메뉴 건너뛰기




Volumn 81, Issue 5, 2011, Pages 649-660

Soraphen A, an inhibitor of acetyl CoA carboxylase activity, interferes with fatty acid elongation

Author keywords

Acetyl CoA carboxylase; De novo lipogenesis; Fatty acid desaturation; Fatty acid elongation; Fatty acid oxidation; Soraphen A

Indexed keywords

ACETYL COENZYME A CARBOXYLASE; ACETYL COENZYME A CARBOXYLASE 1; ACETYL COENZYME A CARBOXYLASE 2; ANTIOBESITY AGENT; FATTY ACID; FATTY ACID DESATURASE FADS1; FATTY ACID DESATURASE FADS2; FATTY ACID ELONGASE; FATTY ACID ELONGASE ELOVL5; FATTY ACID ELONGASE ELOVL6; LINOLEIC ACID; MALONYL COENZYME A; MONOUNSATURATED FATTY ACID; PALMITIC ACID; POLYUNSATURATED FATTY ACID; SATURATED FATTY ACID; SORAPHEN A; UNCLASSIFIED DRUG; UNSATURATED FATTY ACID; VERY LONG CHAIN FATTY ACID;

EID: 79551480612     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2010.12.014     Document Type: Article
Times cited : (95)

References (62)
  • 1
    • 33744781581 scopus 로고    scopus 로고
    • Liver-specific deletion of acetyl-CoA carboxylase 1 reduces hepatic triglyceride accumulation without affecting glucose homeostasis
    • J. Mao, F.J. DeMayo, and H. Li Liver-specific deletion of acetyl-CoA carboxylase 1 reduces hepatic triglyceride accumulation without affecting glucose homeostasis Proc Natl Acad Sci USA 103 2006 8552 8557
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 8552-8557
    • Mao, J.1    Demayo, F.J.2    Li, H.3
  • 2
    • 24744448667 scopus 로고    scopus 로고
    • Mutant mice lacking acetyl-CoA carboxylase 1 are embryonically lethal
    • L. Abu-Elheiga, M.M. Matzuk, and P. Kordari Mutant mice lacking acetyl-CoA carboxylase 1 are embryonically lethal Proc Natl Acad Sci USA 102 2005 12011 12016
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 12011-12016
    • Abu-Elheiga, L.1    Matzuk, M.M.2    Kordari, P.3
  • 3
    • 36749052873 scopus 로고    scopus 로고
    • Continuous fat oxidation in acetyl-CoA carboxylase 2 knockout mice increases total energy expenditure, reduces fat mass, and improves insulin sensitivity
    • C.S. Choi, D.B. Savage, and L. Abu-Elheiga Continuous fat oxidation in acetyl-CoA carboxylase 2 knockout mice increases total energy expenditure, reduces fat mass, and improves insulin sensitivity Proc Natl Acad Sci USA 104 2007 16480 16485
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 16480-16485
    • Choi, C.S.1    Savage, D.B.2    Abu-Elheiga, L.3
  • 4
    • 22544480378 scopus 로고    scopus 로고
    • New hepatic fat activates PPARα to maintain glucose, lipid, and cholesterol homeostasis
    • M.V. Chakravarthy, Z. Pan, and Y. Zhu New hepatic fat activates PPARα to maintain glucose, lipid, and cholesterol homeostasis Cell Metab 1 2005 309 322
    • (2005) Cell Metab , vol.1 , pp. 309-322
    • Chakravarthy, M.V.1    Pan, Z.2    Zhu, Y.3
  • 5
    • 0037143752 scopus 로고    scopus 로고
    • Loss of stearoyl-CoA desaturase-1 function protects mice against adiposity
    • J.M. Ntambi, M. Miyazaki, and J.P. Stoehr Loss of stearoyl-CoA desaturase-1 function protects mice against adiposity Proc Natl Acad Sci USA 99 2002 11482 11486
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 11482-11486
