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Volumn 41, Issue 2, 2013, Pages 674-680

Sedoheptulose kinase regulates cellular carbohydrate metabolism by sedoheptulose 7-phosphate supply

Author keywords

Carbohydrate metabolism; Macrophage activation; Pentose phosphate pathway; Redox regulation; Sedoheptulose 7 phosphate; Sedoheptulose kinase

Indexed keywords

CARBOHYDRATE DERIVATIVE; CYSTINE; FRUCTOSE BISPHOSPHATE ALDOLASE; PHOSPHOTRANSFERASE; SEDOHEPTULOSE 7 PHOSPHATE; SEDOHEPTULOSE KINASE; TRANSALDOLASE; TRANSKETOLASE; UNCLASSIFIED DRUG;

EID: 84875386938     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20120354     Document Type: Review
Times cited : (24)

References (50)
  • 1
    • 0037795745 scopus 로고    scopus 로고
    • The oxidative pentose phosphate pathway: Structure and organisation
    • Kruger, N.J. and von Schaewen, A. (2003) The oxidative pentose phosphate pathway: structure and organisation. Curr. Opin. Plant Biol. 6, 236-246
    • (2003) Curr. Opin. Plant Biol. , vol.6 , pp. 236-246
    • Kruger, N.J.1    Von Schaewen, A.2
  • 2
    • 57649178844 scopus 로고    scopus 로고
    • The biochemistry, metabolism and inherited defects of the pentose phosphate pathway: A review
    • Wamelink, M.M., Struys, E.A. and Jakobs, C. (2008) The biochemistry, metabolism and inherited defects of the pentose phosphate pathway: a review. J. Inherited Metab. Dis. 31, 703-717
    • (2008) J. Inherited Metab. Dis. , vol.31 , pp. 703-717
    • Wamelink, M.M.1    Struys, E.A.2    Jakobs, C.3
  • 3
    • 63049112606 scopus 로고    scopus 로고
    • Transaldolase: From biochemistry to human disease
    • Samland, A.K. and Sprenger, G.A. (2009) Transaldolase: from biochemistry to human disease. Int. J. Biochem. Cell Biol. 41, 1482-1494
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 1482-1494
    • Samland, A.K.1    Sprenger, G.A.2
  • 5
    • 0003121691 scopus 로고
    • Sedoheptulose, a new sugar from sedum spectabile
    • La Forge, F.B. and Hudson, C.S. (1917) Sedoheptulose, a new sugar from Sedum spectabile. J. Biol. Chem. 30, 61-77
    • (1917) J. Biol. Chem. , vol.30 , pp. 61-77
    • La Forge, F.B.1    Hudson, C.S.2
  • 6
    • 0014399667 scopus 로고
    • The occurrence of sedoheptulose in human urine
    • Pitkanen, E. and Sahlstrom, K. (1968) The occurrence of sedoheptulose in human urine. Ann. Med. Exp. Biol. Fenn. 46, 295-300
    • (1968) Ann. Med. Exp. Biol. Fenn. , vol.46 , pp. 295-300
    • Pitkanen, E.1    Sahlstrom, K.2
  • 7
    • 79851510475 scopus 로고    scopus 로고
    • Elevated concentrations of sedoheptulose in bloodspots of patients with cystinosis caused by the 57-kb deletion: Implications for diagnostics and neonatal screening
    • Wamelink, M.M., Struys, E.A., Jansen, E.E., Blom, H.J., Vilboux, T., Gahl, W.A., Komhoff, M., Jakobs, C. and Levtchenko, E.N. (2011) Elevated concentrations of sedoheptulose in bloodspots of patients with cystinosis caused by the 57-kb deletion: implications for diagnostics and neonatal screening. Mol. Genet. Metab. 102, 339-342
    • (2011) Mol. Genet. Metab. , vol.102 , pp. 339-342
    • Wamelink, M.M.1    Struys, E.A.2    Jansen, E.E.3    Blom, H.J.4    Vilboux, T.5    Gahl, W.A.6    Komhoff, M.7    Jakobs, C.8    Levtchenko, E.N.9
  • 10
    • 42049085325 scopus 로고    scopus 로고
    • Sedoheptulokinase deficiency due to a 57-kb deletion in cystinosis patients causes urinary accumulation of sedoheptulose: Elucidation of the carkl gene
