메뉴 건너뛰기




Volumn 7, Issue 2, 2012, Pages 154-167

ATP citrate lyase inhibitors as novel cancer therapeutic agents

Author keywords

ACL inhibitors; ATP citrate lyase; Cancer therapy; Citrate; Lipogenesis; Small chemicals

Indexed keywords

2 HYDROXY N ARYLBENZENESULFONAMIDE; 2,3 BUTANEDIONE; 3 THIADICARBOXYLIC ACID; 3,3,14,14 TETRAMETHYLHEXADECANEDIOIC ACID; ADENOSINE TRIPHOSPHATE CITRATE LYASE; ADENOSINE TRIPHOSPHATE CITRATE LYASE INHIBITOR; ANTIMYCIN A1A; ANTIMYCIN A1B; ANTIMYCIN A2A; ANTINEOPLASTIC AGENT; CISPLATIN; CITRIC ACID DERIVATIVE; CITRININ; DEOXYCHOLIC ACID; DICARBOXYLIC ACID DERIVATIVE; GARCINIA EXTRACT; GLUTAMIC ACID; HYDROXYCITRIC ACID; METHIONINE SULFOXIMINE; METHOTREXATE; PHENYLGLYOXAL; PLANT EXTRACT; POLYCHLORINATED BIPHENYL DERIVATIVE; PURPURONE; RADICICOL; SB 201076; SB 204990; SUCCINIC ACID DERIVATIVE; THIOCTIC ACID; UNCLASSIFIED DRUG; UNINDEXED DRUG; VANADIC ACID;

EID: 84860282413     PISSN: 15748928     EISSN: None     Source Type: Journal    
DOI: 10.2174/157489212799972954     Document Type: Review
Times cited : (56)

References (111)
  • 1
    • 77954618219 scopus 로고    scopus 로고
    • Metabolism in cancer patients
    • Arends J. Metabolism in cancer patients. Anticancer Res 2010; 30: 1863-8.
    • (2010) Anticancer Res , vol.30 , pp. 1863-1868
    • Arends, J.1
  • 2
    • 0032529044 scopus 로고    scopus 로고
    • The role of ATP citrate-lyase in the metabolic regulation of plasma lipids. Hypolipidaemic effects of SB-204990, a lactone prodrug of the potent ATP citrate-lyase inhibitor SB-201076
    • Pearce NJ, Yates JW, Berkhout TA, Jackson B, Tew D, Boyd H. The role of ATP citrate-lyase in the metabolic regulation of plasma lipids. Hypolipidaemic effects of SB-204990, a lactone prodrug of the potent ATP citrate-lyase inhibitor SB-201076. Biochem J 1998; 334: 113-9.
    • (1998) Biochem J , vol.334 , pp. 113-119
    • Pearce, N.J.1    Yates, J.W.2    Berkhout, T.A.3    Jackson, B.4    Tew, D.5    Boyd, H.6
  • 3
    • 0012249041 scopus 로고
    • Metabolism of neoplastic tissue. IV. A study of lipid synthesis in neoplastic tissue slices in vitro
    • Medes G, Thomas A, Weinhouse S. Metabolism of neoplastic tissue. IV. A study of lipid synthesis in neoplastic tissue slices in vitro. Cancer Res 1953; 13: 27-9.
    • (1953) Cancer Res , vol.13 , pp. 27-29
    • Medes, G.1    Thomas, A.2    Weinhouse, S.3
  • 4
    • 0242363618 scopus 로고    scopus 로고
    • Discovery of gene networks regulating cytokineinduced dysfunction and apoptosis in insulin-producing INS-1 cells
    • Kutlu B, Cardozo AK, Darville MI, Kruhøffer M, Magnusson N, Ørntoft T, et al. Discovery of gene networks regulating cytokineinduced dysfunction and apoptosis in insulin-producing INS-1 cells. Diabetes 2003; 52: 2701-19.
    • (2003) Diabetes , vol.52 , pp. 2701-2719
    • Kutlu, B.1    Cardozo, A.K.2    Darville, M.I.3    Kruhøffer, M.4    Magnusson, N.5    Ørntoft, T.6
  • 5
    • 0034002793 scopus 로고    scopus 로고
    • Fatty-acid synthase and human cancer: New perspectives on its role in tumor biology
    • Kuhajda FP. Fatty-acid synthase and human cancer: New perspectives on its role in tumor biology. Nutrition 2000; 16: 202-8.
    • (2000) Nutrition , vol.16 , pp. 202-208
    • Kuhajda, F.P.1
  • 6
    • 9544254829 scopus 로고    scopus 로고
    • ATP-citrate lyase as a target for hypolipidemic intervention. Design and synthesis of 2-substituted butanedioic acids as novel, potent inhibitors of the enzyme
    • Gribble AD, Dolle RE, Shaw A, McNair D, Novelli R, Novelli CE, et al. ATP-citrate lyase as a target for hypolipidemic intervention. Design and synthesis of 2-substituted butanedioic acids as novel, potent inhibitors of the enzyme. J Med Chem 1996; 39: 3569-84.
    • (1996) J Med Chem , vol.39 , pp. 3569-3584
    • Gribble, A.D.1    Dolle, R.E.2    Shaw, A.3    McNair, D.4    Novelli, R.5    Novelli, C.E.6
  • 8
    • 0036375568 scopus 로고    scopus 로고
    • Kinetic and biochemical analyses on the reaction mechanism of a bacterial ATP-citrate lyase
    • Kanao T, Fukui T, Atomi H, Imanaka T. Kinetic and biochemical analyses on the reaction mechanism of a bacterial ATP-citrate lyase. Eur J Biochem 2002; 269: 3409-16.
    • (2002) Eur J Biochem , vol.269 , pp. 3409-3416
    • Kanao, T.1    Fukui, T.2    Atomi, H.3    Imanaka, T.4
  • 10
    • 77957795415 scopus 로고    scopus 로고
    • ATP-citrate lyase reduction mediates palmitate-induced apoptosis in pancreatic beta cells
    • Chu KY, Lin Y, Hendel A, Kulpa JE, Brownsey RW, Johnson JD. ATP-citrate lyase reduction mediates palmitate-induced apoptosis in pancreatic beta cells. J Biol Chem 2010; 285: 32606-15.