    • Ntambi, J.M.1    Miyazaki, M.2    Stoehr, J.P.3
  • 6
    • 0034730532 scopus 로고    scopus 로고
    • The biosynthesis of hepatic cholesterol esters and triglycerides is impaired in mice with a disruption of the gene for stearoyl-CoA desaturase 1
    • M. Miyazaki, Y.C. Kim, and M.P. Gray-Keller The biosynthesis of hepatic cholesterol esters and triglycerides is impaired in mice with a disruption of the gene for stearoyl-CoA desaturase 1 J Biol Chem 275 2000 30132 30138
    • (2000) J Biol Chem , vol.275 , pp. 30132-30138
    • Miyazaki, M.1    Kim, Y.C.2    Gray-Keller, M.P.3
  • 8
    • 34548580317 scopus 로고    scopus 로고
    • Chemical inhibition of acetyl-CoA carboxylase induces growth arrest and cytotoxicity selectively in cancer cells
    • A. Beckers, S. Organe, and L. Timmermans Chemical inhibition of acetyl-CoA carboxylase induces growth arrest and cytotoxicity selectively in cancer cells Cancer Res 67 2007 8180 8187
    • (2007) Cancer Res , vol.67 , pp. 8180-8187
    • Beckers, A.1    Organe, S.2    Timmermans, L.3
  • 9
    • 3042619469 scopus 로고    scopus 로고
    • Acetyl-CoA carboxylase inhibition for the treatment of metabolic syndrome
    • H.J. Harwood Jr Acetyl-CoA carboxylase inhibition for the treatment of metabolic syndrome Curr Opin Investig Drugs 5 2004 283 289
    • (2004) Curr Opin Investig Drugs , vol.5 , pp. 283-289
    • Harwood Jr., H.J.1
  • 10
    • 18144396604 scopus 로고    scopus 로고
    • Treating the metabolic syndrome: Acetyl-CoA carboxylase inhibition
    • H.J. Harwood Jr Treating the metabolic syndrome: acetyl-CoA carboxylase inhibition Expert Opin Ther Targets 9 2005 267 281
    • (2005) Expert Opin Ther Targets , vol.9 , pp. 267-281
    • Harwood Jr., H.J.1
  • 11
    • 18044388542 scopus 로고    scopus 로고
    • Stearoyl-CoA desaturase as a new drug target for obesity treatment
    • A. Dobrzyn, and J.M. Ntambi Stearoyl-CoA desaturase as a new drug target for obesity treatment Obes Rev 6 2005 169 174
    • (2005) Obes Rev , vol.6 , pp. 169-174
    • Dobrzyn, A.1    Ntambi, J.M.2
  • 13
    • 0141510051 scopus 로고    scopus 로고
    • Isozyme-nonselective N-substituted bipiperidylcarboxamide acetyl CoA carboxylase inhibitors reduce tissue malonyl CoA concentrations, inhibit fatty acid synthesis and increase fatty acid oxidation in cultured cells and in experimental animals
    • H.J. Harwood Jr., S.F. Petras, L.D. Shelly, L.M. Zaccaro, D.A. Perry, and M.R. Makowski Isozyme-nonselective N-substituted bipiperidylcarboxamide acetyl CoA carboxylase inhibitors reduce tissue malonyl CoA concentrations, inhibit fatty acid synthesis and increase fatty acid oxidation in cultured cells and in experimental animals J Biol Chem 278 2003 37099 37111
    • (2003) J Biol Chem , vol.278 , pp. 37099-37111
    • Harwood Jr., H.J.1    Petras, S.F.2    Shelly, L.D.3    Zaccaro, L.M.4    Perry, D.A.5    Makowski, M.R.6
  • 14
    • 66349099340 scopus 로고    scopus 로고
    • Fatty acid metabolism: Target for metabolic syndrome
    • S.J. Wakil, and L.A. Abu-Elheiga Fatty acid metabolism: target for metabolic syndrome J Lipid Res 50 Suppl. 2009 S138 S143
    • (2009) J Lipid Res , vol.50 , Issue.SUPPL.
