메뉴 건너뛰기




Volumn 147, Issue 5, 2014, Pages 1084-1093

A GAPDH-mediated trans-nitrosylation pathway is required for feedback inhibition of bile salt synthesis in rat liver

Author keywords

Cholestasis; Cholesterol 7 Hydroxylase; Histone Deacetylase; Nitric Oxide

Indexed keywords

BILE SALT; CHOLESTEROL 7ALPHA MONOOXYGENASE; CHOLIC ACID; DITHIOTHREITOL; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HISTONE DEACETYLASE 2; MESSENGER RNA; N(G) NITROARGININE METHYL ESTER; NITRIC OXIDE; SIRTUIN 1; SMALL INTERFERING RNA; BILE ACID; CELL RECEPTOR; CHOLIC ACID DERIVATIVE; CYP7A1 PROTEIN, RAT; ENZYME INHIBITOR; HDAC2 PROTEIN, RAT; NITRIC OXIDE SYNTHASE; NUCLEAR RECEPTOR SUBFAMILY 0, GROUP B, MEMBER 2; SIRT1 PROTEIN, RAT;

EID: 84908291988     PISSN: 00165085     EISSN: 15280012     Source Type: Journal    
DOI: 10.1053/j.gastro.2014.07.030     Document Type: Article
Times cited : (21)

