메뉴 건너뛰기




Volumn 415, Issue 1, 2008, Pages 123-134

Transaldolase deficiency influences the pentose phosphate pathway, mitochondrial homoeostasis and apoptosis signal processing

Author keywords

Apoptosis; Ca2+; Mitochondrion; Pentose phosphate pathway; Transaldolase

Indexed keywords

CELL DEATH; MAMMALS;

EID: 53149119202     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20080722     Document Type: Article
Times cited : (43)

References (49)
  • 1
    • 0001921711 scopus 로고
    • The pentose phosphate pathway and other pathways of hexose metabolism
    • Murray, R. K, Granner, D. K, Mayes, R A. and Rodwell, V. W, eds, pp, Appleton and Lange, Norwalk, CT
    • Mayes, P. A. (1993) The pentose phosphate pathway and other pathways of hexose metabolism. Harper's Biochemistry (Murray, R. K., Granner, D. K., Mayes, R A. and Rodwell, V. W., eds), pp. 201-211, Appleton and Lange, Norwalk, CT
    • (1993) Harper's Biochemistry , pp. 201-211
    • Mayes, P.A.1
  • 4
    • 0020483024 scopus 로고
    • A pathway for the interconversion of hexose and pentose in the parasitic amoeba Enfamoeba histolytica
    • Susskind, B. M., Warren, L. G. and Reeves, R. E. (1982) A pathway for the interconversion of hexose and pentose in the parasitic amoeba Enfamoeba histolytica. Biochem. J. 204, 191-199
    • (1982) Biochem. J , vol.204 , pp. 191-199
    • Susskind, B.M.1    Warren, L.G.2    Reeves, R.E.3
  • 5
    • 0026451207 scopus 로고
    • Pentose metabolism in Zymomonas mobilis wild-type and recombinant strains
    • Feldmann, S. D., Sahm, H. and Sprenger, G. A. (1992) Pentose metabolism in Zymomonas mobilis wild-type and recombinant strains. Appl. Microbiol. Biotechnol, 38, 354-361
    • (1992) Appl. Microbiol. Biotechnol , vol.38 , pp. 354-361
    • Feldmann, S.D.1    Sahm, H.2    Sprenger, G.A.3
  • 6
    • 1842530284 scopus 로고    scopus 로고
    • ZNF143 mediates basal and tissue-specific expression of human transaldolase
    • Grossman, C. E., Qian, Y., Banki, K. and Perl, A. (2004) ZNF143 mediates basal and tissue-specific expression of human transaldolase. J. Biol. Chem. 279, 12190-12205
    • (2004) J. Biol. Chem , vol.279 , pp. 12190-12205
    • Grossman, C.E.1    Qian, Y.2    Banki, K.3    Perl, A.4
  • 8
    • 34347396343 scopus 로고    scopus 로고
    • The pathogenesis of transaldolase deficiency
    • Perl, A. (2007) The pathogenesis of transaldolase deficiency. IUBMB Life 59, 365-373
    • (2007) IUBMB Life , vol.59 , pp. 365-373
    • Perl, A.1
  • 13
    • 0036314214 scopus 로고    scopus 로고
    • Primary biliary cirrhosis and other ductopenic diseases
    • Burt, A. D. (2002) Primary biliary cirrhosis and other ductopenic diseases. Clin. Liver Dis. 6, 363-380
    • (2002) Clin. Liver Dis , vol.6 , pp. 363-380
    • Burt, A.D.1
  • 14
    • 12644275745 scopus 로고    scopus 로고
    • Glutathione levels and sensitivity to apoptosis are regulated by changes in transaldolase expression
    • Banki, K., Hutter, E., Colombo, E., Gonchoroff, N. J. and Perl, A. (1996) Glutathione levels and sensitivity to apoptosis are regulated by changes in transaldolase expression. J. Biol. Chem. 271, 32994-33001
    • (1996) J. Biol. Chem , vol.271 , pp. 32994-33001
