메뉴 건너뛰기




Volumn 95, Issue 1, 2005, Pages 45-52

New nuclear functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells

Author keywords

Cancer chemotherapy; GAPDH; Glyceraldehyde 3 phosphate dehydrogenase; Membrane fusion; Metabolic syndrome; Post translational modification; Telomere structure; Transcriptional regulation

Indexed keywords

DNA; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GLYCOLYTIC ENZYME; NUCLEOTIDE; HISTONE; NUCLEAR PROTEIN;

EID: 23844452781     PISSN: 07302312     EISSN: None     Source Type: Journal    
DOI: 10.1002/jcb.20399     Document Type: Article
Times cited : (273)

References (57)
  • 1
    • 1542723181 scopus 로고    scopus 로고
    • Preventing cardiovascular events in patients with diabetes mellitus
    • Abraham WT. 2004. Preventing cardiovascular events in patients with diabetes mellitus. Am J Med 116(Suppl 5A):39S-46S.
    • (2004) Am J Med , vol.116 , Issue.SUPPL. 5A
    • Abraham, W.T.1
  • 4
    • 0035844082 scopus 로고    scopus 로고
    • Pot1, the putative telomere end-binding protein in fission yeast and humans
    • Baumann P, Cech TR. 2001. Pot1, the putative telomere end-binding protein in fission yeast and humans. Science 292:1171-1175.
    • (2001) Science , vol.292 , pp. 1171-1175
    • Baumann, P.1    Cech, T.R.2
  • 5
    • 84984775429 scopus 로고    scopus 로고
    • Human telomeres contain two distinct Myb-related proteins, TRF1 and TRF2
    • Broccoli D, Smogorzewska A, Chong L, de Lange T. 1997. Human telomeres contain two distinct Myb-related proteins, TRF1 and TRF2. Nat Genet 17:231-235.
    • (1997) Nat Genet , vol.17 , pp. 231-235
    • Broccoli, D.1    Smogorzewska, A.2    Chong, L.3    De Lange, T.4
  • 7
    • 0032878326 scopus 로고    scopus 로고
    • Micro- And macro-vascular reactivity is impaired in subjects at risk for type 2 diabetes
    • Caballero AE, Arora S, Saouaf R, et al. 1999. Micro- and macro-vascular reactivity is impaired in subjects at risk for type 2 diabetes. Diabetes 48:1863-1867.
    • (1999) Diabetes , vol.48 , pp. 1863-1867
    • Caballero, A.E.1    Arora, S.2    Saouaf, R.3
  • 8
    • 0032211790 scopus 로고    scopus 로고
    • Demonstration of a RNA-dependent nuclear interaction between the promyelocytic protein and glyceraldehyde-3-phosphate dehydrogenase
    • Carlile GW, Tatton WG, Borden KLB. 1998. Demonstration of a RNA-dependent nuclear interaction between the promyelocytic protein and glyceraldehyde-3- phosphate dehydrogenase. Biochem J 335:691-696.
    • (1998) Biochem J , vol.335 , pp. 691-696
    • Carlile, G.W.1    Tatton, W.G.2    Borden, K.L.B.3
  • 9
    • 0041704526 scopus 로고    scopus 로고
    • Telomere maintenance and DNA replication: How close are they connected?
    • Chakhparonian M, Wellinger RJ. 2003. Telomere maintenance and DNA replication: How close are they connected? Trends Genet 19:439-446.
    • (2003) Trends Genet , vol.19 , pp. 439-446
    • Chakhparonian, M.1    Wellinger, R.J.2
  • 10
    • 0036091876 scopus 로고    scopus 로고
    • Proliferative and nutritional dependent regulation of glyceraldehyde-3-phosphate dehydrogenase expression in the rat liver
    • Corbin Gong Y, Zhang M, Minuk GY. 2002. Proliferative and nutritional dependent regulation of glyceraldehyde-3-phosphate dehydrogenase expression in the rat liver. Cell Prolif 38:173-182.
