메뉴 건너뛰기




Volumn 579, Issue 7, 2005, Pages 1607-1612

The effect of calcium ions on subcellular localization of aldolase-FBPase complex in skeletal muscle

Author keywords

Aldolase; Calcium; Co localization; FBPase; Glyconeogenesis; Actinin

Indexed keywords

ALPHA ACTININ; CALCIUM ION; FRUCTOSE BISPHOSPHATASE; FRUCTOSE BISPHOSPHATE ALDOLASE;

EID: 14844330060     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.01.071     Document Type: Article
Times cited : (27)

References (27)
  • 1
    • 0034726708 scopus 로고    scopus 로고
    • Muscle aldolase decreases muscle FBPase sensitivity toward AMP inhibition
    • D. Rakus, and A. Dzugaj Muscle aldolase decreases muscle FBPase sensitivity toward AMP inhibition Biochem. Biophys. Res. Commun. 275 2000 611 616
    • (2000) Biochem. Biophys. Res. Commun. , vol.275 , pp. 611-616
    • Rakus, D.1    Dzugaj, A.2
  • 2
    • 0028979318 scopus 로고
    • Kinetic properties of d-fructose-1,6-bisphosphate 1-phosphohydrolase isolated from human muscle
    • K. Skalecki, W. Mularczyk, and A. Dzugaj Kinetic properties of d-fructose-1,6-bisphosphate 1-phosphohydrolase isolated from human muscle Biochem. J. 310 1995 1029 1035
    • (1995) Biochem. J. , vol.310 , pp. 1029-1035
    • Skalecki, K.1    Mularczyk, W.2    Dzugaj, A.3
  • 3
    • 0037478975 scopus 로고    scopus 로고
    • Muscle FBPase in a complex with muscle aldolase is insensitive to AMP inhibition
    • D. Rakus, M. Pasek, H. Krotkiewski, and A. Dzugaj Muscle FBPase in a complex with muscle aldolase is insensitive to AMP inhibition FEBS Lett. 547 2003 11 14
    • (2003) FEBS Lett. , vol.547 , pp. 11-14
    • Rakus, D.1    Pasek, M.2    Krotkiewski, H.3    Dzugaj, A.4
  • 4
    • 9744229890 scopus 로고    scopus 로고
    • Interaction between muscle aldolase and muscle fructose 1,6-bisphosphatase results in the substrate channeling
    • D. Rakus, M. Pasek, H. Krotkiewski, and A. Dzugaj Interaction between muscle aldolase and muscle fructose 1,6-bisphosphatase results in the substrate channeling Biochemistry 43 2004 14948 14957
    • (2004) Biochemistry , vol.43 , pp. 14948-14957
    • Rakus, D.1    Pasek, M.2    Krotkiewski, H.3    Dzugaj, A.4
  • 5
    • 0242299766 scopus 로고    scopus 로고
    • Colocalization of muscle FBPase and muscle aldolase on both sides of the Z-line
    • D. Rakus, P. Mamczur, A. Gizak, D. Dus, and A. Dzugaj Colocalization of muscle FBPase and muscle aldolase on both sides of the Z-line Biochem. Biophys. Res. Commun. 311 2003 294 299
    • (2003) Biochem. Biophys. Res. Commun. , vol.311 , pp. 294-299
    • Rakus, D.1    Mamczur, P.2    Gizak, A.3    Dus, D.4    Dzugaj, A.5
  • 6
    • 0025359442 scopus 로고
    • Enzyme-enzyme interactions and their metabolic role
    • P.A. Srere, and J. Ovadi Enzyme-enzyme interactions and their metabolic role FEBS Lett. 268 1990 360 364
    • (1990) FEBS Lett. , vol.268 , pp. 360-364
    • Srere, P.A.1    Ovadi, J.2
  • 7
    • 0033991699 scopus 로고    scopus 로고
    • Macromolecular compartmentation and channeling
    • J. Ovadi, and P.A. Srere Macromolecular compartmentation and channeling Int. Rev. Cytol. 192 2000 255 280
    • (2000) Int. Rev. Cytol. , vol.192 , pp. 255-280
    • Ovadi, J.1    Srere, P.A.2
  • 8
    • 0034494381 scopus 로고    scopus 로고
    • Coupling of creatine kinase to glycolytic enzymes at the sarcomeric I-band of skeletal muscle: A biochemical study in situ