    • Banki, K.1    Hutter, E.2    Colombo, E.3    Gonchoroff, N.J.4    Perl, A.5
  • 15
    • 0033083310 scopus 로고    scopus 로고
    • Banki, K.. Hutter, E., Gonchoroff. N, and Perl, A. (1999) Elevation of mitochondrial transmembrane potential and reactive oxygen intermediate levels are early events and occur independently from activation of caspases in Fas signaling. J. Immunol. 162, 1466-1479
    • Banki, K.. Hutter, E., Gonchoroff. N, and Perl, A. (1999) Elevation of mitochondrial transmembrane potential and reactive oxygen intermediate levels are early events and occur independently from activation of caspases in Fas signaling. J. Immunol. 162, 1466-1479
  • 16
    • 0025239794 scopus 로고
    • Oxidative metabolism in the alveolar macrophage: Analysis by flow cytometry
    • Kobzik, L., Godleski, J. J. and Brain, J. D. (1990) Oxidative metabolism in the alveolar macrophage: analysis by flow cytometry. J. Leukocyte Biol. 47, 295-303
    • (1990) J. Leukocyte Biol , vol.47 , pp. 295-303
    • Kobzik, L.1    Godleski, J.J.2    Brain, J.D.3
  • 17
    • 0242663915 scopus 로고    scopus 로고
    • 2+ - and redox-dependent production of nitric oxide
    • 2+ - and redox-dependent production of nitric oxide. J. Immunol. 171, 5188-5197
    • (2003) J. Immunol , vol.171 , pp. 5188-5197
    • Nagy, G.1    Koncz, A.2    Perl, A.3
  • 18
    • 0029143569 scopus 로고    scopus 로고
    • Hajnoczky. G.. Robb-Gaspers, L. D., Seitz, M. B. and Thomas, A. R (11995) Decoding of cytosolic calcium oscillations in the mitochondria. Cell 82, 415-424
    • Hajnoczky. G.. Robb-Gaspers, L. D., Seitz, M. B. and Thomas, A. R (11995) Decoding of cytosolic calcium oscillations in the mitochondria. Cell 82, 415-424
  • 19
    • 0028030737 scopus 로고
    • Cloning and expression of the human gene for transaldolase: A novel highly repetitive element constitutes an integral part of the coding sequence
    • Banki. K., Halladay D. and PerL. A. (1994) Cloning and expression of the human gene for transaldolase: a novel highly repetitive element constitutes an integral part of the coding sequence. J, Biol. Chem. 269, 2847-2851
    • (1994) J, Biol. Chem , vol.269 , pp. 2847-2851
    • Banki, K.1    Halladay, D.2    PerL, A.3
  • 20
    • 0019740344 scopus 로고
    • Glutathione peroxidase
    • Wendel, A. (1981) Glutathione peroxidase. Methods Enzymol. 77, 325-333
    • (1981) Methods Enzymol , vol.77 , pp. 325-333
    • Wendel, A.1
  • 21
    • 0035877177 scopus 로고    scopus 로고
    • Relationship between posttranslational modification of transaldolase and catalase deficiency in UV-sensitive repair-deficient Xeroderma pigmentosum fibroblasts and SV40-transformed human cells
    • Lachaise. F, Martin, G., Drougard, C., Perl, A., Vuillaume, M., Wegnez, M., Sarasin, A. and Daya-Grosjean, L. (2001) Relationship between posttranslational modification of transaldolase and catalase deficiency in UV-sensitive repair-deficient Xeroderma pigmentosum fibroblasts and SV40-transformed human cells. Free Radical Biol. Med. 30. 1365-1373
    • (2001) Free Radical Biol. Med , vol.30 , pp. 1365-1373
    • Lachaise, F.1    Martin, G.2    Drougard, C.3    Perl, A.4    Vuillaume, M.5    Wegnez, M.6    Sarasin, A.7    Daya-Grosjean, L.8
  • 22
    • 0025354323 scopus 로고