    • (2002) Cell Prolif , vol.38 , pp. 173-182
    • Corbin Gong, Y.1    Zhang, M.2    Minuk, G.Y.3
  • 13
    • 0034710891 scopus 로고    scopus 로고
    • Hyperglycemia-induced mitochondrial superoxide overproduction activates the hexosamine pathway and induces plasminogen activator inhibitor-1 expression by increasing Sp1 glycosylation
    • Du X, Edelstein D, Rossetti L, Fantus IG, Goldberg H, Ziyadeh F, Wu J, Brownlee M. 2000. Hyperglycemia-induced mitochondrial superoxide overproduction activates the hexosamine pathway and induces plasminogen activator inhibitor-1 expression by increasing Sp1 glycosylation. Proc Natl Acad Sci 97:12222-12226.
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 12222-12226
    • Du, X.1    Edelstein, D.2    Rossetti, L.3    Fantus, I.G.4    Goldberg, H.5    Ziyadeh, F.6    Wu, J.7    Brownlee, M.8
  • 14
    • 85047691537 scopus 로고    scopus 로고
    • Inhibition of GAPDH activity by poly(ADP-ribose) polymerase activates three major pathways of hyperglycemic damage in endothelial cells
    • Du X, Matsumura T, Edelstein D, Rossetti L, Zsengeller Z, Szabo C, Brownlee M. 2003. Inhibition of GAPDH activity by poly(ADP-ribose) polymerase activates three major pathways of hyperglycemic damage in endothelial cells. J Clin Invest 112:1049-1057.
    • (2003) J Clin Invest , vol.112 , pp. 1049-1057
    • Du, X.1    Matsumura, T.2    Edelstein, D.3    Rossetti, L.4    Zsengeller, Z.5    Szabo, C.6    Brownlee, M.7
  • 16
    • 0023875830 scopus 로고
    • Purification and characterization of OTF-1, a transcription factor regulating cell cycle expression of a human histone H2b gene
    • Fletcher C, Heintz N, Roeder RG. 1987. Purification and characterization of OTF-1, a transcription factor regulating cell cycle expression of a human histone H2b gene. Cell 51:773-781.
    • (1987) Cell , vol.51 , pp. 773-781
    • Fletcher, C.1    Heintz, N.2    Roeder, R.G.3
  • 17
    • 0030009314 scopus 로고    scopus 로고
    • BCL-2 expression or antioxidants prevent hyperglycemia-induced formation of intracellular advanced glycation endproducts in bovine endothelial cells
    • Giardino I, Edelstein D, Brownlee M. 1996. BCL-2 expression or antioxidants prevent hyperglycemia-induced formation of intracellular advanced glycation endproducts in bovine endothelial cells. J Clin Invest 97:1422-1428.
    • (1996) J Clin Invest , vol.97 , pp. 1422-1428
    • Giardino, I.1    Edelstein, D.2    Brownlee, M.3
  • 18
    • 0029123674 scopus 로고
    • Rapid plasmenylethanolamine-selective fusion of membrane bilayers catalyzed by an isoform of glyceraldehyde-3 phosphate dehydrogenase: Discrimination between glycolytic and fusogenic roles of individual isoforms
    • Glaser PE, Gross RW. 1995. Rapid plasmenylethanolamine-selective fusion of membrane bilayers catalyzed by an isoform of glyceraldehyde-3 phosphate dehydrogenase: Discrimination between glycolytic and fusogenic roles of individual isoforms. Biochemistry 34:12194-12203.