    • T. Kraft, T. Hornemann, M. Stolz, V. Nier, and T. Wallimann Coupling of creatine kinase to glycolytic enzymes at the sarcomeric I-band of skeletal muscle: a biochemical study in situ J. Muscle Res. Cell. Motil. 21 2000 691 703
    • (2000) J. Muscle Res. Cell. Motil. , vol.21 , pp. 691-703
    • Kraft, T.1    Hornemann, T.2    Stolz, M.3    Nier, V.4    Wallimann, T.5
  • 9
    • 0042008053 scopus 로고    scopus 로고
    • The network of calcium regulation in muscle
    • N.A. Martonosi, and S. Pikula The network of calcium regulation in muscle Acta Biochim. Pol. 50 2003 1 30
    • (2003) Acta Biochim. Pol. , vol.50 , pp. 1-30
    • Martonosi, N.A.1    Pikula, S.2
  • 10
    • 0027312402 scopus 로고
    • Intracellular calcium homeostasis in cardiac myocytes
    • W.H. Barry, and J.H. Bridge Intracellular calcium homeostasis in cardiac myocytes Circulation 87 1993 1806 1815
    • (1993) Circulation , vol.87 , pp. 1806-1815
    • Barry, W.H.1    Bridge, J.H.2
  • 12
    • 0014796144 scopus 로고
    • Effect of bivalent cations on some enzymes of gluconeogenesis
    • M.J. Wimhurst, and K.L. Manchester Effect of bivalent cations on some enzymes of gluconeogenesis Biochem. J. 118 1970 19P
    • (1970) Biochem. J. , vol.118
    • Wimhurst, M.J.1    Manchester, K.L.2
  • 14
    • 6344253345 scopus 로고    scopus 로고
    • Calcium inhibits muscle FBPase and affects its intracellular localization in cardiomyocytes
    • A. Gizak, M. Majkowski, D. Dus, and A. Dzugaj Calcium inhibits muscle FBPase and affects its intracellular localization in cardiomyocytes FEBS Lett. 576 2004 445 448
    • (2004) FEBS Lett. , vol.576 , pp. 445-448
    • Gizak, A.1    Majkowski, M.2    Dus, D.3    Dzugaj, A.4
  • 15
    • 0014600740 scopus 로고
    • Isolation of fructose diphosphate aldolases A, B, and C
    • E.E. Penhoet, M. Kochman, and J.W. Rutter Isolation of fructose diphosphate aldolases A, B, and C Biochemistry 8 1969 4391 4395
    • (1969) Biochemistry , vol.8 , pp. 4391-4395
    • Penhoet, E.E.1    Kochman, M.2    Rutter, J.W.3
  • 16
    • 0034283264 scopus 로고    scopus 로고
    • Kinetic properties of pig (Sus scrofa domestica) and bovine (Bos Taurus) d-fructose-1,6-bisphosphate 1-phosphohydrolase (F1,6Bpase): Liver-like isozymes in mammalian lung tissue
    • D. Rakus, K. Skalecki, and A. Dzugaj Kinetic properties of pig (Sus scrofa domestica) and bovine (Bos Taurus) d-fructose-1,6-bisphosphate 1-phosphohydrolase (F1,6Bpase): liver-like isozymes in mammalian lung tissue Comp. Biochem. Physiol. B 127 2000 123 134
    • (2000) Comp. Biochem. Physiol. B , vol.127 , pp. 123-134
    • Rakus, D.1    Skalecki, K.2    Dzugaj, A.3
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0017033341 scopus 로고
    • Conjugation of antibodies with fluorochromes: Modifications to the standard methods
    • J.W. Goding Conjugation of antibodies with fluorochromes: modifications to the standard methods J. Immunol. Methods 13 1976 215 226
    • (1976) J. Immunol. Methods , vol.13 , pp. 215-226
    • Goding, J.W.1
  • 20
    • 0027418205 scopus 로고
    • Measurement of co-localization of objects in dual-color confocal images
    • M.E. Manders, F.J. Verbeek, and J.A. Aten Measurement of co-localization of objects in dual-color confocal images J. Micros. 169 1993 375 382
    • (1993) J. Micros. , vol.169 , pp. 375-382
    • Manders, M.E.1    Verbeek, F.J.2    Aten, J.A.3
  • 21