    • Wakil, S.J.1    Abu-Elheiga, L.A.2
  • 15
    • 50949087166 scopus 로고    scopus 로고
    • Malonyl-CoA key signaling molecule in mammalian cells
    • D. Saggerson Malonyl-CoA key signaling molecule in mammalian cells Annu Rev Nutr 28 2008 253 272
    • (2008) Annu Rev Nutr , vol.28 , pp. 253-272
    • Saggerson, D.1
  • 16
    • 36049029132 scopus 로고    scopus 로고
    • A novel acetyl CoA carboxylase inhibitor reduces de novo fatty acid synthesis in HepG2 cells and rat primary hepatocytes
    • Y. Sugimoto, Y. Naniwa, T. Nakamura, H. Kato, M. Yamamato, and H. Tanabe A novel acetyl CoA carboxylase inhibitor reduces de novo fatty acid synthesis in HepG2 cells and rat primary hepatocytes Arch Biochem Biophys 468 2007 44 48
    • (2007) Arch Biochem Biophys , vol.468 , pp. 44-48
    • Sugimoto, Y.1    Naniwa, Y.2    Nakamura, T.3    Kato, H.4    Yamamato, M.5    Tanabe, H.6
  • 17
    • 33751579134 scopus 로고    scopus 로고
    • Acetyl CoA carboxylase: Versitile targets for drug discovery
    • L Tong, and H.J. Harwood Jr. Acetyl CoA carboxylase: versitile targets for drug discovery J Cell Biochem 99 2006 1476 1488
    • (2006) J Cell Biochem , vol.99 , pp. 1476-1488
    • Tong, L.1    Harwood Jr., H.J.2
  • 18
    • 0026544667 scopus 로고
    • The fatty acid chain elongation system of mammalian endoplasmic reticulum
    • D.L. Cinti, L. Cook, M.N. Nagi, and S.K. Suneja The fatty acid chain elongation system of mammalian endoplasmic reticulum Prog Lipid Res 31 1992 1 51
    • (1992) Prog Lipid Res , vol.31 , pp. 1-51
    • Cinti, D.L.1    Cook, L.2    Nagi, M.N.3    Suneja, S.K.4
  • 19
    • 33646018341 scopus 로고    scopus 로고
    • Fatty acid elongases in mammals: Their regulation and role in metabolism
    • A. Jakobsson, R. Westerberg, and A. Jacobsson Fatty acid elongases in mammals: their regulation and role in metabolism Prog Lipid Res 45 2006 237 249
    • (2006) Prog Lipid Res , vol.45 , pp. 237-249
    • Jakobsson, A.1    Westerberg, R.2    Jacobsson, A.3
  • 21
    • 34547947625 scopus 로고    scopus 로고
    • A molecular caliper mechanism for determining very long-chain fatty acid length
    • V. Denic, and J.S. Weissman A molecular caliper mechanism for determining very long-chain fatty acid length Cell 130 2007 663 677
    • (2007) Cell , vol.130 , pp. 663-677
    • Denic, V.1    Weissman, J.S.2
  • 22
    • 0037470063 scopus 로고    scopus 로고
    • Identification of two mammalian reductases involved in the two-carbon fatty acyl elongation cascade
    • Y.A. Moon, and J.D. Horton Identification of two mammalian reductases involved in the two-carbon fatty acyl elongation cascade J Biol Chem 278 2003 7335 7343
    • (2003) J Biol Chem , vol.278 , pp. 7335-7343
    • Moon, Y.A.1    Horton, J.D.2
  • 23
    • 0001819717 scopus 로고
    • Fatty acid desaturation and chain elongation in eukaryotes
    • Vance DE, Vance JE, editors chapter 6
    • Cook HW. Fatty acid desaturation and chain elongation in eucaryotes. In: Vance DE, Vance JE, editors. Biochemistry of lipids and membranes; 1985. p. 181-212 [chapter 6].