    • (1995) Biochemistry , vol.34 , pp. 12194-12203
    • Glaser, P.E.1    Gross, R.W.2
  • 19
    • 0037195125 scopus 로고    scopus 로고
    • Tubulin is the endogenous inhibitor of the glyceraldehyde-3-phosphate dehydrogenase isoform that catalyzes membrane fusion: Implications for the coordinated regulation of glycolysis and membrane fusion
    • Glaser PE, Han X, Gross RW. 2002. Tubulin is the endogenous inhibitor of the glyceraldehyde-3-phosphate dehydrogenase isoform that catalyzes membrane fusion: Implications for the coordinated regulation of glycolysis and membrane fusion. Proc Natl Acad Sci USA 99: 14104-14108.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14104-14108
    • Glaser, P.E.1    Han, X.2    Gross, R.W.3
  • 20
    • 0032741858 scopus 로고    scopus 로고
    • Identification of an oxygen responsive enhancer element in the glyceraldehyde-3-phosphate gene
    • Graven KK, Yu Q, Pan D, Roncarati JS, Farber HW. 1999. Identification of an oxygen responsive enhancer element in the glyceraldehyde-3-phosphate gene. Biochim Biophys Acta 1447:208-218.
    • (1999) Biochim Biophys Acta , vol.1447 , pp. 208-218
    • Graven, K.K.1    Yu, Q.2    Pan, D.3    Roncarati, J.S.4    Farber, H.W.5
  • 22
    • 0036787485 scopus 로고    scopus 로고
    • Components of the "metabolic syndrome" and incidence of type 2 diabetes
    • Hanson RL, Imperatore G, Bennett PH, Knowler WC. 2002. Components of the "metabolic syndrome" and incidence of type 2 diabetes. Diabetes 51:3120-3127.
    • (2002) Diabetes , vol.51 , pp. 3120-3127
    • Hanson, R.L.1    Imperatore, G.2    Bennett, P.H.3    Knowler, W.C.4
  • 23
    • 0029838525 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase antisense oligodeoxynucleotides protect against cytosine arabinonucleoside-induced apoptosis in cultured cerebellar neurons
    • Ishitani R, Chuang D-M. 1996. Glyceraldehyde-3-phosphate dehydrogenase antisense oligodeoxynucleotides protect against cytosine arabinonucleoside- induced apoptosis in cultured cerebellar neurons. Proc Natl Acad Sci USA 93:9937-9941.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 9937-9941
    • Ishitani, R.1    Chuang, D.-M.2
  • 24
    • 0031474883 scopus 로고    scopus 로고
    • Localization of the phosphatidylserine-binding site of glyceraldehyde-3-phosphate dehydrogenase responsible for membrane fusion
    • Kaneda M, Takeuchi K, Inoue K, Umeda M. 1997. Localization of the phosphatidylserine-binding site of glyceraldehyde-3-phosphate dehydrogenase responsible for membrane fusion. J Biochem 122:1233-1240.
    • (1997) J Biochem , vol.122 , pp. 1233-1240
    • Kaneda, M.1    Takeuchi, K.2    Inoue, K.3    Umeda, M.4
  • 25
    • 0022477471 scopus 로고
    • Autophosphorylation of glyceraldehydephosphate dehydrogenase and phosphorylation of protein from skeletal muscle microsomes
    • Kawamoto RM, Caswell AH. 1986. Autophosphorylation of glyceraldehydephosphate dehydrogenase and phosphorylation of protein from skeletal muscle microsomes. Biochemistry 25:656-661.
    • (1986) Biochemistry , vol.25 , pp. 656-661
    • Kawamoto, R.M.1    Caswell, A.H.2
  • 26
    • 0842324785 scopus 로고    scopus 로고
    • The nucleosome: From genomic organization to genomic regulation
    • Khorasanizadeh S. 2004. The nucleosome: From genomic organization to genomic regulation. Cell 116:259-272.
    • (2004) Cell , vol.116 , pp. 259-272
    • Khorasanizadeh, S.1
  • 27
    • 18144453930 scopus 로고    scopus 로고
    • Inhibition of glyceraldehyde-3-phosphate dehydrogenase in post-ischaemic myocardium
    • Knight RJ, Kofoed KF, Schelbert HR, Buxton DB. 1996. Inhibition of glyceraldehyde-3-phosphate dehydrogenase in post-ischaemic myocardium. Cardiovas Res 32:1016-1023.