    • Alteration of endogenous glutathione peroxidase, manganese superoxide dismutase and glutathione transferase activity in cells transfected with a copper-zinc superoxide dismutase expression vector. Explanation for variations in paraquat resistance
    • Kelner, M. J. and Bagnell, R. (1990) Alteration of endogenous glutathione peroxidase, manganese superoxide dismutase and glutathione transferase activity in cells transfected with a copper-zinc superoxide dismutase expression vector. Explanation for variations in paraquat resistance. J. Biol. Chem. 265, 10872-10875
    • (1990) J. Biol. Chem , vol.265 , pp. 10872-10875
    • Kelner, M.J.1    Bagnell, R.2
  • 24
    • 0025006627 scopus 로고
    • High-performance anion-exchange chromatography for carbohydrate analysis
    • Lee, Y. C. (1990) High-performance anion-exchange chromatography for carbohydrate analysis. Anal.Biochem. 189, 151-162
    • (1990) Anal.Biochem , vol.189 , pp. 151-162
    • Lee, Y.C.1
  • 25
    • 0027423360 scopus 로고
    • HPLC determination of oxidized and reduced pyridine coenzymes in human erythrocytes
    • Micheli, V, Simmonds, H. A., Bari, M. and Pompucci, G. (1993) HPLC determination of oxidized and reduced pyridine coenzymes in human erythrocytes. Clin. Chim. Acta 220, 1-17
    • (1993) Clin. Chim. Acta , vol.220 , pp. 1-17
    • Micheli, V.1    Simmonds, H.A.2    Bari, M.3    Pompucci, G.4
  • 27
    • 0031739195 scopus 로고    scopus 로고
    • Nichols, T. C., Guthridge, J, M., Karp. D. R., Molina, H., Fletcher, D. R. and Holers, V. M. (1998) γ-Glutamyl transpeptidase, an ecto-enzyme regulator of intracellular redox potential, is a component of TM4 signal transduction complexes. Eur. J. Immunol. 28, 4123-4129
    • Nichols, T. C., Guthridge, J, M., Karp. D. R., Molina, H., Fletcher, D. R. and Holers, V. M. (1998) γ-Glutamyl transpeptidase, an ecto-enzyme regulator of intracellular redox potential, is a component of TM4 signal transduction complexes. Eur. J. Immunol. 28, 4123-4129
  • 28
    • 0026720075 scopus 로고    scopus 로고
    • Gossen, M. and Bujard, H. (1992) Tight control of gene expression in mammalian cells by tetracyclin-responsive promoters. Proc. Nall. Acad. Sci. U.S.A. 89, 5547-5551
    • Gossen, M. and Bujard, H. (1992) Tight control of gene expression in mammalian cells by tetracyclin-responsive promoters. Proc. Nall. Acad. Sci. U.S.A. 89, 5547-5551
  • 29
    • 0029863399 scopus 로고    scopus 로고
    • Modulation of the mitochondrial permeability transition pore by pyridine nucleolides and dithiol oxidation at two separate sites
    • Constantini, P., Chernyak, B. V., Petronilli, V and Bernardi, P. (1996) Modulation of the mitochondrial permeability transition pore by pyridine nucleolides and dithiol oxidation at two separate sites. J. Biol. Chem. 271, 6746-6751
    • (1996) J. Biol. Chem , vol.271 , pp. 6746-6751
    • Constantini, P.1    Chernyak, B.V.2    Petronilli, V.3    Bernardi, P.4
  • 30
    • 0032496222 scopus 로고    scopus 로고
    • Molecular ordering in HIV-induced apoptosis: Oxidative stress, activation of caspases and cell survival are regulated by transaldolase
    • Banki. K., Hutter, E., Gonchoroff, N. J. and Perl, A. (1998) Molecular ordering in HIV-induced apoptosis: oxidative stress, activation of caspases and cell survival are regulated by transaldolase. J. Biol. Chem. 273, 11944-11953