    • (2010) J Biol Chem , vol.285 , pp. 32606-32615
    • Chu, K.Y.1    Lin, Y.2    Hendel, A.3    Kulpa, J.E.4    Brownsey, R.W.5    Johnson, J.D.6
  • 11
    • 0018769394 scopus 로고
    • Lipogenetic and glycolytic enzyme activities in carcinoma and nonmalignant diseases of the human breast
    • Szutowicz A, Kwiatkowski J, Angielski S. Lipogenetic and glycolytic enzyme activities in carcinoma and nonmalignant diseases of the human breast. Br J Cancer 1979; 39: 681-7.
    • (1979) Br J Cancer , vol.39 , pp. 681-687
    • Szutowicz, A.1    Kwiatkowski, J.2    Angielski, S.3
  • 12
    • 0345448918 scopus 로고    scopus 로고
    • Increased activity of glycerol 3-phosphate dehydroge-nase and other lipogenic enzymes in human bladder cancer
    • Turyn J, Schlichtholz B, Dettlaff-Pokora A, Presler M, Goyke E, Matuszewski M, et al. Increased activity of glycerol 3-phosphate dehydroge-nase and other lipogenic enzymes in human bladder cancer. Horm Metab Res 2003; 35: 565-9.
    • (2003) Horm Metab Res , vol.35 , pp. 565-569
    • Turyn, J.1    Schlichtholz, B.2    Dettlaff-Pokora, A.3    Presler, M.4    Goyke, E.5    Matuszewski, M.6
  • 15
    • 34249820242 scopus 로고    scopus 로고
    • Metastatic progression and gene expression between breast cancer cell lines from African American and Caucasian women
    • Yancy HF, Mason JA, Peters S, Thompson CE, Littleton GK, Jett M. Metastatic progression and gene expression between breast cancer cell lines from African American and Caucasian women. J Carcinog 2007; 6: 8.
    • (2007) J Carcinog , vol.6 , pp. 8
    • Yancy, H.F.1    Mason, J.A.2    Peters, S.3    Thompson, C.E.4    Littleton, G.K.5    Jett, M.6
  • 16
    • 77951239243 scopus 로고    scopus 로고
    • Identification of ATP citrate lyase as a positive regulator of glycolytic function in glioblastomas
    • Beckner ME, Fellows-Mayle W, Zhang Z, Agostino NR, Kant JA, Day BW, et al. Identification of ATP citrate lyase as a positive regulator of glycolytic function in glioblastomas. Int J Cancer 2010; 126: 2282-95.
    • (2010) Int J Cancer , vol.126 , pp. 2282-2295
    • Beckner, M.E.1    Fellows-Mayle, W.2    Zhang, Z.3    Agostino, N.R.4    Kant, J.A.5    Day, B.W.6
  • 17
    • 0036570356 scopus 로고    scopus 로고
    • Targets of gene amplification and overexpression at 17q in gastric cancer
    • Varis A, Wolf M, Monni O, Vakkari ML, Kokkola A, Moskaluk C, et al. Targets of gene amplification and overexpression at 17q in gastric cancer. Cancer Res 2002; 62: 2625-9.
    • (2002) Cancer Res , vol.62 , pp. 2625-2629
    • Varis, A.1    Wolf, M.2    Monni, O.3    Vakkari, M.L.4    Kokkola, A.5    Moskaluk, C.6
  • 18
    • 0025058095 scopus 로고
    • Rat ATP citrate-lyase. Molecular cloning and sequence analysis of a full-length cDNA and mRNA abundance as a function of diet, organ, and age
    • Elshourbagy NA, Near JC, Kmetz PJ, Sathe GM, Southan C, Strickler JE, et al. Rat ATP citrate-lyase. Molecular cloning and sequence analysis of a full-length cDNA and mRNA abundance as a function of diet, organ, and age. J Biol Chem 1990; 265: 1430-5.
    • (1990) J Biol Chem , vol.265 , pp. 1430-1435
    • Elshourbagy, N.A.1    Near, J.C.2    Kmetz, P.J.3    Sathe, G.M.4    Southan, C.5    Strickler, J.E.6
  • 19
    • 0017138570 scopus 로고
    • Structure of ATP citrate lyase from rat liver. Physicochemical studies and proteolytic modification
    • Singh M, Richards EG, Mukherjee A, Srere PA. Structure of ATP citrate lyase from rat liver. Physicochemical studies and proteolytic modification. J Biol Chem 1976; 251: 5242-50.
    • (1976) J Biol Chem , vol.251 , pp. 5242-5250
    • Singh, M.1    Richards, E.G.2    Mukherjee, A.3    Srere, P.A.4
  • 21
    • 0034635193 scopus 로고    scopus 로고
    • ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed by x-ray crystallography
    • Joyce MA, Fraser ME, James MN, Bridger WA, Wolodko WT. ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed by x-ray crystallography. Biochemistry 2000; 39: 17-25.
    • (2000) Biochemistry , vol.39 , pp. 17-25
    • Joyce, M.A.1    Fraser, M.E.2    James, M.N.3    Bridger, W.A.4    Wolodko, W.T.5
  • 23
    • 0028276977 scopus 로고
    • The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-A resolution
    • Wolodko WT, Fraser ME, James MN, Bridger WA. The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-A resolution. J Biol Chem 1994; 269: 10883-90.
    • (1994) J Biol Chem , vol.269 , pp. 10883-10890
    • Wolodko, W.T.1    Fraser, M.E.2    James, M.N.3    Bridger, W.A.4
  • 24
    • 33744957627 scopus 로고    scopus 로고
    • Interactions of GTP with the ATP-grasp Domain of GTP-specific Succinyl-CoA Synthetase
    • Fraser ME, Hayakawa K, Hume MS, Ryan DG, Brownie ER. Interactions of GTP with the ATP-grasp Domain of GTP-specific Succinyl-CoA Synthetase. J Biol Chem 2006; 281: 11058-65.
    • (2006) J Biol Chem , vol.281 , pp. 11058-11065
    • Fraser, M.E.1    Hayakawa, K.2    Hume, M.S.3    Ryan, D.G.4    Brownie, E.R.5
  • 25
    • 0034705332 scopus 로고    scopus 로고
    • Phosphorylated and dephosphorylated structures of pig heart, GTPspecific succinyl-CoA synthetase
    • Fraser ME, James MN, Bridger WA, Wolodko WT. Phosphorylated and dephosphorylated structures of pig heart, GTPspecific succinyl-CoA synthetase. J Mol Biol 2000; 299: 1325-39.
