메뉴 건너뛰기




Volumn 140, Issue 1, 2005, Pages 37-43

Localization of chicken muscle FBPase in cardiomyocyte nuclei

Author keywords

Bis Tris propane; BTP; Cardiomyocyte; D Fructose 1,6 bisphosphate 1 phosphohydrolase, EC 3.1.3.11 ; EDTA; ethylenediaminetetraacetic acid; FBPase; Fru 1,6P 2; Fructose 1,6 bisphosphatase; Fructose 1,6 bisphosphate; Gallus domesticus; NADP; Nucleus

Indexed keywords

ADENOSINE PHOSPHATE; FRUCTOSE BISPHOSPHATASE;

EID: 11144283574     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpc.2004.04.016     Document Type: Article
Times cited : (7)

References (35)
  • 1
    • 0032842869 scopus 로고    scopus 로고
    • Rat muscle fructose-1,6-bisphosphatase: Cloning of the cDNA, expression of the recombinant enzyme, and expression analysis in different tissues
    • Al-Robaiy S., Eschrich K. Rat muscle fructose-1,6-bisphosphatase: cloning of the cDNA, expression of the recombinant enzyme, and expression analysis in different tissues. Biol. Chem. 380:1999;1079-1085
    • (1999) Biol. Chem. , vol.380 , pp. 1079-1085
    • Al-Robaiy, S.1    Eschrich, K.2
  • 2
    • 0017169244 scopus 로고
    • Blood metabolites and glucose metabolism in the fed and fasted chicken
    • Belo P.S., Romsos D.R., Leville G.A. Blood metabolites and glucose metabolism in the fed and fasted chicken. J. Nutr. 106:1976;1135-1143
    • (1976) J. Nutr. , vol.106 , pp. 1135-1143
    • Belo, P.S.1    Romsos, D.R.2    Leville, G.A.3
  • 4
    • 0010557267 scopus 로고
    • Immunochemical techniques for the identification and estimation of macromolecules
    • R.H. Burdon, & P.H. van Knippenberg. Amsterdam: Elsevier
    • Clausen J. Immunochemical techniques for the identification and estimation of macromolecules. Burdon R.H., van Knippenberg P.H. Laboratory Techniques in Biochemistry and Molecular Biology. 1988;281 Elsevier, Amsterdam
    • (1988) Laboratory Techniques in Biochemistry and Molecular Biology , pp. 281
    • Clausen, J.1
  • 6
    • 0030853642 scopus 로고    scopus 로고
    • Muscle glycogen synthase translocates from the cell nucleus to the cystosol in response to glucose
    • Ferrer J.C., Baque S., Guinovart J.J. Muscle glycogen synthase translocates from the cell nucleus to the cystosol in response to glucose. FEBS Lett. 415:1997;249-252
    • (1997) FEBS Lett. , vol.415 , pp. 249-252
    • Ferrer, J.C.1    Baque, S.2    Guinovart, J.J.3
  • 8
    • 0037468610 scopus 로고    scopus 로고
    • FBPase is in the nuclei of cardiomyocytes
    • Gizak A., Dzugaj A. FBPase is in the nuclei of cardiomyocytes. FEBS Lett. 539:2003;51-55
    • (2003) FEBS Lett. , vol.539 , pp. 51-55
    • Gizak, A.1    Dzugaj, A.2
  • 10
    • 0037219728 scopus 로고    scopus 로고
    • Immunohistochemical localization of human fructose-1,6-bisphosphatase in subcellular structures of myocytes
    • Gizak A., Rakus D., Dzugaj A. Immunohistochemical localization of human fructose-1,6-bisphosphatase in subcellular structures of myocytes. Histol. Histopathol. 18:2003;135-142
    • (2003) Histol. Histopathol. , vol.18 , pp. 135-142
    • Gizak, A.1    Rakus, D.2    Dzugaj, A.3
  • 11
    • 0029870297 scopus 로고    scopus 로고
    • Post-exercise lactate metabolism: A comparative review of sites, pathways, and regulation
    • Gleeson T.T. Post-exercise lactate metabolism: a comparative review of sites, pathways, and regulation. Annu. Rev. Physiol. 58:1996;5655-5681
    • (1996) Annu. Rev. Physiol. , vol.58 , pp. 5655-5681