    • (1998) J. Biol. Chem , vol.273 , pp. 11944-11953
    • Banki, K.1    Hutter, E.2    Gonchoroff, N.J.3    Perl, A.4
  • 31
    • 0037686243 scopus 로고    scopus 로고
    • Megamitochondria formation - physiology and pathology
    • Wakabayashi, T. (2002) Megamitochondria formation - physiology and pathology. J. Cell. Mol. Med. 6, 497-538
    • (2002) J. Cell. Mol. Med , vol.6 , pp. 497-538
    • Wakabayashi, T.1
  • 32
    • 33746841367 scopus 로고    scopus 로고
    • Nitric oxide and mitochondrial biogenesis
    • Nisoli, E. and Carruba, M. O. (2006) Nitric oxide and mitochondrial biogenesis. J. Cell Sci. 119, 2855-2862
    • (2006) J. Cell Sci , vol.119 , pp. 2855-2862
    • Nisoli, E.1    Carruba, M.O.2
  • 33
    • 0025126555 scopus 로고
    • Role of free radicals and catalytic metal ions in human disease: An overview
    • Halliwell, B. and Gutteridge, J. M. (1990) Role of free radicals and catalytic metal ions in human disease: an overview. Methods Enzymol. 186, 1-85
    • (1990) Methods Enzymol , vol.186 , pp. 1-85
    • Halliwell, B.1    Gutteridge, J.M.2
  • 34
    • 0033924228 scopus 로고    scopus 로고
    • Stimulation of the pentose phosphate pathway and glutathione levels by dehydroascorbate, the oxidized form of vitamin C
    • Puskas, F, Gergely, R, Banki, K. and Perl, A. (2000) Stimulation of the pentose phosphate pathway and glutathione levels by dehydroascorbate, the oxidized form of vitamin C. FASEB J. 14, 1352-1361
    • (2000) FASEB J , vol.14 , pp. 1352-1361
    • Puskas, F.1    Gergely, R.2    Banki, K.3    Perl, A.4
  • 36
    • 0141996463 scopus 로고    scopus 로고
    • Mizuno, T.. Zhong. X. and Rothstein, T L. (2003) Fas-induced apoplosis in B cells. Apoptosis 8, 451-460
    • Mizuno, T.. Zhong. X. and Rothstein, T L. (2003) Fas-induced apoplosis in B cells. Apoptosis 8, 451-460
  • 37
    • 0032030699 scopus 로고    scopus 로고
    • Apoptosis of malignant human B cells by ligation of CD20 with monoclonal antibodies
    • Shan, D., Ledbetter. J. A. and Press, O. W. (1998) Apoptosis of malignant human B cells by ligation of CD20 with monoclonal antibodies. Blood 91, 1644-1652
    • (1998) Blood , vol.91 , pp. 1644-1652
    • Shan, D.1    Ledbetter, J.A.2    Press, O.W.3
  • 38
    • 0032999223 scopus 로고    scopus 로고
    • CD95-mediated murine hepatic apoptosis requires an intact glutathione status
    • Hentze, H., Kunstle, G., Volbracht, C., Ertel, W. and Wendel, A. (1999) CD95-mediated murine hepatic apoptosis requires an intact glutathione status. Hepatology 30, 177-185
    • (1999) Hepatology , vol.30 , pp. 177-185
    • Hentze, H.1    Kunstle, G.2    Volbracht, C.3    Ertel, W.4    Wendel, A.5
  • 39
    • 0030589731 scopus 로고    scopus 로고
    • (11996) Kinetic and chemical mechanisms of the sheep liver 6-phosphogluconate dehydrogenase
    • Price, N. E. and Cook, P. F (11996) Kinetic and chemical mechanisms of the sheep liver 6-phosphogluconate dehydrogenase. Arch. Biochem. Biophys. 336, 215-223
    • Arch. Biochem. Biophys , vol.336 , pp. 215-223
    • Price, N.E.1    Cook, P.F.2
  • 40
    • 0034024290 scopus 로고    scopus 로고
    • Cyclic ADP-ribose