    • (2000) J Mol Biol , vol.299 , pp. 1325-1339
    • Fraser, M.E.1    James, M.N.2    Bridger, W.A.3    Wolodko, W.T.4
  • 26
    • 0019813025 scopus 로고
    • ATP-citrate lyase. Structure of a tryptic peptide containing the phosphorylation site directed by glucagon and the cAMP-dependent protein kinase
    • Pierce MW, Palmer JL, Keutmann HT, Avruch J. ATP-citrate lyase. Structure of a tryptic peptide containing the phosphorylation site directed by glucagon and the cAMP-dependent protein kinase. J Biol Chem 1981; 256: 8867-70.
    • (1981) J Biol Chem , vol.256 , pp. 8867-8870
    • Pierce, M.W.1    Palmer, J.L.2    Keutmann, H.T.3    Avruch, J.4
  • 27
    • 0025102029 scopus 로고
    • Sequence of sites on ATP-citrate lyase and phosphatase inhibitor 2 phosphorylated by multifunctional protein kinase (a glycogen synthase kinase 3 like kinase)
    • Ramakrishna S, D'Angelo G, Benjamin WB. Sequence of sites on ATP-citrate lyase and phosphatase inhibitor 2 phosphorylated by multifunctional protein kinase (a glycogen synthase kinase 3 like kinase). Biochemistry 1990; 29: 7617-24.
    • (1990) Biochemistry , vol.29 , pp. 7617-7624
    • Ramakrishna, S.1    D'Angelo, G.2    Benjamin, W.B.3
  • 28
    • 0037072780 scopus 로고    scopus 로고
    • The identification of ATP-citrate lyase as a protein kinase B (Akt) substrate in primary adipocytes
    • Berwick DC, Hers I, Heesom KJ, Moule SK, Tavare JM. The identification of ATP-citrate lyase as a protein kinase B (Akt) substrate in primary adipocytes. J Biol Chem 2002; 277: 33895-900.
    • (2002) J Biol Chem , vol.277 , pp. 33895-33900
    • Berwick, D.C.1    Hers, I.2    Heesom, K.J.3    Moule, S.K.4    Tavare, J.M.5
  • 29
    • 0021750757 scopus 로고
    • Contributions of glycolysis and oxidative phosphorylation to adenosine 5'-triphosphate production in AS-30D hepatoma cells
    • Nakashima RA, Paggi MG, Pedersen PL. Contributions of glycolysis and oxidative phosphorylation to adenosine 5'-triphosphate production in AS-30D hepatoma cells. Cancer Res 1984; 44: 5702-6.
    • (1984) Cancer Res , vol.44 , pp. 5702-5706
    • Nakashima, R.A.1    Paggi, M.G.2    Pedersen, P.L.3
  • 30
    • 0026619273 scopus 로고
    • Deviant energetic metabolism of glycolytic cancer cells
    • Baggetto LG. Deviant energetic metabolism of glycolytic cancer cells. Biochimie 1992; 74: 959-74.
    • (1992) Biochimie , vol.74 , pp. 959-974
    • Baggetto, L.G.1
  • 31
    • 0027441813 scopus 로고
    • The mitochondrial tricarboxylate transport rotein. cDNA cloning, primary structure, and com-parison with other mitochondrial transport proteins
    • Kaplan RS, Mayor JA, Wood DO. The mitochondrial tricarboxylate transport rotein. cDNA cloning, primary structure, and com-parison with other mitochondrial transport proteins. J Biol Chem 1993; 268: 13682-90.
    • (1993) J Biol Chem , vol.268 , pp. 13682-13690
    • Kaplan, R.S.1    Mayor, J.A.2    Wood, D.O.3
  • 32
    • 77956244445 scopus 로고    scopus 로고
    • Identification of the citrate-binding site of human ATP-citrate lyase using X-ray crystallography
    • Sun T, Hayakawa K, Bateman KS, Fraser ME. Identification of the citrate-binding site of human ATP-citrate lyase using X-ray crystallography. J Biol Chem 2010; 285: 27418-28.
    • (2010) J Biol Chem , vol.285 , pp. 27418-27428
    • Sun, T.1    Hayakawa, K.2    Bateman, K.S.3    Fraser, M.E.4
  • 34
    • 0022467061 scopus 로고
    • Effects of an antitumoural rhodium complex on thioacetamide-induced liver tumor in rats. Changes in the activities of ornithine decarboxylase, tyrosine minotransferase and of enzymes involved in fatty acid and glycerolipid synthesis
    • Cascales C, Martin-Sanz P, Pittner RA, Hopewell R, Brindley DN, Cascales M, et al. Effects of an antitumoural rhodium complex on thioacetamide-induced liver tumor in rats. Changes in the activities of ornithine decarboxylase, tyrosine minotransferase and of enzymes involved in fatty acid and glycerolipid synthesis. Biochem Pharmacol 1986; 35: 2655-61.
    • (1986) Biochem Pharmacol , vol.35 , pp. 2655-2661
    • Cascales, C.1    Martin-Sanz, P.2    Pittner, R.A.3    Hopewell, R.4    Brindley, D.N.5    Cascales, M.6
  • 36
    • 0347316398 scopus 로고    scopus 로고
    • The role of adenosine triphosphate citrate lyase in the metabolism of acetyl coenzyme a and function of blood platelets in diabetes mellitus
    • Michno A, Skibowska A, Raszeja-Specht A, Cwikowska J, Szutowicz A. The role of adenosine triphosphate citrate lyase in the metabolism of acetyl coenzyme a and function of blood platelets in diabetes mellitus. Metabolism 2004; 53: 66-72.
    • (2004) Metabolism , vol.53 , pp. 66-72
    • Michno, A.1    Skibowska, A.2    Raszeja-Specht, A.3    Cwikowska, J.4    Szutowicz, A.5
  • 37
    • 0027223550 scopus 로고
    • Kinetic and spatial interrelationships between ganglioside glyco-syltransferases and O-acetyltransferase(s) in human melanoma cells
    • Sjoberg ER, Varki A. Kinetic and spatial interrelationships between ganglioside glyco-syltransferases and O-acetyltransferase(s) in human melanoma cells. J Biol Chem 1993; 268: 10185-96.