    • Wamelink, M.M., Struys, E.A., Jansen, E.E., Levtchenko, E.N., Zijlstra, F.S., Engelke, U., Blom, H.J., Jakobs, C. and Wevers, R.A. (2008) Sedoheptulokinase deficiency due to a 57-kb deletion in cystinosis patients causes urinary accumulation of sedoheptulose: elucidation of the CARKL gene. Hum. Mutat. 29, 532-536
    • (2008) Hum. Mutat. , vol.29 , pp. 532-536
    • Wamelink, M.M.1    Struys, E.A.2    Jansen, E.E.3    Levtchenko, E.N.4    Zijlstra, F.S.5    Engelke, U.6    Blom, H.J.7    Jakobs, C.8    Wevers, R.A.9
  • 11
    • 53049096537 scopus 로고    scopus 로고
    • Characterization of mammalian sedoheptulokinase and mechanism of formation of erythritol in sedoheptulokinase deficiency
    • Kardon, T., Stroobant, V., Veiga-da-Cunha, M. and Schaftingen, E.V. (2008) Characterization of mammalian sedoheptulokinase and mechanism of formation of erythritol in sedoheptulokinase deficiency. FEBS Lett. 582, 3330-3334
    • (2008) FEBS Lett. , vol.582 , pp. 3330-3334
    • Kardon, T.1    Stroobant, V.2    Veiga-da-Cunha, M.3    Schaftingen, E.V.4
  • 12
    • 17344382077 scopus 로고    scopus 로고
    • The genomic region encompassing the nephropathic cystinosis gene (ctns): Complete sequencing of a 200-kb segment and discovery of a novel gene within the common cystinosis-causing deletion
    • Touchman, J.W., Anikster, Y., Dietrich, N.L., Maduro, V.V., McDowell, G., Shotelersuk, V., Bouffard, G.G., Beckstrom-Sternberg, S.M., Gahl, W.A. and Green, E.D. (2000) The genomic region encompassing the nephropathic cystinosis gene (CTNS): complete sequencing of a 200-kb segment and discovery of a novel gene within the common cystinosis-causing deletion. Genome Res. 10, 165-173
    • (2000) Genome Res. , vol.10 , pp. 165-173
    • Touchman, J.W.1    Anikster, Y.2    Dietrich, N.L.3    Maduro, V.V.4    McDowell, G.5    Shotelersuk, V.6    Bouffard, G.G.7    Beckstrom-Sternberg, S.M.8    Gahl, W.A.9    Green, E.D.10
  • 13
    • 0034835289 scopus 로고    scopus 로고
    • The promoter of a lysosomal membrane transporter gene, ctns, binds sp-1, shares sequences with the promoter of an adjacent gene, carkl, and causes cystinosis if mutated in a critical region
    • Phornphutkul, C., Anikster, Y., Huizing, M., Braun, P., Brodie, C., Chou, J.Y. and Gahl, W.A. (2001) The promoter of a lysosomal membrane transporter gene, CTNS, binds Sp-1, shares sequences with the promoter of an adjacent gene, CARKL, and causes cystinosis if mutated in a critical region. Am. J. Hum. Genet. 69, 712-721
    • (2001) Am. J. Hum. Genet. , vol.69 , pp. 712-721
    • Phornphutkul, C.1    Anikster, Y.2    Huizing, M.3    Braun, P.4    Brodie, C.5    Chou, J.Y.6    Gahl, W.A.7
  • 14
    • 84870410249 scopus 로고    scopus 로고
    • Cystinosis: The evolution of a treatable disease
    • Nesterova, G. and Gahl, W.A. (2013) Cystinosis: the evolution of a treatable disease. Pediatr. Nephrol. 28, 51-59
    • (2013) Pediatr. Nephrol. , vol.28 , pp. 51-59
    • Nesterova, G.1    Gahl, W.A.2
  • 16
    • 79961129117 scopus 로고    scopus 로고
    • The 57 kb deletion in cystinosis patients extends into trpv1 causing dysregulation of transcription in peripheral blood mononuclear cells
    • Freed, K.A., Blangero, J., Howard, T., Johnson, M.P., Curran, J.E., Garcia, Y.R., Lan, H.C., Abboud, H.E. and Moses, E.K. (2011) The 57 kb deletion in cystinosis patients extends into TRPV1 causing dysregulation of transcription in peripheral blood mononuclear cells. J. Med. Genet. 48, 563-566
    • (2011) J. Med. Genet. , vol.48 , pp. 563-566