    • (1985) Biochemistry of Lipids and Membranes , pp. 181-212
    • Cook, H.W.1
  • 24
    • 33748744535 scopus 로고    scopus 로고
    • Regulation of hepatic fatty acid elongase and desaturase expression in diabetes and obesity
    • Y. Wang, D. Botolin, and J. Xu Regulation of hepatic fatty acid elongase and desaturase expression in diabetes and obesity J Lipid Res 47 2006 2028 2041
    • (2006) J Lipid Res , vol.47 , pp. 2028-2041
    • Wang, Y.1    Botolin, D.2    Xu, J.3
  • 25
    • 21744446895 scopus 로고    scopus 로고
    • Tissue-specific, nutritional, and developmental regulation of rat fatty acid elongases
    • Y. Wang, D. Botolin, and B. Christian Tissue-specific, nutritional, and developmental regulation of rat fatty acid elongases J Lipid Res 46 2005 706 715
    • (2005) J Lipid Res , vol.46 , pp. 706-715
    • Wang, Y.1    Botolin, D.2    Christian, B.3
  • 26
    • 0034958783 scopus 로고    scopus 로고
    • A lipogenic diet in mice with a disruption of the stearoyl-CoA desaturase 1 gene reveals a stringent requirement of endogenous monounsaturated fatty acids for triglyceride synthesis
    • M. Miyazaki, Y.C. Kim, and J.M. Ntambi A lipogenic diet in mice with a disruption of the stearoyl-CoA desaturase 1 gene reveals a stringent requirement of endogenous monounsaturated fatty acids for triglyceride synthesis J Lipid Res 42 2001 1018 1024
    • (2001) J Lipid Res , vol.42 , pp. 1018-1024
    • Miyazaki, M.1    Kim, Y.C.2    Ntambi, J.M.3
  • 27
    • 36448991861 scopus 로고    scopus 로고
    • Hepatic stearoyl-CoA desaturase-1 deficiency protects mice from carbohydrate-induced adiposity and hepatic steatosis
    • M. Miyazaki, M.T. Flowers, and H. Sampath Hepatic stearoyl-CoA desaturase-1 deficiency protects mice from carbohydrate-induced adiposity and hepatic steatosis Cell Metab 6 2007 484 496
    • (2007) Cell Metab , vol.6 , pp. 484-496
    • Miyazaki, M.1    Flowers, M.T.2    Sampath, H.3
  • 28
    • 34948904815 scopus 로고    scopus 로고
    • Crucial role of a long-chain fatty acid elongase, Elovl6, in obesity-induced insulin resistance
    • T. Matsuzaka, H. Shimano, and N. Yahagi Crucial role of a long-chain fatty acid elongase, Elovl6, in obesity-induced insulin resistance Nat Med 13 2007 1193 1202
    • (2007) Nat Med , vol.13 , pp. 1193-1202
    • Matsuzaka, T.1    Shimano, H.2    Yahagi, N.3
  • 29
    • 50949112066 scopus 로고    scopus 로고
    • Elevated hepatic fatty acid elongase-5 activity affects multiple pathways controlling hepatic lipid and carbohydrate composition
    • Y. Wang, M. Torres-Gonzalez, and S. Tripathy Elevated hepatic fatty acid elongase-5 activity affects multiple pathways controlling hepatic lipid and carbohydrate composition J Lipid Res 49 2008 1538 1552
    • (2008) J Lipid Res , vol.49 , pp. 1538-1552
    • Wang, Y.1    Torres-Gonzalez, M.2    Tripathy, S.3
  • 30
    • 64149083800 scopus 로고    scopus 로고
    • Deletion of ELOVL5 leads to fatty liver through activation of SREBP-1c in mice
    • Y.A. Moon, R.E. Hammer, and J.D. Horton Deletion of ELOVL5 leads to fatty liver through activation of SREBP-1c in mice J Lipid Res 50 2008 412 423
    • (2008) J Lipid Res , vol.50 , pp. 412-423
    • Moon, Y.A.1    Hammer, R.E.2    Horton, J.D.3
  • 31
    • 41849099558 scopus 로고    scopus 로고
    • Novel isolation prodedure for short, medium- and long-chain acyl-coenzyme A esters from tissue