    • (1996) Cardiovas Res , vol.32 , pp. 1016-1023
    • Knight, R.J.1    Kofoed, K.F.2    Schelbert, H.R.3    Buxton, D.B.4
  • 29
    • 0037228781 scopus 로고    scopus 로고
    • A nuclear protein complex containing high mobility group proteins B1 and B2, heat shock cognate protein 70, ERp60, and glyceraldehyde-3-phosphate dehydrogenase is involved in the cytotoxic response to DNA modified by incorporation of anticancer nucleoside analogues
    • Krynetski EY, Krynetskaia NF, Bianchi ME, Evans WE. 2003. A nuclear protein complex containing high mobility group proteins B1 and B2, heat shock cognate protein 70, ERp60, and glyceraldehyde-3-phosphate dehydrogenase is involved in the cytotoxic response to DNA modified by incorporation of anticancer nucleoside analogues. Cancer Res 63:100-106.
    • (2003) Cancer Res , vol.63 , pp. 100-106
    • Krynetski, E.Y.1    Krynetskaia, N.F.2    Bianchi, M.E.3    Evans, W.E.4
  • 30
    • 0034716904 scopus 로고    scopus 로고
    • Identification of human Rap1: Implications for telomere evolution
    • Li B, Oestriech S, de Lange T. 2000. Identification of human Rap1: Implications for telomere evolution. Cell 101:471-483.
    • (2000) Cell , vol.101 , pp. 471-483
    • Li, B.1    Oestriech, S.2    De Lange, T.3
  • 31
    • 0037133736 scopus 로고    scopus 로고
    • Identification of an additional hypoxia responsive element in the glyceraldehyde-3-phosphate dehydrogenase gene promoter
    • Lu S, Gu X, Hoestje S, Epner DE. 2002. Identification of an additional hypoxia responsive element in the glyceraldehyde-3-phosphate dehydrogenase gene promoter. Biochim Biophys Acta 1574:152-156.
    • (2002) Biochim Biophys Acta , vol.1574 , pp. 152-156
    • Lu, S.1    Gu, X.2    Hoestje, S.3    Epner, D.E.4
  • 32
    • 0029041509 scopus 로고
    • Cloning, functional characterization, and mechanism of action of the B-cell-specific transcriptional coactivator OCA-B
    • Luo Y, Roeder RG. 1995. Cloning, functional characterization, and mechanism of action of the B-cell-specific transcriptional coactivator OCA-B. Mol Cell Biol 15: 4115-4124.
    • (1995) Mol Cell Biol , vol.15 , pp. 4115-4124
    • Luo, Y.1    Roeder, R.G.2
  • 33
    • 0042698617 scopus 로고    scopus 로고
    • Gene switching by metabolic enzymes- How did you get on the invitation list?
    • McKnight S. 2003. Gene switching by metabolic enzymes- How did you get on the invitation list? Cell 114: 150-152.
    • (2003) Cell , vol.114 , pp. 150-152
    • McKnight, S.1
  • 34
  • 36
    • 0002584292 scopus 로고
    • Relationship between metabolic control and long term complications of diabetes
    • Kahn CR, Weir G, editors. Philadelphia, PA: Lea and Febiger
    • Nathan D. 1994. Relationship between metabolic control and long term complications of diabetes. In: Kahn CR, Weir G, editors. Joslin's diabetes. Philadelphia, PA: Lea and Febiger; 620-631.
    • (1994) Joslin's Diabetes , pp. 620-631
    • Nathan, D.1
  • 40
    • 0029037649 scopus 로고
    • Pathophysiology of insulin resistance in human disease
    • Reaven GM. 1995. Pathophysiology of insulin resistance in human disease. Physiol Rev 75:473-486.
    • (1995) Physiol Rev , vol.75 , pp. 473-486
    • Reaven, G.M.1
  • 41
    • 0022834087 scopus 로고
    • Five enzymes of the glycolytic pathway serve as substrates for purified epidermal-growth-factor-receptor kinase
    • Reiss N, Kanety H, Schlessinger J. 1986. Five enzymes of the glycolytic pathway serve as substrates for purified epidermal-growth-factor-receptor kinase. Biochem J 239: 691-697.