    • Gleeson, T.T.1
  • 12
    • 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. 227:1970;680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 3042778425 scopus 로고    scopus 로고
    • Nuclear localization of aldolase a in pig cardiomyocytes
    • Mamczur P., Dzugaj A. Nuclear localization of aldolase A in pig cardiomyocytes. Histol. Histopathol. 19:2004;753-758
    • (2004) Histol. Histopathol. , vol.19 , pp. 753-758
    • Mamczur, P.1    Dzugaj, A.2
  • 15
    • 0016746158 scopus 로고
    • Comparative enzymatic properties of avian liver and skeletal muscle D-fructose-1,6-bisphosphate 1-phosphohydrolase
    • Marquardt R.R., Olson J.P. Comparative enzymatic properties of avian liver and skeletal muscle D-fructose-1,6-bisphosphate 1-phosphohydrolase. Can. J. Biochem. 53:1975;1214-1219
    • (1975) Can. J. Biochem. , vol.53 , pp. 1214-1219
    • Marquardt, R.R.1    Olson, J.P.2
  • 16
    • 0025610673 scopus 로고
    • Evidence for the presence of rat liver glucokinase in the nucleus as well as in the cytoplasm
    • Miwa I., Mitsuyama S., Toyoda Y., Nonogaki T., Aoki S., Okuda J. Evidence for the presence of rat liver glucokinase in the nucleus as well as in the cytoplasm. Biochem. Int. 22:1990;759-767
    • (1990) Biochem. Int. , vol.22 , pp. 759-767
    • Miwa, I.1    Mitsuyama, S.2    Toyoda, Y.3    Nonogaki, T.4    Aoki, S.5    Okuda, J.6
  • 17
    • 0019887960 scopus 로고
    • The role of fructose 2,6-bisphosphate in regulation of fructose-1,6-bis-phosphatase
    • Pilkis S.J., El-Maghrabi M.R., McGrane M.M., Pilkis J., Claus T.H. The role of fructose 2,6-bisphosphate in regulation of fructose-1,6-bis-phosphatase. J. Biol. Chem. 256:1981;3619-3622
    • (1981) J. Biol. Chem. , vol.256 , pp. 3619-3622
    • Pilkis, S.J.1    El-Maghrabi, M.R.2    McGrane, M.M.3    Pilkis, J.4    Claus, T.H.5
  • 18
    • 0032053510 scopus 로고    scopus 로고
    • Modulation of DNA polymerases alpha, delta and epsilon by lactate dehydrogenase and 3-phosphoglycerate kinase
    • Popanda O., Fox G., Thielmann H.W. Modulation of DNA polymerases alpha, delta and epsilon by lactate dehydrogenase and 3-phosphoglycerate kinase. Biochim. Biophys. Acta. 1397:1998;102-117
    • (1998) Biochim. Biophys. Acta , vol.1397 , pp. 102-117
    • Popanda, O.1    Fox, G.2    Thielmann, H.W.3
  • 19
    • 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
    • Rakus D., Skalecki K., Dzugaj A. 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
  • 20
    • 0037906790 scopus 로고    scopus 로고
    • Rabbit muscle fructose-1,6-bisphosphatase is phosphorylated in vivo
    • Rakus D., Zarzycki M., Dzugaj A. Rabbit muscle fructose-1,6- bisphosphatase is phosphorylated in vivo. Acta Biochim. Pol. 50:2003;115-121
    • (2003) Acta Biochim. Pol. , vol.50 , pp. 115-121
    • Rakus, D.1    Zarzycki, M.2    Dzugaj, A.3
  • 21
    • 0027214981 scopus 로고
    • Glycolytic enzymes as DNA binding proteins
    • Ronai Z. Glycolytic enzymes as DNA binding proteins. Int. J. Biochem. 25:1993;1073-1076
    • (1993) Int. J. Biochem. , vol.25 , pp. 1073-1076
    • Ronai, Z.1
  • 22
    • 0028835588 scopus 로고
    • Distinguishable substrate pools for muscle glyconeogenesis in lactate-supplemented recovery from exercise
    • Ryan C., Radziuk J. Distinguishable substrate pools for muscle glyconeogenesis in lactate-supplemented recovery from exercise. Am. J. Physiol. 269:1995;E538-E550