    • P. Minkler, J. Kerner, S.T. Ingalls, and C.L. Hoppel Novel isolation prodedure for short, medium- and long-chain acyl-coenzyme A esters from tissue Anal Biochem 376 2008 275 276
    • (2008) Anal Biochem , vol.376 , pp. 275-276
    • Minkler, P.1    Kerner, J.2    Ingalls, S.T.3    Hoppel, C.L.4
  • 32
    • 0032532655 scopus 로고    scopus 로고
    • Pharmacological inhibitors of mammalian fatty acid synthase suppress DNA replication and induce apoptosis in tumor cell lines
    • E.S. Pizer, F.J. Chrest, J.A. DiGiuseppe, and W.F. Han Pharmacological inhibitors of mammalian fatty acid synthase suppress DNA replication and induce apoptosis in tumor cell lines Cancer Res 58 1998 4611 4615
    • (1998) Cancer Res , vol.58 , pp. 4611-4615
    • Pizer, E.S.1    Chrest, F.J.2    Digiuseppe, J.A.3    Han, W.F.4
  • 33
    • 0035816590 scopus 로고    scopus 로고
    • Expression and characterization of recombinant rat acyl-CoA synthetases 1, 4, and 5. Selective inhibition by triacsin C and thiazolidinediones
    • J.H. Kim, T.M. Lewin, and R.A. Coleman Expression and characterization of recombinant rat acyl-CoA synthetases 1, 4, and 5. Selective inhibition by triacsin C and thiazolidinediones J Biol Chem 276 2001 24667 24673
    • (2001) J Biol Chem , vol.276 , pp. 24667-24673
    • Kim, J.H.1    Lewin, T.M.2    Coleman, R.A.3
  • 34
    • 0028154083 scopus 로고
    • The soraphens: A family of novel antifungal compounds from Sorangium cellulosum (Myxobacteria). I. Soraphen A1 alpha: Fermentation, isolation, biological properties
    • K. Gerth, N. Bedorf, and H. Irschik The soraphens: a family of novel antifungal compounds from Sorangium cellulosum (Myxobacteria). I. Soraphen A1 alpha: fermentation, isolation, biological properties J Antibiot (Tokyo) 47 1994 23 31
    • (1994) J Antibiot (Tokyo) , vol.47 , pp. 23-31
    • Gerth, K.1    Bedorf, N.2    Irschik, H.3
  • 35
    • 0142164488 scopus 로고    scopus 로고
    • Myxobacteria: Proficient producers of novel natural products with various biological activities - Past and future biotechnological aspects with the focus on the genus Sorangium
    • K. Gerth, S. Pradella, and O. Perlova Myxobacteria: proficient producers of novel natural products with various biological activities - past and future biotechnological aspects with the focus on the genus Sorangium J Biotechnol 106 2003 233 253
    • (2003) J Biotechnol , vol.106 , pp. 233-253
    • Gerth, K.1    Pradella, S.2    Perlova, O.3
  • 36
    • 0028040134 scopus 로고
    • Identification of the yeast ACC1 gene product (acetyl-CoA carboxylase) as the target of the polyketide fungicide soraphen A
    • H.F. Vahlensieck, L. Pridzun, H. Reichenbach, and A. Hinnen Identification of the yeast ACC1 gene product (acetyl-CoA carboxylase) as the target of the polyketide fungicide soraphen A Curr Genet 25 1994 95 100
    • (1994) Curr Genet , vol.25 , pp. 95-100
    • Vahlensieck, H.F.1    Pridzun, L.2    Reichenbach, H.3    Hinnen, A.4
  • 37
    • 10944226843 scopus 로고    scopus 로고
    • A mechanism for the potent inhibition of eukaryotic acetyl-coenzyme A carboxylase by soraphen A, a macrocyclic polyketide natural product
    • Y. Shen, S.L. Volrath, and S.C. Weatherly A mechanism for the potent inhibition of eukaryotic acetyl-coenzyme A carboxylase by soraphen A, a macrocyclic polyketide natural product Mol Cell 16 2004 881 891
    • (2004) Mol Cell , vol.16 , pp. 881-891