    • (1986) Biochem J , vol.239 , pp. 691-697
    • Reiss, N.1    Kanety, H.2    Schlessinger, J.3
  • 42
    • 0242380324 scopus 로고    scopus 로고
    • Diabetes, microvascular complications, and cardiovascular complications: What is it about glucose?
    • Reusch JEB. 2003. Diabetes, microvascular complications, and cardiovascular complications: What is it about glucose? J Clin Invest 112:986-988.
    • (2003) J Clin Invest , vol.112 , pp. 986-988
    • Reusch, J.E.B.1
  • 43
    • 0029095105 scopus 로고
    • A mutation in glyceraldehyde-3-phosphate dehydrogenase alters endocytosis in CHO cells
    • Robbins AR, Ward RD, Oliver C. 1995. A mutation in glyceraldehyde-3- phosphate dehydrogenase alters endocytosis in CHO cells. J Cell Biol 130:1093-1104.
    • (1995) J Cell Biol , vol.130 , pp. 1093-1104
    • Robbins, A.R.1    Ward, R.D.2    Oliver, C.3
  • 44
    • 0032972037 scopus 로고    scopus 로고
    • Nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase isoforms during neuronal apoptosis
    • Saunders PA, Chen R-W, Chuang D-M. 1999. Nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase isoforms during neuronal apoptosis. J Neurochem 72:925-932.
    • (1999) J Neurochem , vol.72 , pp. 925-932
    • Saunders, P.A.1    Chen, R.-W.2    Chuang, D.-M.3
  • 45
    • 2542619763 scopus 로고    scopus 로고
    • Obesity and cardiovascular risk: The new public health problem of worldwide proportions
    • Scaglione R, Argano C, Di Chiara T, Licata G. 2004. Obesity and cardiovascular risk: The new public health problem of worldwide proportions. Exp Rev Cardiovas Ther 2:203-212.
    • (2004) Exp Rev Cardiovas Ther , vol.2 , pp. 203-212
    • Scaglione, R.1    Argano, C.2    Di Chiara, T.3    Licata, G.4
  • 46
    • 0034957426 scopus 로고    scopus 로고
    • Reversible nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase upon serum stimulation
    • Schmitz H-D. 2001. Reversible nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase upon serum stimulation. Eur J Cell Biol 80:419-427.
    • (2001) Eur J Cell Biol , vol.80 , pp. 419-427
    • Schmitz, H.-D.1
  • 47
    • 0032032578 scopus 로고    scopus 로고
    • Overexpression of glyoxalase-I in bovine endothelial cells inhibits intracellular advanced glycation endproduct formation and prevents hyperglycemia-induced increases in macromolecular endocytosis
    • Shinohara M, Thornalley PJ, Giardino I, Beisswenger P, Thorpe SR, Onorato J, Brownlee M. 1998. Overexpression of glyoxalase-I in bovine endothelial cells inhibits intracellular advanced glycation endproduct formation and prevents hyperglycemia-induced increases in macromolecular endocytosis. J Clin Invest 101:1142-1147.
    • (1998) J Clin Invest , vol.101 , pp. 1142-1147
    • Shinohara, M.1    Thornalley, P.J.2    Giardino, I.3    Beisswenger, P.4    Thorpe, S.R.5    Onorato, J.6    Brownlee, M.7
  • 48
    • 0032973950 scopus 로고    scopus 로고
    • New insight into an old protein: The functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase
    • Sirover MA. 1999. New insight into an old protein: The functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase. Biochim Biophys Acta 1432: 159-184.