    • (1993) J Biol Chem , vol.268 , pp. 10185-10196
    • Sjoberg, E.R.1    Varki, A.2
  • 38
    • 0019579785 scopus 로고
    • Evidence for an essential arginine residue at the active site of ATP citrate lyase from rat liver
    • Ramakrishna S, Benjamin WB. Evidence for an essential arginine residue at the active site of ATP citrate lyase from rat liver. Biochem J 1981; 195: 735-43.
    • (1981) Biochem J , vol.195 , pp. 735-743
    • Ramakrishna, S.1    Benjamin, W.B.2
  • 39
    • 0021746740 scopus 로고
    • Purification and some kinetic properties of rat liver ATP citrate lyase
    • Houston B, Nimmo HG. Purification and some kinetic properties of rat liver ATP citrate lyase. Bio chem J 1984; 224: 437-43.
    • (1984) Bio chem J , vol.224 , pp. 437-443
    • Houston, B.1    Nimmo, H.G.2
  • 40
    • 0023110791 scopus 로고
    • Presence and regulation of ATP: Citrate lyase from the citric acid producing fungus Aspergillus niger
    • Pfitzner A, Kubicek CP, Rohr M. Presence and regulation of ATP: Citrate lyase from the citric acid producing fungus Aspergillus niger. Arch Microbiol 1987; 147: 88-91.
    • (1987) Arch Microbiol , vol.147 , pp. 88-91
    • Pfitzner, A.1    Kubicek, C.P.2    Rohr, M.3
  • 41
    • 0034620591 scopus 로고    scopus 로고
    • Phosphorylation of recombinant human ATP: Citrate lyase by cAMP-dependent protein kinase abolishes homotropic allosteric regulation of the enzyme by citrate and increases the enzyme activity. Allosteric activation of ATP: Citrate lyase by phosphorylated sugars
    • Potapova IA, El-Maghrabi MR, Doronin SV, Benjamin WB. Phosphorylation of recombinant human ATP: Citrate lyase by cAMP-dependent protein kinase abolishes homotropic allosteric regulation of the enzyme by citrate and increases the enzyme activity. Allosteric activation of ATP: Citrate lyase by phosphorylated sugars. Biochemistry 2000; 39: 1169-79.
    • (2000) Biochemistry , vol.39 , pp. 1169-1179
    • Potapova, I.A.1    El-Maghrabi, M.R.2    Doronin, S.V.3    Benjamin, W.B.4
  • 42
    • 0025103362 scopus 로고
    • ATP: Citrate lyase of Rhodotorula gracilis: Purification and properties
    • Shashi K, Bachhawat AK, Joseph R. ATP: Citrate lyase of Rhodotorula gracilis: Purification and properties. Biochim Biophys Acta 1990; 1033: 23-30.
    • (1990) Biochim Biophys Acta , vol.1033 , pp. 23-30
    • Shashi, K.1    Bachhawat, A.K.2    Joseph, R.3
  • 43
    • 0034002018 scopus 로고    scopus 로고
    • Compartmentation of ATP: Citrate lyase in plants
    • Rangasamy D, Ratledge C. Compartmentation of ATP: Citrate lyase in plants. Plant Physiol 2000; 122: 1225-30.
    • (2000) Plant Physiol , vol.122 , pp. 1225-1230
    • Rangasamy, D.1    Ratledge, C.2
  • 44
    • 0034725048 scopus 로고    scopus 로고
    • Transcriptional regulation of the ATP citrate-lyase genebysterol regulatory element-binding proteins
    • Sato R, Okamoto A, Inoue J, Miyamoto W, Sakai Y, Emoto N, et al. Transcriptional regulation of the ATP citrate-lyase genebysterol regulatory element-binding proteins. J Biol Chem 2000; 275: 12497-502.
    • (2000) J Biol Chem , vol.275 , pp. 12497-12502
    • Sato, R.1    Okamoto, A.2    Inoue, J.3    Miyamoto, W.4    Sakai, Y.5    Emoto, N.6
  • 45
    • 0027077743 scopus 로고
    • Regulation of ATP-citrate lyase at transcriptional and post-transcriptional levels in rat liver
    • Kim KS, Park SW, Kim YS. Regulation of ATP-citrate lyase at transcriptional and post-transcriptional levels in rat liver. Biochem Biophys Res Commun 1992; 189: 264-71.
    • (1992) Biochem Biophys Res Commun , vol.189 , pp. 264-271
    • Kim, K.S.1    Park, S.W.2    Kim, Y.S.3
  • 46
    • 0028221152 scopus 로고
    • Induction of hepatic ATP-citrate lyase by insulin in diabetic rat--effects of insulin on the contents of enzyme and its mRNA in cytosol, and the transcriptional activity in nuclei
    • Park SW, Kim KS, Whang SK, Kim JS, Kim YS. Induction of hepatic ATP-citrate lyase by insulin in diabetic rat--effects of insulin on the contents of enzyme and its mRNA in cytosol, and the transcriptional activity in nuclei. Yonsei Med J 1994; 35: 25-33.
    • (1994) Yonsei Med J , vol.35 , pp. 25-33
    • Park, S.W.1    Kim, K.S.2    Whang, S.K.3    Kim, J.S.4    Kim, Y.S.5
  • 48
    • 0033386512 scopus 로고    scopus 로고
    • ranscriptional regulation of fatty acid synthase gene and ATP citrate-lyase gene by Sp1 and Sp3 in rat hepatocytes
    • Fukuda H, Noguchi T, Iritani N. ranscriptional regulation of fatty acid synthase gene and ATP citrate-lyase gene by Sp1 and Sp3 in rat hepatocytes. FEBS Lett 1999; 464: 113-7
    • (1999) FEBS Lett , vol.464 , pp. 113-117
    • Fukuda, H.1    Noguchi, T.2    Iritani, N.3
  • 49
    • 0030046776 scopus 로고    scopus 로고
    • Insulin-and polyunsaturated fatty acid-responsive region(s) of rat ATP citrate lyase gene promoter
    • Fukuda H, Iritani N, Katsurada A, Noguchi T. Insulin-and polyunsaturated fatty acid-responsive region(s) of rat ATP citrate lyase gene promoter. FEBS Lett 1996; 12: 204-7.