    • Shen, Y.1    Volrath, S.L.2    Weatherly, S.C.3
  • 38
    • 72949114063 scopus 로고    scopus 로고
    • Molecular mechanism for the regulation of human ACC2 through phosphorylation by AMPK
    • Y.S. Cho, J.L. Lee, D. Shin, H.T. Kim, H.Y. Jung, and T.G. Lee Molecular mechanism for the regulation of human ACC2 through phosphorylation by AMPK Biochem Biophys Res Commun 391 2010 187 192
    • (2010) Biochem Biophys Res Commun , vol.391 , pp. 187-192
    • Cho, Y.S.1    Lee, J.L.2    Shin, D.3    Kim, H.T.4    Jung, H.Y.5    Lee, T.G.6
  • 39
    • 1542720382 scopus 로고    scopus 로고
    • Orlistat is a novel inhibitor of fatty acid synthase with antitumor activity
    • S.J. Kridel, F. Axelrod, N. Rozenkrantz, and J.W. Smith Orlistat is a novel inhibitor of fatty acid synthase with antitumor activity Cancer Res 64 2004 2070 2075
    • (2004) Cancer Res , vol.64 , pp. 2070-2075
    • Kridel, S.J.1    Axelrod, F.2    Rozenkrantz, N.3    Smith, J.W.4
  • 40
    • 0034650757 scopus 로고    scopus 로고
    • Malonyl-coenzyme-A is a potential mediator of cytotoxicity induced by fatty-acid synthase inhibition in human breast cancer cells and xenografts
    • E.S. Pizer, J. Thupari, and W.F. Han Malonyl-coenzyme-A is a potential mediator of cytotoxicity induced by fatty-acid synthase inhibition in human breast cancer cells and xenografts Cancer Res 60 2000 213 218
    • (2000) Cancer Res , vol.60 , pp. 213-218
    • Pizer, E.S.1    Thupari, J.2    Han, W.F.3
  • 41
    • 0035977004 scopus 로고    scopus 로고
    • Identification of a mammalian long chain fatty acyl elongase regulated by sterol regulatory element-binding proteins
    • Y.A. Moon, N.A. Shah, and S. Mohapatra Identification of a mammalian long chain fatty acyl elongase regulated by sterol regulatory element-binding proteins J Biol Chem 276 2001 45358 45366
    • (2001) J Biol Chem , vol.276 , pp. 45358-45366
    • Moon, Y.A.1    Shah, N.A.2    Mohapatra, S.3
  • 42
    • 67650549976 scopus 로고    scopus 로고
    • An alternate pathway to long chain polyunsaturates: The FADS2 gene product u8-desaturates 20:2n - 6 and 20:3n - 3
    • W.J. Park, K.S. Kothapalli, and P. Lawrence An alternate pathway to long chain polyunsaturates: The FADS2 gene product u8-desaturates 20:2n - 6 and 20:3n - 3 J Lipid Res 50 2009 1195 1202
    • (2009) J Lipid Res , vol.50 , pp. 1195-1202
    • Park, W.J.1    Kothapalli, K.S.2    Lawrence, P.3
  • 43
    • 48249146621 scopus 로고    scopus 로고
    • Fatty acid oxidation and insulin action: When less is more
    • D.M. Muoio, and C.B. Newgard Fatty acid oxidation and insulin action: when less is more Diabetes 57 2008 1455 1456
    • (2008) Diabetes , vol.57 , pp. 1455-1456
    • Muoio, D.M.1    Newgard, C.B.2
  • 44
    • 47949104798 scopus 로고    scopus 로고
    • The role of exercise and PGC1α in inflammation and chronic disease
    • C. Handschin, and B.M. Spiegelman The role of exercise and PGC1α in inflammation and chronic disease Nature 454 2008 463 469
    • (2008) Nature , vol.454 , pp. 463-469
    • Handschin, C.1    Spiegelman, B.M.2
  • 45
    • 38649110496 scopus 로고    scopus 로고
    • Hepatic insulin resistance is sufficient to produce dyslipidemia and susceptibility to atherosclerosis
    • S.B. Biddinger, A. Hernandez-Ono, and C. Rask-Madsen Hepatic insulin resistance is sufficient to produce dyslipidemia and susceptibility to atherosclerosis Cell Metab 7 2008 125 134
