acad. Sci. , vol.151 , pp. 332-350
    • Schimke, R.T.1    Grossbard, L.2
  • 62
    • 0015964680 scopus 로고
    • Kinetics, mechanism, and regulation of rat skeletal muscle hexokinase
    • Lueck, J. D. and Fromm, H. J. (1974) Kinetics, mechanism, and regulation of rat skeletal muscle hexokinase. J. Biol. Chem. 249, 1341-1347
    • (1974) J. Biol. Chem. , vol.249 , pp. 1341-1347
    • Lueck, J.D.1    Fromm, H.J.2
  • 63
    • 0022386994 scopus 로고
    • Initial rate and isotope exchange studies of rat skeletal muscle hexokinase
    • Ganson, N. J. and Fromm, H. J. (1985) Initial rate and isotope exchange studies of rat skeletal muscle hexokinase. J. Biol. Chem. 260, 12099-12105
    • (1985) J. Biol. Chem. , vol.260 , pp. 12099-12105
    • Ganson, N.J.1    Fromm, H.J.2
  • 65
    • 33745908987 scopus 로고    scopus 로고
    • Sugar sensing and signaling in plants: Conserved and novel mechanisms
    • Rolland, F., Baena-Gonzalez, E. and Sheen, J. (2006) Sugar sensing and signaling in plants: conserved and novel mechanisms. Annu. Rev. Plant Biol. 57, 675-709
    • (2006) Annu. Rev. Plant Biol. , vol.57 , pp. 675-709
    • Rolland, F.1    Baena-Gonzalez, E.2    Sheen, J.3
  • 66
    • 0034988197 scopus 로고    scopus 로고
    • Hexokinase isozyme distribution in human skeletal muscle
    • Ritov, V. B. and Kelley, D. E. (2001) Hexokinase isozyme distribution in human skeletal muscle. Diabetes 50, 1253-1262
    • (2001) Diabetes , vol.50 , pp. 1253-1262
    • Ritov, V.B.1    Kelley, D.E.2
  • 67
    • 0021200432 scopus 로고
    • Fructose is a good substrate for rat liver 'glucokinase' (hexokinase D)
    • Cárdenas, M. L., Rabajille, E. and Niemeyer, H. (1984) Fructose is a good substrate for rat liver 'glucokinase' (hexokinase D). Biochem. J. 222, 363-370
    • (1984) Biochem. J. , vol.222 , pp. 363-370
    • Cárdenas, M.L.1    Rabajille, E.2    Niemeyer, H.3
  • 68
    • 0030729851 scopus 로고    scopus 로고
    • High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria
    • Korshunov, S. S., Skulachev, V. P. and Starkov, A. A. (1997) High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria. FEBS Lett. 416, 15-18
    • (1997) FEBS Lett. , vol.416 , pp. 15-18
    • Korshunov, S.S.1    Skulachev, V.P.2    Starkov, A.A.3
  • 69
    • 0014198143 scopus 로고
    • Mitochondrial hexokinase. Release, rebinding, and location
    • Rose, I. A. and Warms, J. V. (1967) Mitochondrial hexokinase. Release, rebinding, and location. J. Biol. Chem. 242, 1635-1645
    • (1967) J. Biol. Chem. , vol.242 , pp. 1635-1645
    • Rose, I.A.1    Warms, J.V.2
  • 70
    • 0032545759 scopus 로고    scopus 로고
    • Clotrimazole and bifonazole detach hexokinase from mitochondria of melanoma cells
    • Penso, J. and Beitner, R. (1998) Clotrimazole and bifonazole detach hexokinase from mitochondria of melanoma cells. Eur. J. Pharmacol. 342, 113-117
    • (1998) Eur. J. Pharmacol. , vol.342 , pp. 113-117
    • Penso, J.1    Beitner, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.