    • (1999) Biochim Biophys Acta , vol.1432 , pp. 159-184
    • Sirover, M.A.1
  • 49
    • 1242294390 scopus 로고    scopus 로고
    • Rapid shortening of telomere length in response to ceramide involves the inhibition of telomere binding activity of nuclear glyceraldehyde-3-phosphate dehydrogenase
    • Sundararaj KP, Wood RE, Ponnusamy S, Salas AM, Szule Z, Bielawska A, Obeid LM, Hannun YA, Ogretmen B. 2004. Rapid shortening of telomere length in response to ceramide involves the inhibition of telomere binding activity of nuclear glyceraldehyde-3-phosphate dehydrogenase. J Biol Chem 279:6152.
    • (2004) J Biol Chem , vol.279 , pp. 6152
    • Sundararaj, K.P.1    Wood, R.E.2    Ponnusamy, S.3    Salas, A.M.4    Szule, Z.5    Bielawska, A.6    Obeid, L.M.7    Hannun, Y.A.8    Ogretmen, B.9
  • 50
    • 0033551557 scopus 로고    scopus 로고
    • Over-expression of GAPDH induces apoptosis in COS-7 cells transfected with cloned GAPDH cDNAs
    • Tajima H, Tsuchiya K, Yamada M, Kondo K, Katsube N, Ishitani R. 1999. Over-expression of GAPDH induces apoptosis in COS-7 cells transfected with cloned GAPDH cDNAs. Neuro Report 10:2029-2033.
    • (1999) Neuro Report , vol.10 , pp. 2029-2033
    • Tajima, H.1    Tsuchiya, K.2    Yamada, M.3    Kondo, K.4    Katsube, N.5    Ishitani, R.6
  • 51
    • 0035951872 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is required for vesicular transport in the early secretory pathway
    • Tisdale EJ. 2001. Glyceraldehyde-3-phosphate dehydrogenase is required for vesicular transport in the early secretory pathway. J Biol Chem 276:2480-2486.
    • (2001) J Biol Chem , vol.276 , pp. 2480-2486
    • Tisdale, E.J.1
  • 52
    • 0036479109 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Cι/λ and plays a role in microtubule dynamics in the early secretory pathway
    • Tisdale EJ. 2002. Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Cι/λ and plays a role in microtubule dynamics in the early secretory pathway. J Biol Chem 277:3334-3341.
    • (2002) J Biol Chem , vol.277 , pp. 3334-3341
    • Tisdale, E.J.1
  • 53
    • 0346732291 scopus 로고    scopus 로고
    • Rab2 interacts directly with atypical protein kinase C (aPKC) ι/λ and inhibits aPKC ι/λ-dependent glyceraldehyde-3- phosphate dehydrogenase phosphorylation
    • Tisdale EJ. 2003. Rab2 interacts directly with atypical protein kinase C (aPKC) ι/λ and inhibits aPKC ι/λ-dependent glyceraldehyde-3-phosphate dehydrogenase phosphorylation. J Biol Chem 278:52524-52530.
    • (2003) J Biol Chem , vol.278 , pp. 52524-52530
    • Tisdale, E.J.1
  • 54
    • 8144219547 scopus 로고    scopus 로고
    • Disclosure of a pro-apoptotic glyceraldehyde-3-phosphate dehydrogenase promoter: Anti-dementia drugs depress its activation in apoptosis
    • Tsuchiya K, Tajima H, Yamada M, Takahashi H, Kuwae T, Sunaga K, Katsube N, Ishitani R. 2004. Disclosure of a pro-apoptotic glyceraldehyde-3-phosphate dehydrogenase promoter: Anti-dementia drugs depress its activation in apoptosis. Life Sci 74:3245-3258.
    • (2004) Life Sci , vol.74 , pp. 3245-3258
    • Tsuchiya, K.1    Tajima, H.2    Yamada, M.3    Takahashi, H.4    Kuwae, T.5    Sunaga, K.6    Katsube, N.7    Ishitani, R.8
  • 57
    • 0041352962 scopus 로고    scopus 로고
    • S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component
    • Zheng L, Roeder RG, Luo Y. 2003. S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component. Cell 114: 255-266.
    • (2003) Cell , vol.114 , pp. 255-266
    • Zheng, L.1    Roeder, R.G.2    Luo, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.