    • 0037219728 scopus 로고    scopus 로고
    • Immunohistochemical localization of human fructose-1,6-bisphosphatase in subcellular structures of myocytes, Histol
    • A. Gizak, D. Rakus, and A. Dzugaj Immunohistochemical localization of human fructose-1,6-bisphosphatase in subcellular structures of myocytes, Histol Histopathology 18 2003 135 142
    • (2003) Histopathology , vol.18 , pp. 135-142
    • Gizak, A.1    Rakus, D.2    Dzugaj, A.3
  • 22
    • 0036848504 scopus 로고    scopus 로고
    • Glycogen resynthesis in the absence of food ingestion during recovery from moderate or high intensity physical activity: Novel insights from rat and human studies
    • P.A. Fournier, L. Brau, L.D. Ferreira, T. Fairchild, G. Raja, A. James, and T.N. Palmer Glycogen resynthesis in the absence of food ingestion during recovery from moderate or high intensity physical activity: novel insights from rat and human studies Comp. Biochem. Physiol. A 133 2002 755 763
    • (2002) Comp. Biochem. Physiol. a , vol.133 , pp. 755-763
    • Fournier, P.A.1    Brau, L.2    Ferreira, L.D.3    Fairchild, T.4    Raja, G.5    James, A.6    Palmer, T.N.7
  • 23
    • 0022483071 scopus 로고
    • Calcium-dependent activation of glycogen phosphorylase in rat pheochromocytoma PC12 cells by nerve growth factor
    • L.H. Davis, and F.C. Kauffman Calcium-dependent activation of glycogen phosphorylase in rat pheochromocytoma PC12 cells by nerve growth factor Biochem. Biophys. Res. Commun. 138 1986 917 924
    • (1986) Biochem. Biophys. Res. Commun. , vol.138 , pp. 917-924
    • Davis, L.H.1    Kauffman, F.C.2
  • 24
    • 0014963089 scopus 로고
    • Control of phosphorylase activity in a muscle glycogen particle. II. Activation by calcium
    • L.M. Heilmeyer, F. Meyer, R.H. Haschke, and E.H. Fischer Control of phosphorylase activity in a muscle glycogen particle. II. Activation by calcium J. Biol. Chem. 245 1970 6649 6656
    • (1970) J. Biol. Chem. , vol.245 , pp. 6649-6656
    • Heilmeyer, L.M.1    Meyer, F.2    Haschke, R.H.3    Fischer, E.H.4
  • 25
    • 0037369214 scopus 로고    scopus 로고
    • A forty-year memoir of research on the regulation of glucose transport into muscle
    • J.O. Holloszy A forty-year memoir of research on the regulation of glucose transport into muscle Am. J. Physiol. Endocrinol. Metab. 284 2003 E453 E467
    • (2003) Am. J. Physiol. Endocrinol. Metab. , vol.284
    • Holloszy, J.O.1
  • 26
    • 0016440506 scopus 로고
    • On the association of glycolytic enzymes with structural proteins of skeletal muscle
    • F.M. Clarke, and C.J. Masters On the association of glycolytic enzymes with structural proteins of skeletal muscle Biochim. Biophys. Acta 381 1975 37 46
    • (1975) Biochim. Biophys. Acta , vol.381 , pp. 37-46
    • Clarke, F.M.1    Masters, C.J.2
  • 27
    • 0016670453 scopus 로고
    • Immunofluorescent localization of glycogenolytic and glycolytic enzyme proteins and of malate dehydrogenase isozymes in cross-striated skeletal muscle and heart of the rabbit
    • G. Dolken, E. Leisner, and D. Pette Immunofluorescent localization of glycogenolytic and glycolytic enzyme proteins and of malate dehydrogenase isozymes in cross-striated skeletal muscle and heart of the rabbit Histochemistry 43 1975 113 121
    • (1975) Histochemistry , vol.43 , pp. 113-121
    • Dolken, G.1    Leisner, E.2    Pette, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.