    • (1996) FEBS Lett , vol.12 , pp. 204-207
    • Fukuda, H.1    Iritani, N.2    Katsurada, A.3    Noguchi, T.4
  • 50
    • 0030855350 scopus 로고    scopus 로고
    • Transcriptional regulatory region for expression of the rat ATP citrate-lyase gene
    • Fukuda H, Iritani N, Noguchi T. Transcriptional regulatory region for expression of the rat ATP citrate-lyase gene. Eur J Biochem 1997; 247: 497-502.
    • (1997) Eur J Biochem , vol.247 , pp. 497-502
    • Fukuda, H.1    Iritani, N.2    Noguchi, T.3
  • 51
    • 0030753971 scopus 로고    scopus 로고
    • Regulation of the expression of lipogenic enzyme genes by carbohydrate
    • Towle HC, Kaytor EN, Shih HM. Regulation of the expression of lipogenic enzyme genes by carbohydrate. Annu Rev Nutr 1997; 17: 405-33.
    • (1997) Annu Rev Nutr , vol.17 , pp. 405-433
    • Towle, H.C.1    Kaytor, E.N.2    Shih, H.M.3
  • 53
    • 0020646348 scopus 로고
    • Glucose-and insulin-dependent induction of ATP citrate lyase in primary cultures of rat hepatocytes
    • Katz NR, Giffhorn S. Glucose-and insulin-dependent induction of ATP citrate lyase in primary cultures of rat hepatocytes. Biochem J 1983; 212: 65-71.
    • (1983) Biochem J , vol.212 , pp. 65-71
    • Katz, N.R.1    Giffhorn, S.2
  • 55
    • 0038329800 scopus 로고    scopus 로고
    • GTP, a nonsubstrate of ATP citrate lyase, is a phosphodonor for the enzyme histidine autophosphorylation
    • Tuhácková Z, Krivánek J. GTP, a nonsubstrate of ATP citrate lyase, is a phosphodonor for the enzyme histidine autophosphorylation. Biochem Biophys Res Commun 1996; 218: 61-6.
    • (1996) Biochem Biophys Res Commun , vol.218 , pp. 61-66
    • Tuhácková, Z.1    Krivánek, J.2
  • 56
    • 0029101744 scopus 로고
    • Phosphorylation of ATP-citrate lyase by nucleoside diphosphate kinase
    • Wagner PD, Vu ND. Phosphorylation of ATP-citrate lyase by nucleoside diphosphate kinase. J Biol Chem 1995; 270: 21758-64.
    • (1995) J Biol Chem , vol.270 , pp. 21758-21764
    • Wagner, P.D.1    Vu, N.D.2
  • 57
    • 0018704572 scopus 로고
    • Purification of a hepatic 123000-dalton hormone-stimulated 32Ppeptide and its identification as ATP-citrate lyase
    • Alexander MC, Kowaloff EM, Witters LA, Dennihy DT, Avruch J. Purification of a hepatic 123000-dalton hormone-stimulated 32Ppeptide and its identification as ATP-citrate lyase. J Biol Chem 1979; 254: 8052-6.
    • (1979) J Biol Chem , vol.254 , pp. 8052-8056
    • Alexander, M.C.1    Kowaloff, E.M.2    Witters, L.A.3    Dennihy, D.T.4    Avruch, J.5
  • 58
    • 0025290954 scopus 로고
    • An insulin-sensitive cytosolic protein kinase accounts for the regulation of ATP citrate-lyase phosphorylation
    • Yu KT, Benjamin WB, Ramakrishna S, Khalaf N, Czech MP. An insulin-sensitive cytosolic protein kinase accounts for the regulation of ATP citrate-lyase phosphorylation. Biochem J 1990; 268: 539-45.
    • (1990) Biochem J , vol.268 , pp. 539-545
    • Yu, K.T.1    Benjamin, W.B.2    Ramakrishna, S.3    Khalaf, N.4    Czech, M.P.5
  • 59
    • 30544433533 scopus 로고    scopus 로고
    • ATP citrate lyase is an important component of cell growth and transformation
    • Bauer DE, Hatzivassiliou G, Zhao F, Andreadis C, Thompson CB. ATP citrate lyase is an important component of cell growth and transformation. Oncogene 2005; 24: 6314-22.
    • (2005) Oncogene , vol.24 , pp. 6314-6322
    • Bauer, D.E.1    Hatzivassiliou, G.2    Zhao, F.3    Andreadis, C.4    Thompson, C.B.5
  • 60
    • 54249161009 scopus 로고    scopus 로고
    • ATP citrate lyase: Activation and therapeutic implications in non-small cell lung cancer
    • Migita T, Narita T, Nomura K, Miyagi E, Inazuka F, Matsuura M, et al. ATP citrate lyase: Activation and therapeutic implications in non-small cell lung cancer. Cancer Res 2008; 68: 8547-54.
    • (2008) Cancer Res , vol.68 , pp. 8547-8554
    • Migita, T.1    Narita, T.2    Nomura, K.3    Miyagi, E.4    Inazuka, F.5    Matsuura, M.6
  • 61
    • 65549096661 scopus 로고    scopus 로고
    • De novo fatty-acid synthesis and related pathways as molecular targets for cancer therapy
    • Mashima T, Seimiya H, Tsuruo T. De novo fatty-acid synthesis and related pathways as molecular targets for cancer therapy. Br J Cancer 2009; 100: 1369-72.
    • (2009) Br J Cancer , vol.100 , pp. 1369-1372
    • Mashima, T.1    Seimiya, H.2    Tsuruo, T.3
  • 62
    • 33744969828 scopus 로고    scopus 로고
    • Energy deregulation: Licensing tumors to grow
    • Garber K. Energy deregulation: Licensing tumors to grow. Science 2006; 312: 1158-9.
    • (2006) Science , vol.312 , pp. 1158-1159
    • Garber, K.1
  • 63
    • 77950841021 scopus 로고    scopus 로고
    • A combination of alpha lipoic acid and calcium hydroxycitrate is efficient against mouse cancer models: Preliminary results
    • Schwartz L, Abolhassani M, Guais A, Sanders E, Steyaert JM, Campion F, et al. A combination of alpha lipoic acid and calcium hydroxycitrate is efficient against mouse cancer models: Preliminary results. Oncol Rep 2010; 23: 1407-16.