    • (1995) Am. J. Physiol. , vol.269
    • Ryan, C.1    Radziuk, J.2
  • 23
    • 0342264393 scopus 로고    scopus 로고
    • Subcellular localization of aldolase B
    • Saez D.E., Slebe J.C. Subcellular localization of aldolase B. J. Cell. Biochem. 78:2000;62-72
    • (2000) J. Cell. Biochem. , vol.78 , pp. 62-72
    • Saez, D.E.1    Slebe, J.C.2
  • 24
    • 0030475850 scopus 로고    scopus 로고
    • Localization of the fructose 1,6-bisphosphatase at the nuclear periphery
    • Saez D.E., Figueroa C.D., Concha I.I., Slebe J.C. Localization of the fructose 1,6-bisphosphatase at the nuclear periphery. J. Cell. Biochem. 63:1996;453-462
    • (1996) J. Cell. Biochem. , vol.63 , pp. 453-462
    • Saez, D.E.1    Figueroa, C.D.2    Concha, I.I.3    Slebe, J.C.4
  • 26
    • 0028920008 scopus 로고
    • Colocalization of fructose-1,6-bisphosphatase and glial fibrillary acidic protein in rat brain
    • Schmoll D., Cesar M., Fuhrmann E., Hamprecht B. Colocalization of fructose-1,6-bisphosphatase and glial fibrillary acidic protein in rat brain. Brain Res. 677:1995;341-344
    • (1995) Brain Res. , vol.677 , pp. 341-344
    • Schmoll, D.1    Cesar, M.2    Fuhrmann, E.3    Hamprecht, B.4
  • 27
    • 0030746213 scopus 로고    scopus 로고
    • Role of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in normal cell function and in cell pathology
    • Sirover M.A. Role of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in normal cell function and in cell pathology. J. Cell. Biochem. 66:1997;133-140
    • (1997) J. Cell. Biochem. , vol.66 , pp. 133-140
    • Sirover, M.A.1
  • 28
    • 0028979318 scopus 로고
    • Kinetic properties of D-fructose-1,6-bisphosphate 1-phosphohydrolase isolated from human muscle
    • Skalecki K., Mularczyk W., Dzugaj A. 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
  • 30
    • 0035925055 scopus 로고    scopus 로고
    • Characterization of the mouse liver fructose-1,6-bisphosphatase gene
    • Stein S., Liehr T., Eschrich K. Characterization of the mouse liver fructose-1,6-bisphosphatase gene. Gene. 264:2001;215-224
    • (2001) Gene , vol.264 , pp. 215-224
    • Stein, S.1    Liehr, T.2    Eschrich, K.3
  • 31
  • 32
    • 0032496619 scopus 로고    scopus 로고
    • Isolation and characterization of an allelic cDNA for human muscle fructose-1,6-bisphosphatase
    • Tillmann H., Eschrich K. Isolation and characterization of an allelic cDNA for human muscle fructose-1,6-bisphosphatase. Gene. 212:1998;295-304
    • (1998) Gene , vol.212 , pp. 295-304
    • Tillmann, H.1    Eschrich, K.2
  • 33
    • 0037193694 scopus 로고    scopus 로고
    • Fructose-1,6-bisphosphatase genes in animals
    • Tillmann H., Bernhard D., Eschrich K. Fructose-1,6-bisphosphatase genes in animals. Gene. 291:2002;57-66
    • (2002) Gene , vol.291 , pp. 57-66
    • Tillmann, H.1    Bernhard, D.2    Eschrich, K.3
  • 34
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U. S. A. 76:1979;4350-4354
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 35
    • 0019568187 scopus 로고
    • Inhibition of fructose-1,6-bisphosphatase by fructose-2,6-bisphosphate
    • Van Schaftingen E., Hers H.G. Inhibition of fructose-1,6-bisphosphatase by fructose-2,6-bisphosphate. Proc. Natl. Acad. Sci. U. S. A. 78:1981;2861-2863
    • (1981) Proc. Natl. Acad. Sci. U. S. A. , vol.78 , pp. 2861-2863
    • Van Schaftingen, E.1    Hers, H.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.