References (39)
  • 1
    • 0025000828 scopus 로고
    • Bile acid secretion, bile flow and biliary lipid secretion in humans
    • A.F. Hofmann Bile acid secretion, bile flow and biliary lipid secretion in humans Hepatology 12 1990 17S 25S
    • (1990) Hepatology , vol.12 , pp. 17S-25S
    • Hofmann, A.F.1
  • 3
    • 84858796689 scopus 로고    scopus 로고
    • Transcriptional integration of metabolism by the nuclear sterol-activated receptors LXR and FXR
    • A.C. Calkin, and P. Tontonoz Transcriptional integration of metabolism by the nuclear sterol-activated receptors LXR and FXR Nat Rev Mol Cell Biol 13 2012 213 224
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 213-224
    • Calkin, A.C.1    Tontonoz, P.2
  • 4
    • 0033636789 scopus 로고    scopus 로고
    • Molecular basis for feedback regulation of bile acid synthesis by nuclear receptors
    • T.T. Lu, M. Makishima, and J.J. Repa Molecular basis for feedback regulation of bile acid synthesis by nuclear receptors Mol Cell 6 2000 507 515
    • (2000) Mol Cell , vol.6 , pp. 507-515
    • Lu, T.T.1    Makishima, M.2    Repa, J.J.3
  • 5
    • 0036086427 scopus 로고    scopus 로고
    • Nuclear receptors. I. Nuclear receptors and bile acid homeostasis
    • B. Goodwin, and S.A. Kliewer Nuclear receptors. I. Nuclear receptors and bile acid homeostasis Am J Physiol Gastrointest Liver Physiol 282 2002 G926 G931
    • (2002) Am J Physiol Gastrointest Liver Physiol , vol.282 , pp. 926-G931
    • Goodwin, B.1    Kliewer, S.A.2
  • 6
    • 70349430938 scopus 로고    scopus 로고
    • Bile acids: Regulation of synthesis
    • J.Y.L. Chiang Bile acids: regulation of synthesis J Lipid Res 50 2009 1955 1966
    • (2009) J Lipid Res , vol.50 , pp. 1955-1966
    • Chiang, J.Y.L.1
  • 7
    • 33846910174 scopus 로고    scopus 로고
    • Coordinated recruitment of histone methyltransferase G9a and other chromatin-modifying enzymes in SHP-mediated regulation of hepatic bile acid metabolism
    • S. Fang, J. Miao, and L. Xiang Coordinated recruitment of histone methyltransferase G9a and other chromatin-modifying enzymes in SHP-mediated regulation of hepatic bile acid metabolism Mol Cell Biol 27 2007 1407 1424
    • (2007) Mol Cell Biol , vol.27 , pp. 1407-1424
    • Fang, S.1    Miao, J.2    Xiang, L.3
  • 8
    • 17644363708 scopus 로고    scopus 로고
    • SHP represses transcriptional activity via recruitment of histone deacetylases
    • J. Gobinet, S. Carascossa, and V. Cavailles SHP represses transcriptional activity via recruitment of histone deacetylases Biochemistry 44 2005 6312 6320
    • (2005) Biochemistry , vol.44 , pp. 6312-6320
    • Gobinet, J.1    Carascossa, S.2    Cavailles, V.3
  • 9
    • 77955666599 scopus 로고    scopus 로고
    • Biliary secretion of S-nitrosoglutathione is involved in the hypercholeresis induced by ursodeoxycholic acid in the normal rat
    • C.M. Rodríguez-Ortigosa, J.M. Banales, and I. Olivas Biliary secretion of S-nitrosoglutathione is involved in the hypercholeresis induced by ursodeoxycholic acid in the normal rat Hepatology 52 2010 667 677
    • (2010) Hepatology , vol.52 , pp. 667-677
    • Rodríguez-Ortigosa, C.M.1    Banales, J.M.2    Olivas, I.3
  • 10
    • 0032563283 scopus 로고    scopus 로고
    • Diffusion-limited reaction of free nitric oxide with erythrocytes
    • X. Liu, M.J.S. Miller, and M.S. Joshi Diffusion-limited reaction of free nitric oxide with erythrocytes J Biol Chem 273 1998 18709 18713
    • (1998) J Biol Chem , vol.273 , pp. 18709-18713
    • Liu, X.1    Miller, M.J.S.2    Joshi, M.S.3
  • 11
    • 0026586147 scopus 로고
    • S-nitrosylation of proteins with nitric oxide: Synthesis and characterization of biologically active compounds
    • J.S. Stamler, D.I. Simon, and J.A. Osborne S-nitrosylation of proteins with nitric oxide: synthesis and characterization of biologically active compounds Proc Natl Acad Sci U S A 89 1992 444 448
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 444-448
    • Stamler, J.S.1    Simon, D.I.2    Osborne, J.A.3
  • 12
    • 0035252076 scopus 로고    scopus 로고
    • Export by red blood cells of nitric oxide bioactivity
    • J.R. Pawloski, D.T. Hess, and J.S. Stamler Export by red blood cells of nitric oxide bioactivity Nature 409 2001 622 626
    • (2001) Nature , vol.409 , pp. 622-626
    • Pawloski, J.R.1    Hess, D.T.2    Stamler, J.S.3
  • 13
  • 14
    • 78149284226 scopus 로고    scopus 로고
    • GAPDH mediates nitrosylation of nuclear proteins
    • M.D. Kornberg, N. Sen, and M.R. Hara GAPDH mediates nitrosylation of nuclear proteins Nat Cell Biol 12 2010 1094 1100
    • (2010) Nat Cell Biol , vol.12 , pp. 1094-1100
    • Kornberg, M.D.1    Sen, N.2    Hara, M.R.3
  • 15
    • 84862556342 scopus 로고    scopus 로고
    • Enzymatic mechanisms regulating protein S-nitrosylation: Implications in health and disease
    • P. Anand, and J.S. Stamler Enzymatic mechanisms regulating protein S-nitrosylation: implications in health and disease J Mol Med (Berl) 90 2012 233 244