    • (2010) Oncol Rep , vol.23 , pp. 1407-1416
    • Schwartz, L.1    Abolhassani, M.2    Guais, A.3    Sanders, E.4    Steyaert, J.M.5    Campion, F.6
  • 64
    • 57649128306 scopus 로고    scopus 로고
    • Inhibition of fattyacid synthase induces caspase-8-mediated tumor cell apoptosis by up-regulating DDIT4
    • Knowles LM, Yang C, Osterman A, Smith JW. Inhibition of fattyacid synthase induces caspase-8-mediated tumor cell apoptosis by up-regulating DDIT4. J Biol Chem 2008; 283: 31378-84.
    • (2008) J Biol Chem , vol.283 , pp. 31378-31384
    • Knowles, L.M.1    Yang, C.2    Osterman, A.3    Smith, J.W.4
  • 69
    • 0033646094 scopus 로고    scopus 로고
    • Effects of acute (-)hydroxycitrate supplementation on substrate metabolism at rest and during exercise in humans
    • van Loon LJ, van Rooijen JJ, Niesen B, Verhagen H, Saris WH, Wagenmakers AJ. Effects of acute (-)hydroxycitrate supplementation on substrate metabolism at rest and during exercise in humans. Am J Clin Nutr 2000; 72: 1445-50.
    • (2000) Am J Clin Nutr , vol.72 , pp. 1445-1450
    • van Loon, L.J.1    van Rooijen, J.J.2    Niesen, B.3    Verhagen, H.4    Saris, W.H.5    Wagenmakers, A.J.6
  • 71
    • 34250678991 scopus 로고    scopus 로고
    • Chemistry, physiological properties, and microbial production of hydroxycitric acid
    • Yamada T, Hida H, Yamada Y. Chemistry, physiological properties, and microbial production of hydroxycitric acid. Appl Microbiol Biotechnol 2007; 75: 977-82.
    • (2007) Appl Microbiol Biotechnol , vol.75 , pp. 977-982
    • Yamada, T.1    Hida, H.2    Yamada, Y.3
  • 72
    • 0014618774 scopus 로고
    • Tricarballylate and hydroxycitrate: Substrate and inhibitor of ATP: Citrateoxaloacetate lyase
    • Watson JA, Fang M, Lowenstein JM. Tricarballylate and hydroxycitrate: Substrate and inhibitor of ATP: Citrateoxaloacetate lyase. Arch Biochem Biophys 1969; 135: 209-17.
    • (1969) Arch Biochem Biophys , vol.135 , pp. 209-217
    • Watson, J.A.1    Fang, M.2    Lowenstein, J.M.3
  • 73
    • 0015840321 scopus 로고
    • Inhibition of enzymes which interact with citrate by (-)-hydroxycitrate and 1,2,3-tricarboxybenzene
    • Cheema-Dhadli S, Halperin ML, Leznoff CC. Inhibition of enzymes which interact with citrate by (-)-hydroxycitrate and 1,2,3-tricarboxybenzene. Eur J Biochem 1973; 38: 98-102.
    • (1973) Eur J Biochem , vol.38 , pp. 98-102
    • Cheema-Dhadli, S.1    Halperin, M.L.2    Leznoff, C.C.3
  • 74
    • 0017358376 scopus 로고
    • Hypolipidemic activity of (-)-hydroxy-citrate
    • Sullivan AC, Triscari J, Hamilton JG. Hypolipidemic activity of (-)-hydroxy-citrate. Lipids 1977; 12: 1-9.
    • (1977) Lipids , vol.12 , pp. 1-9
    • Sullivan, A.C.1    Triscari, J.2    Hamilton, J.G.3
  • 75
    • 0017672536 scopus 로고
    • Reactivity and inhibitor potential of hydroxycitrate isomers with citrate synthase, citrate lyase, and ATP citrate lyase
    • Sullivan AC, Singh M, Srere PA, Glusker JP. Reactivity and inhibitor potential of hydroxycitrate isomers with citrate synthase, citrate lyase, and ATP citrate lyase. J BiolChem 1977; 252: 7583-90.
    • (1977) J BiolChem , vol.252 , pp. 7583-7590
    • Sullivan, A.C.1    Singh, M.2    Srere, P.A.3    Glusker, J.P.4
  • 76
    • 0242577147 scopus 로고    scopus 로고
    • Acetate and butyrate are the major substrates for de novo lipogenesis in rat colonic epithelial cells
    • Zambell KL, Fitch MD, Fleming SE. Acetate and butyrate are the major substrates for de novo lipogenesis in rat colonic epithelial cells. J Nutr Sci Vitaminol 2003; 133: 3509-15.
    • (2003) J Nutr Sci Vitaminol , vol.133 , pp. 3509-3515
    • Zambell, K.L.1    Fitch, M.D.2    Fleming, S.E.3
  • 77
    • 0025251789 scopus 로고
    • The effect of (-)-hydroxycitrate on the activity of the low-density-lipoprotein receptor and 3-hydroxy-3-methylglutaryl-CoA reductase levels in the human hepatoma cell line HepG2
    • Berkhout TA, Havekes LM, Pearce NJ, Groot PH. The effect of (-)-hydroxycitrate on the activity of the low-density-lipoprotein receptor and 3-hydroxy-3-methylglutaryl-CoA reductase levels in the human hepatoma cell line HepG2. Biochem J 1990;272: 181-6.
    • (1990) Biochem J , vol.272 , pp. 181-186
    • Berkhout, T.A.1    Havekes, L.M.2    Pearce, N.J.3    Groot, P.H.4
  • 78
    • 84856515477 scopus 로고    scopus 로고
    • Adding a combination of hydroxycitrate and lipoic acid (METABLOC™) to chemotherapy improves effectiveness against tumor development: Experimental results and case report
    • Guais A, Baronzio G, Sanders E, Campion F, Mainini C, Fiorentini G, et al. Adding a combination of hydroxycitrate and lipoic acid (METABLOC™) to chemotherapy improves effectiveness against tumor development: Experimental results and case report. Invest New Drugs 2012; 30: 200-11.