    • (2008) Cell Metab , vol.7 , pp. 125-134
    • Biddinger, S.B.1    Hernandez-Ono, A.2    Rask-Madsen, C.3
  • 46
    • 33645982255 scopus 로고    scopus 로고
    • From mice to men: Insights into the insulin resistance syndromes
    • S.B. Biddinger, and C.R. Kahn From mice to men: insights into the insulin resistance syndromes Annu Rev Physiol 68 2006 123 158
    • (2006) Annu Rev Physiol , vol.68 , pp. 123-158
    • Biddinger, S.B.1    Kahn, C.R.2
  • 47
    • 60149088480 scopus 로고    scopus 로고
    • From chronic overnutrition to insulin resistance: The role of fat-storing capacity and inflammation
    • L. Lionetti, M.P. Mollica, and A. Lombardi From chronic overnutrition to insulin resistance: the role of fat-storing capacity and inflammation Nutr Metab Cardiovasc Dis 19 2009 146 152
    • (2009) Nutr Metab Cardiovasc Dis , vol.19 , pp. 146-152
    • Lionetti, L.1    Mollica, M.P.2    Lombardi, A.3
  • 48
    • 69249205739 scopus 로고    scopus 로고
    • Obesity, inflammation, and atherosclerosis
    • V.Z. Rocha, and P. Libby Obesity, inflammation, and atherosclerosis Nat Rev Cardiol 6 2009 399 409
    • (2009) Nat Rev Cardiol , vol.6 , pp. 399-409
    • Rocha, V.Z.1    Libby, P.2
  • 49
    • 38749119359 scopus 로고    scopus 로고
    • Gene expression analysis in rats treated with experimental acetyl-coenzyme A carboxylase inhibitors suggests interactions with the peroxisome proliferator-activated receptor α pathway
    • J.F. Waring, Y. Yang, and C.H. Healan-Greenberg Gene expression analysis in rats treated with experimental acetyl-coenzyme A carboxylase inhibitors suggests interactions with the peroxisome proliferator-activated receptor α pathway J Pharmacol Exp Ther 324 2008 507 516
    • (2008) J Pharmacol Exp Ther , vol.324 , pp. 507-516
    • Waring, J.F.1    Yang, Y.2    Healan-Greenberg, C.H.3
  • 50
    • 33744808464 scopus 로고    scopus 로고
    • Acetyl-CoA carboxylase α is essential to breast cancer cell survival
    • V. Chajes, M. Cambot, and K. Moreau Acetyl-CoA carboxylase α is essential to breast cancer cell survival Cancer Res 66 2006 5287 5294
    • (2006) Cancer Res , vol.66 , pp. 5287-5294
    • Chajes, V.1    Cambot, M.2    Moreau, K.3
  • 51
    • 23044482013 scopus 로고    scopus 로고
    • RNA interference-mediated silencing of the acetyl-CoA-carboxylase-α gene induces growth inhibition and apoptosis of prostate cancer cells
    • K. Brusselmans, E. De Schrijver, G. Verhoeven, and J.V. Swinnen RNA interference-mediated silencing of the acetyl-CoA-carboxylase-α gene induces growth inhibition and apoptosis of prostate cancer cells Cancer Res 65 2005 6719 6725
    • (2005) Cancer Res , vol.65 , pp. 6719-6725
    • Brusselmans, K.1    De Schrijver, E.2    Verhoeven, G.3    Swinnen, J.V.4
  • 52
    • 2642540877 scopus 로고    scopus 로고
    • Expression and characterization of recombinant fungal acetyl-CoA carboxylase and isolation of a soraphen-binding domain
    • S.C. Weatherly, S.L. Volrath, and T.D. Elich Expression and characterization of recombinant fungal acetyl-CoA carboxylase and isolation of a soraphen-binding domain Biochem J 380 2004 105 110
    • (2004) Biochem J , vol.380 , pp. 105-110
    • Weatherly, S.C.1    Volrath, S.L.2    Elich, T.D.3
  • 53
    • 43249114663 scopus 로고    scopus 로고
    • N-3 polyunsaturated fatty acid regulation of hepatic gene transcription