    • Freed, K.A.1    Blangero, J.2    Howard, T.3    Johnson, M.P.4    Curran, J.E.5    Garcia, Y.R.6    Lan, H.C.7    Abboud, H.E.8    Moses, E.K.9
  • 19
    • 0019628397 scopus 로고
    • Synthesis of sedoheptulose from non-dialyzable, endogenous substrates in mammalian tissue extracts
    • Hipps, P.P., Ackermann, K., Holland, W.H. and Sherman, W.R. (1981) Synthesis of sedoheptulose from non-dialyzable, endogenous substrates in mammalian tissue extracts. Carbohydr. Res. 96, 1-6
    • (1981) Carbohydr. Res. , vol.96 , pp. 1-6
    • Hipps, P.P.1    Ackermann, K.2    Holland, W.H.3    Sherman, W.R.4
  • 20
    • 84869089892 scopus 로고    scopus 로고
    • 7-O-Galloyl-d-sedoheptulose ameliorates renal damage triggered by reactive oxygen species-sensitive pathway of inflammation and apoptosis
    • Park, C.H., Noh, J.S., Tanaka, T. and Yokozawa, T. (2012) 7-O-Galloyl-d-sedoheptulose ameliorates renal damage triggered by reactive oxygen species-sensitive pathway of inflammation and apoptosis. J. Pharm. Pharmacol. 64, 1730-1740
    • (2012) J. Pharm. Pharmacol. , vol.64 , pp. 1730-1740
    • Park, C.H.1    Noh, J.S.2    Tanaka, T.3    Yokozawa, T.4
  • 22
    • 0036138692 scopus 로고    scopus 로고
    • Postulated physiological roles of the seven-carbon sugars, mannoheptulose, and perseitol in avocado
    • Liu, X., Sievert, J., Arpaia, M.L. and Madore, M.A. (2002) Postulated physiological roles of the seven-carbon sugars, mannoheptulose, and perseitol in avocado. J. Am. Soc. Hort. Sci. 127, 108-114
    • (2002) J. Am. Soc. Hort. Sci. , vol.127 , pp. 108-114
    • Liu, X.1    Sievert, J.2    Arpaia, M.L.3    Madore, M.A.4
  • 23
    • 12344323379 scopus 로고
    • Effects of d-mannoheptulose and d-sedoheptulose on blood glucose and ketone bodies in the rat
    • Simon, E., Scow, R.O. and Chernick, S.S. (1961) Effects of d-mannoheptulose and d-sedoheptulose on blood glucose and ketone bodies in the rat. Am. J. Physiol. 201, 1073-1077
    • (1961) Am. J. Physiol. , vol.201 , pp. 1073-1077
    • Simon, E.1    Scow, R.O.2    Chernick, S.S.3
  • 25
    • 0344854011 scopus 로고
    • Purification and properties of yeast transaldolase
    • Horecker, B.L. and Smyrniotis, P.Z. (1955) Purification and properties of yeast transaldolase. J. Biol. Chem. 212, 811-825
    • (1955) J. Biol. Chem. , vol.212 , pp. 811-825
    • Horecker, B.L.1    Smyrniotis, P.Z.2
  • 26
    • 0348054921 scopus 로고
    • Pathways of carbohydrate metabolism in microorganisms
    • Gunsalus, I.C., Horecker, B.L. and Wood, W.A. (1955) Pathways of carbohydrate metabolism in microorganisms. Bacteriol. Rev. 19, 79-128
    • (1955) Bacteriol. Rev. , vol.19 , pp. 79-128
    • Gunsalus, I.C.1    Horecker, B.L.2    Wood, W.A.3
  • 27
    • 70449246142 scopus 로고
    • Conversion of nucleoside to sedoheptulose monophosphate by rat liver
    • Sie, H.G., Nigam, V.N. and Fishman, W.H. (1959) Conversion of nucleoside to sedoheptulose monophosphate by rat liver. J. Biol. Chem. 234, 1202-1207
    • (1959) J. Biol. Chem. , vol.234 , pp. 1202-1207
    • Sie, H.G.1    Nigam, V.N.2    Fishman, W.H.3
  • 28
    • 70449294192 scopus 로고
    • The natural occurrence of sedoheptulose monophosphate in liver
    • Nigam, V.N., Sie, H.G. and Fishman, W.H. (1959) The natural occurrence of sedoheptulose monophosphate in liver. J. Biol. Chem. 234, 1955-1957
    • (1959) J. Biol. Chem. , vol.234 , pp. 1955-1957
    • Nigam, V.N.1    Sie, H.G.2    Fishman, W.H.3
  • 30
    • 0014622009 scopus 로고