    • (2012) Invest New Drugs , vol.30 , pp. 200-211
    • Guais, A.1    Baronzio, G.2    Sanders, E.3    Campion, F.4    Mainini, C.5    Fiorentini, G.6
  • 81
    • 0017403518 scopus 로고
    • Metabolic regulation as a control for lipid disorders. II. Influence of (--)-hydroxycitrate on genetically and experimentally induced hypertriglyceridemia in the rat
    • Sullivan AC, Triscari J, Spiegel JE. Metabolic regulation as a control for lipid disorders. II. Influence of (--)-hydroxycitrate on genetically and experimentally induced hypertriglyceridemia in the rat. Am J Clin Nutr 1977; 30: 777-84.
    • (1977) Am J Clin Nutr , vol.30 , pp. 777-784
    • Sullivan, A.C.1    Triscari, J.2    Spiegel, J.E.3
  • 82
    • 0020957544 scopus 로고
    • Interactions of between insulin and thyroid hormone in the control of lipogenesis
    • Sugden MC, Steare SE, Watts DI, Palmer TN. Interactions of between insulin and thyroid hormone in the control of lipogenesis. Biochem J 1983; 210: 937-44.
    • (1983) Biochem J , vol.210 , pp. 937-944
    • Sugden, M.C.1    Steare, S.E.2    Watts, D.I.3    Palmer, T.N.4
  • 84
    • 0027094047 scopus 로고
    • ATP-citrate lyase as a target for hypolipidemic intervention. Sulfoximine and 3-hydroxy-beta-lactam containing analogues of citric acid as potential tight-binding inhibitors
    • Dolle RE, McNair D, Hughes MJ, Kruse LI, Eggelston D, Saxty BA, et al. ATP-citrate lyase as a target for hypolipidemic intervention. Sulfoximine and 3-hydroxy-beta-lactam containing analogues of citric acid as potential tight-binding inhibitors. J Med Chem 1992; 35: 4875-84.
    • (1992) J Med Chem , vol.35 , pp. 4875-4884
    • Dolle, R.E.1    McNair, D.2    Hughes, M.J.3    Kruse, L.I.4    Eggelston, D.5    Saxty, B.A.6
  • 85
    • 0029002448 scopus 로고
    • Synthesis of novel thiol-containing citric acid analogues. Kinetic evaluation of these and other potential active-site-directed and mechanism-based inhibitors of ATP citrate lyase
    • Dolle RE, Gribble A, Wilkes T, Kruse LI, Eggleston D, Saxty BA, et al. Synthesis of novel thiol-containing citric acid analogues. Kinetic evaluation of these and other potential active-site-directed and mechanism-based inhibitors of ATP citrate lyase. J Med Chem 1995; 38: 537-43.
    • (1995) J Med Chem , vol.38 , pp. 537-543
    • Dolle, R.E.1    Gribble, A.2    Wilkes, T.3    Kruse, L.I.4    Eggleston, D.5    Saxty, B.A.6
  • 88
    • 0019886922 scopus 로고
    • Stereochemical outcome of processing of fluorinated substrates by ATP citrate lyase and malate synthase
    • Marletta MA, Srere PA, Walsh C. Stereochemical outcome of processing of fluorinated substrates by ATP citrate lyase and malate synthase. Biochemistry 1981; 20: 3719-23.
    • (1981) Biochemistry , vol.20 , pp. 3719-3723
    • Marletta, M.A.1    Srere, P.A.2    Walsh, C.3
  • 89
    • 0025884649 scopus 로고
    • Preparation of (+)-erythro)and (+)-(threo)-2-vinyl citric acids as potential mechanism-based inhibitors of ATP-citrate lyase
    • Dolle RE, Novelli R, Saxty BA. Preparation of (+)-erythro)and (+)-(threo)-2-vinyl citric acids as potential mechanism-based inhibitors of ATP-citrate lyase. Tetrahedron Lett 1991; 32: 4587-90.
    • (1991) Tetrahedron Lett , vol.32 , pp. 4587-4590
    • Dolle, R.E.1    Novelli, R.2    Saxty, B.A.3
  • 90
    • 0026321684 scopus 로고
    • Synthesis and evaluation of (+) and (-)-2,2-difluorocitrate as inhibitors of rat-liver ATP-citrate lyase and porcine-heart aconitase
    • Saxty BA, Novelli R, Dolle RE, Kruse LI, Reid DG, Camilleri P, et al. Synthesis and evaluation of (+) and (-)-2,2-difluorocitrate as inhibitors of rat-liver ATP-citrate lyase and porcine-heart aconitase. Eur J Biochem 1991; 202: 889-96.
    • (1991) Eur J Biochem , vol.202 , pp. 889-896
    • Saxty, B.A.1    Novelli, R.2    Dolle, R.E.3    Kruse, L.I.4    Reid, D.G.5    Camilleri, P.6
  • 93
    • 0031844350 scopus 로고    scopus 로고
    • Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin
    • Schulte TW, Akinaga S, Soga S, Sullivan W, Stensgard B, Toft D, et al. Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin. Cell Stress Chaperones 1998; 3: 100-8.
    • (1998) Cell Stress Chaperones , vol.3 , pp. 100-108
    • Schulte, T.W.1    Akinaga, S.2    Soga, S.3    Sullivan, W.4    Stensgard, B.5    Toft, D.6
  • 94
    • 0032554763 scopus 로고    scopus 로고
    • Targeting of the protein chaperone, HSP90, by the transformation suppressing agent, radicicol
    • Sharma SV, Agatsuma T, Nakano H. Targeting of the protein chaperone, HSP90, by the transformation suppressing agent, radicicol. Oncogene 1998; 16: 2639-45.
    • (1998) Oncogene , vol.16 , pp. 2639-2645
    • Sharma, S.V.1    Agatsuma, T.2    Nakano, H.3
  • 95
    • 37249016344 scopus 로고    scopus 로고
    • A role for ATP-citrate lyase, malic enzyme, and pyruvate/citrate cycling in glucose-induced insulin secretion
    • Guay C, Madiraju SR, Aumais A, Joly E, Prentki M. A role for ATP-citrate lyase, malic enzyme, and pyruvate/citrate cycling in glucose-induced insulin secretion. J Biol Chem 2007; 282: 35657-65.