    • Guse, A. H. (2000) Cyclic ADP-ribose. J. Mol. Med. 78, 26-35
    • (2000) J. Mol. Med , vol.78 , pp. 26-35
    • Guse, A.H.1
  • 41
    • 0034023238 scopus 로고    scopus 로고
    • New functions of a long-known molecule. Emerging roles of NAD in cellular signaling
    • Ziegler, M. (2000) New functions of a long-known molecule. Emerging roles of NAD in cellular signaling. Eur.J. Biochem. 267, 1550-1564
    • (2000) Eur.J. Biochem , vol.267 , pp. 1550-1564
    • Ziegler, M.1
  • 42
    • 0035142953 scopus 로고    scopus 로고
    • Release of calcium from mitochondrial and nonmitochondrial intracellular stores in mouse pancreatic acinar cells by hydrogen peroxide
    • Pariente, J. A., Camello, C., Camello, P. J. and Salido, G. M. (2001) Release of calcium from mitochondrial and nonmitochondrial intracellular stores in mouse pancreatic acinar cells by hydrogen peroxide. J. Membr. Biol. 179, 27-35
    • (2001) J. Membr. Biol , vol.179 , pp. 27-35
    • Pariente, J.A.1    Camello, C.2    Camello, P.J.3    Salido, G.M.4
  • 43
    • 0025060741 scopus 로고
    • Regulation and rate of the hexose monophosphate shunt in Rana ridibunda erythrocytes
    • Kaloyianni, M. and Kalomenopoulou, M. (1990) Regulation and rate of the hexose monophosphate shunt in Rana ridibunda erythrocytes. Comp. Biochem. Physiol. B Comp. Biochem. 95, 287-294
    • (1990) Comp. Biochem. Physiol. B Comp. Biochem , vol.95 , pp. 287-294
    • Kaloyianni, M.1    Kalomenopoulou, M.2
  • 45
    • 28944442995 scopus 로고    scopus 로고
    • Altered CD38 expression in thioacetamide-induced rat model of liver cirrhosis
    • Gan, B. H., Ng, G. L., Bay, B. H. and Chang, C. F. (2005) Altered CD38 expression in thioacetamide-induced rat model of liver cirrhosis. Liver Int. 25, 1233-1242
    • (2005) Liver Int , vol.25 , pp. 1233-1242
    • Gan, B.H.1    Ng, G.L.2    Bay, B.H.3    Chang, C.F.4
  • 46
    • 0037972522 scopus 로고    scopus 로고
    • Mitochondrial respiratory-chain diseases
    • DiMauro, S. and Schon, E. A. (2003) Mitochondrial respiratory-chain diseases. New Engl. J. Med. 348, 2656-2668
    • (2003) New Engl. J. Med , vol.348 , pp. 2656-2668
    • DiMauro, S.1    Schon, E.A.2
  • 47
    • 0014964296 scopus 로고
    • The redox state of the mitochondrial NAD system in cirrhosis of the liver and in chronic quantitative undernutrition in the rat
    • Henley, K. S. and Laughrey, E. G. (1970) The redox state of the mitochondrial NAD system in cirrhosis of the liver and in chronic quantitative undernutrition in the rat. Biochim. Biophys. Acta 201, 9-12
    • (1970) Biochim. Biophys. Acta , vol.201 , pp. 9-12
    • Henley, K.S.1    Laughrey, E.G.2
  • 49
    • 38049123914 scopus 로고    scopus 로고
    • CD95 signaling deficient mice with a wild-type hematopoietic system are prone to hepatic neoplasia
    • Park, S. M., Rajapaksha, T., Zhang, M., Sattar, H., Fichera, A., Ashton-Rickardt, P. and Peter, M. (2008) CD95 signaling deficient mice with a wild-type hematopoietic system are prone to hepatic neoplasia. Apoptosis 13, 41-51
    • (2008) Apoptosis , vol.13 , pp. 41-51
    • Park, S.M.1    Rajapaksha, T.2    Zhang, M.3    Sattar, H.4    Fichera, A.5    Ashton-Rickardt, P.6    Peter, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.