    • The pentose phosphate pathway of glucose metabolism. Enzyme profiles and transient and steady-state content of intermediates of alternative pathways of glucose metabolism in krebs ascites cells
    • Gumaa, K.A. and McLean, P. (1969) The pentose phosphate pathway of glucose metabolism. Enzyme profiles and transient and steady-state content of intermediates of alternative pathways of glucose metabolism in Krebs ascites cells. Biochem. J. 115, 1009-1029
    • (1969) Biochem. J. , vol.115 , pp. 1009-1029
    • Gumaa, K.A.1    McLean, P.2
  • 31
    • 0014406863 scopus 로고
    • Enzymatic phosphorylation of d-sedoheptulose with animal liver
    • Iwai, H., Kiyomoto, A. and Takeshita, M. (1968) Enzymatic phosphorylation of d-sedoheptulose with animal liver. Biochim. Biophys. Acta 167, 302-307
    • (1968) Biochim. Biophys. Acta , vol.167 , pp. 302-307
    • Iwai, H.1    Kiyomoto, A.2    Takeshita, M.3
  • 32
    • 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
  • 34
    • 0013844498 scopus 로고
    • Phosphate esters of human erythrocytes. Iv. Sedoheptulose-1,7- diphosphate, octulose-1,8-diphosphate, inosine triphosphate and uridine diphosphate
    • Vanderheiden, B.S. (1965) Phosphate esters of human erythrocytes. IV. Sedoheptulose-1,7-diphosphate, octulose-1,8-diphosphate, inosine triphosphate and uridine diphosphate. Biochem. Biophys. Res. Commun. 21, 265-270
    • (1965) Biochem. Biophys. Res. Commun. , vol.21 , pp. 265-270
    • Vanderheiden, B.S.1
  • 35
    • 0018598809 scopus 로고
    • Detection and estimation of sedoheptulose and octulose mono-And bisphosphates in extracts of rat liver
    • Paoletti, F., Williams, J.F. and Horecker, B.L. (1979) Detection and estimation of sedoheptulose and octulose mono-And bisphosphates in extracts of rat liver. Arch. Biochem. Biophys. 198, 620-626
    • (1979) Arch. Biochem. Biophys. , vol.198 , pp. 620-626
    • Paoletti, F.1    Williams, J.F.2    Horecker, B.L.3
  • 36
    • 0020476786 scopus 로고
    • Regulation of hepatic altro heptulose 1,7-bisphosphate levels and control of flux through the pentose pathway by fructose 2,6-bisphosphate
    • Blackmore, P.F. and E.A., S. (1982) Regulation of hepatic altro heptulose 1,7-bisphosphate levels and control of flux through the pentose pathway by fructose 2,6-bisphosphate. FEBS Lett. 142, 255-259
    • (1982) FEBS Lett. , vol.142 , pp. 255-259
    • Blackmore P.F E.A, S.1
  • 37
    • 0028133103 scopus 로고
    • The involvement of fructose 2,6-bisphosphate in substrate cycle control in the nonoxidative stage of the pentose phosphate pathway. A phosphorus magnetic resonance spectroscopy study
    • Belyaeva, N.F., Golubev, M.A., Grigorovich, J.A., Dubinsky, Z.V., Semenova, N.A., Pitkanen, E. and Korovkin, B.F. (1994) The involvement of fructose 2,6-bisphosphate in substrate cycle control in the nonoxidative stage of the pentose phosphate pathway. A phosphorus magnetic resonance spectroscopy study. Experientia 50, 780-784
    • (1994) Experientia , vol.50 , pp. 780-784
    • Belyaeva, N.F.1    Golubev, M.A.2    Grigorovich, J.A.3    Dubinsky, Z.V.4    Semenova, N.A.5    Pitkanen, E.6    Korovkin, B.F.7
  • 38
    • 0347554062 scopus 로고
    • Tetrose phosphate and the formation of sedoheptulose diphosphate
    • Horecker, B.L., Smyrniotis, P.Z., Hiatt, H.H. and Marks, P.A. (1955) Tetrose phosphate and the formation of sedoheptulose diphosphate. J. Biol. Chem. 212, 827-836
    • (1955) J. Biol. Chem. , vol.212 , pp. 827-836
    • Horecker, B.L.1    Smyrniotis, P.Z.2    Hiatt, H.H.3    Marks, P.A.4
  • 39
    • 0015813008 scopus 로고