    • (2007) J Biol Chem , vol.282 , pp. 35657-35665
    • Guay, C.1    Madiraju, S.R.2    Aumais, A.3    Joly, E.4    Prentki, M.5
  • 98
    • 15644363825 scopus 로고    scopus 로고
    • ATP-Citrate lyase as a target for hypolipidemic intervention. 2. Synthesis and evaluation of (3R,5S)-omega-substituted-3-carboxy-3, 5-dihydroxyalkanoic acids and their gamma-lactone prodrugs as inhibitors of the enzyme in vitro and in vivo
    • Gribble AD, Ife RJ, Shaw A, McNair D, Novelli CE, Bakewell S, et al. ATP-Citrate lyase as a target for hypolipidemic intervention. 2. Synthesis and evaluation of (3R,5S)-omega-substituted-3-carboxy-3, 5-dihydroxyalkanoic acids and their gamma-lactone prodrugs as inhibitors of the enzyme in vitro and in vivo. J Med Chem 1998; 41: 3582-95.
    • (1998) J Med Chem , vol.41 , pp. 3582-3595
    • Gribble, A.D.1    Ife, R.J.2    Shaw, A.3    McNair, D.4    Novelli, C.E.5    Bakewell, S.6
  • 100
    • 0036319122 scopus 로고    scopus 로고
    • MEDICA 16 inhibits hepatic acetyl-CoA carboxylase and reduces plasma triacylglycerol levels in insulin-resistant JCR: LA-cp rats
    • Atkinson LL, Kelly SE, Russell JC, Bar-Tana J, Lopaschuk GD. MEDICA 16 inhibits hepatic acetyl-CoA carboxylase and reduces plasma triacylglycerol levels in insulin-resistant JCR: LA-cp rats. Diabetes 2002; 51: 1548-55.
    • (2002) Diabetes , vol.51 , pp. 1548-1555
    • Atkinson, L.L.1    Kelly, S.E.2    Russell, J.C.3    Bar-Tana, J.4    Lopaschuk, G.D.5
  • 101
    • 0021812755 scopus 로고
    • Inhibition of lipid synthesis by beta beta'-tetramethyl-substituted, C14-C22, alpha, omega-dicarboxylic acids in cultured rat hepatocytes
    • Rose-Kahn G, Bar-Tana J. Inhibition of lipid synthesis by beta beta'-tetramethyl-substituted, C14-C22, alpha, omega-dicarboxylic acids in cultured rat hepatocytes. J Biol Chem 1985; 260: 8411-5.
    • (1985) J Biol Chem , vol.260 , pp. 8411-8415
    • Rose-Kahn, G.1    Bar-Tana, J.2
  • 105
    • 0027324752 scopus 로고
    • Purpurone, an inhibitor of ATP-citrate lyase: A novel alkaloid from the marine sponge Iotrochota sp
    • Chan GW, Francis T, Thureen DR, Offen PH, Pierce NJ, Westley JW, et al. Purpurone, an inhibitor of ATP-citrate lyase: A novel alkaloid from the marine sponge Iotrochota sp. J Org Chem 1993; 58: 2544-6.
    • (1993) J Org Chem , vol.58 , pp. 2544-2546
    • Chan, G.W.1    Francis, T.2    Thureen, D.R.3    Offen, P.H.4    Pierce, N.J.5    Westley, J.W.6
  • 106
    • 77956564684 scopus 로고    scopus 로고
    • One-Pot AgOAc-mediated synthesis of polysubstituted pyrroles from primaryamines and aldehydes: Application to the total synthesis of purpurone
    • Li QJ, Fan AL, Lu ZY, Cu YX, Lin WH, Jia YX. One-Pot AgOAc-mediated synthesis of polysubstituted pyrroles from primaryamines and aldehydes: Application to the total synthesis of purpurone. Org Lett 2010; 12: 4066-9.
    • (2010) Org Lett , vol.12 , pp. 4066-4069
    • Li, Q.J.1    Fan, A.L.2    Lu, Z.Y.3    Cu, Y.X.4    Lin, W.H.5    Jia, Y.X.6
  • 107
    • 0015997032 scopus 로고
    • The inhibition of rat brain ATP: Citrate oxaloacetate-lyase by L-glutamate
    • Szutowicz A, Stepień M, Angielski S. The inhibition of rat brain ATP: Citrate oxaloacetate-lyase by L-glutamate. J Neurochem 1974; 22: 85-91.
    • (1974) J Neurochem , vol.22 , pp. 85-91
    • Szutowicz, A.1    Stepień, M.2    Angielski, S.3
  • 108
    • 0028092754 scopus 로고
    • Early changes in energy metabolism in rats exposed to an acute level of deoxycholate and fed a Nigerian-like diet
    • Eriyamremu GE, Adamson I. Early changes in energy metabolism in rats exposed to an acute level of deoxycholate and fed a Nigerian-like diet. Ann Nutr Metab 1994; 38: 174-83.
    • (1994) Ann Nutr Metab , vol.38 , pp. 174-183
    • Eriyamremu, G.E.1    Adamson, I.2
  • 109
    • 0019837081 scopus 로고
    • In vivo inhibition of citrate cleavage enzyme by polychlorinated biphenyls
    • Kling D, Gamble W. In vivo inhibition of citrate cleavage enzyme by polychlorinated biphenyls. Experientia 1981; 37: 1258-9.
    • (1981) Experientia , vol.37 , pp. 1258-1259
    • Kling, D.1    Gamble, W.2
  • 110
    • 0022667078 scopus 로고
    • Role of vanadium in biology. Symposium summary
    • Nechay BR, Nanninga LB, Nechay PSE. Role of vanadium in biology. Symposium summary. Fed Proc 1986; 45: 123-32.
    • (1986) Fed Proc , vol.45 , pp. 123-132
    • Nechay, B.R.1    Nanninga, L.B.2    Nechay, P.S.E.3
  • 111
    • 0025872905 scopus 로고
    • ATP-citrate lyase is another enzyme the histidine phosphorylation of which is inhibited by vanadate
    • Krivanek J, Novakova L. ATP-citrate lyase is another enzyme the histidine phosphorylation of which is inhibited by vanadate. FEBS Lett 1991; 282: 32-4.
    • (1991) FEBS Lett , vol.282 , pp. 32-34
    • Krivanek, J.1    Novakova, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.