    • D.B. Jump N-3 polyunsaturated fatty acid regulation of hepatic gene transcription Curr Opin Lipidol 19 2008 242 247
    • (2008) Curr Opin Lipidol , vol.19 , pp. 242-247
    • Jump, D.B.1
  • 54
    • 57649221152 scopus 로고    scopus 로고
    • Inhibition of gluconeogenesis in primary hepatocytes by stromal cell-derived factor-1 (SDF-1) through a c-Src/Akt-dependent signaling pathway
    • H.Y. Liu, G.B. Wen, and J. Han Inhibition of gluconeogenesis in primary hepatocytes by stromal cell-derived factor-1 (SDF-1) through a c-Src/Akt-dependent signaling pathway J Biol Chem 283 2008 30642 30649
    • (2008) J Biol Chem , vol.283 , pp. 30642-30649
    • Liu, H.Y.1    Wen, G.B.2    Han, J.3
  • 55
    • 43049181895 scopus 로고    scopus 로고
    • Docosahexaenoic acid (DHA) and hepatic gene transcription
    • D.B. Jump, D. Botolin, and Y. Wang Docosahexaenoic acid (DHA) and hepatic gene transcription Chem Phys Lipids 153 2008 3 13
    • (2008) Chem Phys Lipids , vol.153 , pp. 3-13
    • Jump, D.B.1    Botolin, D.2    Wang, Y.3
  • 56
    • 3142753961 scopus 로고    scopus 로고
    • Structure, function, and dietary regulation of delta6, delta5, and delta9 desaturases
    • M.T. Nakamura, and T.Y. Nara Structure, function, and dietary regulation of delta6, delta5, and delta9 desaturases Annu Rev Nutr 24 2004 345 376
    • (2004) Annu Rev Nutr , vol.24 , pp. 345-376
    • Nakamura, M.T.1    Nara, T.Y.2
  • 58
    • 0033000889 scopus 로고    scopus 로고
    • Essentiality of fatty acids
    • A.A. Spector Essentiality of fatty acids Lipids 34 1999 S1 S4
    • (1999) Lipids , vol.34
    • Spector, A.A.1
  • 59
    • 2342509057 scopus 로고    scopus 로고
    • Hepatic expression of malonyl CoA decarboxylase reverses muscle, liver and whole animal insulin resistance
    • J. An, D.M. Muoio, M. Shiota, Y. Fujimoto, G.W. Cline, and G.I. Shulman Hepatic expression of malonyl CoA decarboxylase reverses muscle, liver and whole animal insulin resistance Nat Med 10 2004 268 274
    • (2004) Nat Med , vol.10 , pp. 268-274
    • An, J.1    Muoio, D.M.2    Shiota, M.3    Fujimoto, Y.4    Cline, G.W.5    Shulman, G.I.6
  • 60
    • 77956838705 scopus 로고    scopus 로고
    • Elevated hepatic fatty acid elongase-5 (Elovl5) activity corrects dietary fat induced hyperglycemia in obese C57BL/6J mice
    • S. Tripathy, M. Torres-Gonzalez, and D.B. Jump Elevated hepatic fatty acid elongase-5 (Elovl5) activity corrects dietary fat induced hyperglycemia in obese C57BL/6J mice J Lipid Res 51 2010 2642 2654
    • (2010) J Lipid Res , vol.51 , pp. 2642-2654
    • Tripathy, S.1    Torres-Gonzalez, M.2    Jump, D.B.3
  • 61
    • 0141592581 scopus 로고    scopus 로고
    • Unsaturated fatty acid regulation of peroxisome proliferator-activated receptor alpha activity in rat primary hepatocytes
    • A. Pawar, and D.B. Jump Unsaturated fatty acid regulation of peroxisome proliferator-activated receptor alpha activity in rat primary hepatocytes J Biol Chem 278 2003 35931 35939
    • (2003) J Biol Chem , vol.278 , pp. 35931-35939
    • Pawar, A.1    Jump, D.B.2
  • 62
    • 0034686664 scopus 로고    scopus 로고
    • Metabolism of highly unsaturated n - 3 and n - 6 fatty acids
    • H. Sprecher Metabolism of highly unsaturated n - 3 and n - 6 fatty acids Biochim Biophys Acta 1486 2000 219 231
    • (2000) Biochim Biophys Acta , vol.1486 , pp. 219-231
    • Sprecher, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.