    • Sedoheptulose-7-phosphate kinase activity of phosphofructokinase from the different tissues of rabbit
    • Karadsheh, N.S., Tejwani, G.A. and Ramaiah, A. (1973) Sedoheptulose-7-phosphate kinase activity of phosphofructokinase from the different tissues of rabbit. Biochim. Biophys. Acta 327, 66-81
    • (1973) Biochim. Biophys. Acta , vol.327 , pp. 66-81
    • Karadsheh, N.S.1    Tejwani, G.A.2    Ramaiah, A.3
  • 41
    • 0018094549 scopus 로고
    • Fructose-1,6-biphosphatase of the small intestine. Purification and comparison with liver and muscle fructose-1,6-bisphosphatases
    • Mizunuma, H. and Tashima, Y. (1978) Fructose-1,6-biphosphatase of the small intestine. Purification and comparison with liver and muscle fructose-1,6-bisphosphatases. J. Biochem. (Tokyo) 84, 327-336
    • (1978) J. Biochem. (Tokyo) , vol.84 , pp. 327-336
    • Mizunuma, H.1    Tashima, Y.2
  • 42
    • 0037227450 scopus 로고    scopus 로고
    • The calvin cycle revisited
    • Raines, C.A. (2003) The Calvin cycle revisited. Photosynth. Res. 75, 1-10
    • (2003) Photosynth. Res. , vol.75 , pp. 1-10
    • Raines, C.A.1
  • 44
    • 80053922625 scopus 로고    scopus 로고
    • Metabolic flux and the regulation of mammalian cell growth
    • Locasale, J.W. and Cantley, L.C. (2011) Metabolic flux and the regulation of mammalian cell growth. Cell Metab. 14, 443-451
    • (2011) Cell Metab. , vol.14 , pp. 443-451
    • Locasale, J.W.1    Cantley, L.C.2
  • 46
    • 84872576236 scopus 로고    scopus 로고
    • Extraordinary metabolism of inflammation limited by pseudo-starvation and amp kinase
    • O'Neill, L.A. and Hardie, D.G. (2013) Extraordinary metabolism of inflammation limited by pseudo-starvation and AMP kinase. Nature 493, 346-355
    • (2013) Nature , vol.493 , pp. 346-355
    • O'Neill, L.A.1    Hardie, D.G.2
  • 47
    • 0011062750 scopus 로고
    • Mechanism of action of transaldolase. I. Crystalization and properties of yeast enzyme
    • Venkataraman, R. and Racker, E. (1961) Mechanism of action of transaldolase. I. Crystalization and properties of yeast enzyme. J. Biol. Chem. 236, 1876-1882
    • (1961) J. Biol. Chem. , vol.236 , pp. 1876-1882
    • Venkataraman, R.1    Racker, E.2
  • 48
    • 0036066728 scopus 로고    scopus 로고
    • Novel pathways for biosynthesis of nucleotide-Activated glycero-manno-heptose precursors of bacterial glycoproteins and cell surface polysaccharides
    • Valvano, M.A., Messner, P. and Kosma, P. (2002) Novel pathways for biosynthesis of nucleotide-Activated glycero-manno-heptose precursors of bacterial glycoproteins and cell surface polysaccharides. Microbiology 148, 1979-1989
    • (2002) Microbiology , vol.148 , pp. 1979-1989
    • Valvano, M.A.1    Messner, P.2    Kosma, P.3
  • 49
    • 33746689858 scopus 로고    scopus 로고
    • Metabolic futile cycles and their functions: A systems analysis of energy and control
    • Qian, H. and Beard, D.A. (2006) Metabolic futile cycles and their functions: a systems analysis of energy and control. Systems Biol. 153, 192-200
    • (2006) Systems Biol. , vol.153 , pp. 192-200
    • Qian, H.1    Beard, D.A.2
  • 50
    • 0022921589 scopus 로고
    • Metabolic effects of d-glyceraldehyde in isolated hepatocytes
    • Maswoswe, S.M., Daneshmand, F. and Davies, D.R. (1986) Metabolic effects of d-glyceraldehyde in isolated hepatocytes. Biochem. J. 240, 771-776
    • (1986) Biochem. J. , vol.240 , pp. 771-776
    • Maswoswe, S.M.1    Daneshmand, F.2    Davies, D.R.3


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