    • (2012) J Mol Med (Berl) , vol.90 , pp. 233-244
    • Anand, P.1    Stamler, J.S.2
  • 16
    • 13444282230 scopus 로고    scopus 로고
    • Protein S-nitrosylation: Purview and parameters
    • D.T. Hess, A. Matsumoto, and S.-O. Kim Protein S-nitrosylation: purview and parameters Nature 6 2005 150 166
    • (2005) Nature , vol.6 , pp. 150-166
    • Hess, D.T.1    Matsumoto, A.2    Kim, S.-O.3
  • 17
    • 70049083635 scopus 로고    scopus 로고
    • Protein S-nitrosylation in health and disease: A current perspective
    • M.W. Foster, D.T. Hess, and J.S. Stamler Protein S-nitrosylation in health and disease: a current perspective Trends Mol Med 15 2009 391 404
    • (2009) Trends Mol Med , vol.15 , pp. 391-404
    • Foster, M.W.1    Hess, D.T.2    Stamler, J.S.3
  • 18
    • 70349466515 scopus 로고    scopus 로고
    • Protein denitrosylation: Enzymatic mechanisms and cellular functions
    • M. Benhar, M.T. Forrester, and J.S. Stamler Protein denitrosylation: enzymatic mechanisms and cellular functions Nat Rev Mol Cell Biol 10 2009 721 732
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 721-732
    • Benhar, M.1    Forrester, M.T.2    Stamler, J.S.3
  • 19
    • 80052483609 scopus 로고    scopus 로고
    • Host S-nitrosylation inhibits clostridial small molecule-activated glucosylating toxins
    • T.C. Savidge, P. Urvil, and N. Oezguen Host S-nitrosylation inhibits clostridial small molecule-activated glucosylating toxins Nat Med 17 2011 1136 1141
    • (2011) Nat Med , vol.17 , pp. 1136-1141
    • Savidge, T.C.1    Urvil, P.2    Oezguen, N.3
  • 20
    • 79959226194 scopus 로고    scopus 로고
    • On the functional diversity of glyceraldehyde-3-phosphate dehydrogenase: Biochemical mechanisms and regulatory control
    • M.A. Sirover On the functional diversity of glyceraldehyde-3-phosphate dehydrogenase: biochemical mechanisms and regulatory control Biochim Biophys Acta 1810 2011 741 751
    • (2011) Biochim Biophys Acta , vol.1810 , pp. 741-751
    • Sirover, M.A.1
  • 21
    • 22144477159 scopus 로고    scopus 로고
    • S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding
    • M.R. Hara, N. Agrawal, and S.F. Kim S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding Nat Cell Biol 7 2005 665 674
    • (2005) Nat Cell Biol , vol.7 , pp. 665-674
    • Hara, M.R.1    Agrawal, N.2    Kim, S.F.3
  • 22
    • 33947383769 scopus 로고    scopus 로고
    • The G-protein coupled bile salt receptor TGR5 is expressed in liver sinusoidal endothelial cells
    • V. Keitel, R. Reinehr, and P. Gatsios The G-protein coupled bile salt receptor TGR5 is expressed in liver sinusoidal endothelial cells Hepatology 45 2007 695 704
    • (2007) Hepatology , vol.45 , pp. 695-704
    • Keitel, V.1    Reinehr, R.2    Gatsios, P.3
  • 23
    • 0035800772 scopus 로고    scopus 로고
    • Human bile salt export pump promoter is transactivated by the farnesoid X receptor/bile acid receptor
    • M. Ananthanarayanan, N. Balasubramaniyan, and M. Makishima Human bile salt export pump promoter is transactivated by the farnesoid X receptor/bile acid receptor J Biol Chem 276 2001 28857 28865
    • (2001) J Biol Chem , vol.276 , pp. 28857-28865
    • Ananthanarayanan, M.1    Balasubramaniyan, N.2    Makishima, M.3
  • 24
    • 12444301770 scopus 로고    scopus 로고
    • Role of nuclear bile acid receptor, FXR, in adaptive ABC transporter regulation by cholic and ursodeoxycholic acid in mouse liver, kidney and intestine
    • G. Zollner, P. Fickert, and A. Fuchsbichler Role of nuclear bile acid receptor, FXR, in adaptive ABC transporter regulation by cholic and ursodeoxycholic acid in mouse liver, kidney and intestine J Hepatol 39 2003 480 488
    • (2003) J Hepatol , vol.39 , pp. 480-488
    • Zollner, G.1    Fickert, P.2    Fuchsbichler, A.3
  • 25
    • 33644857006 scopus 로고    scopus 로고
    • Neuroprotection by pharmacologic blockade of the GAPDH death cascade
    • M.R. Hara, B. Thomas, and M.B. Cascio Neuroprotection by pharmacologic blockade of the GAPDH death cascade Proc Natl Acad Sci U S A 103 2006 3887 3889
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 3887-3889
    • Hara, M.R.1    Thomas, B.2    Cascio, M.B.3
  • 26
    • 62849091792 scopus 로고    scopus 로고
    • Intracellular glutathione mediates the denitrosylation of protein nitrosothiols in the rat spinal cord
    • J.M. Romero, and O.A. Bizzozero Intracellular glutathione mediates the denitrosylation of protein nitrosothiols in the rat spinal cord J Neurosci Res 87 2009 701 709
    • (2009) J Neurosci Res , vol.87 , pp. 701-709
    • Romero, J.M.1    Bizzozero, O.A.2
  • 27
    • 46649101876 scopus 로고    scopus 로고
    • Nitric oxide-induced nuclear GAPDH activates p300/CBP and mediates apoptosis
    • N. Sen, M.R. Hara, and M.D. Kornberg Nitric oxide-induced nuclear GAPDH activates p300/CBP and mediates apoptosis Nat Cell Biol 10 2008 866 873
    • (2008) Nat Cell Biol , vol.10 , pp. 866-873
    • Sen, N.1    Hara, M.R.2    Kornberg, M.D.3
  • 28
    • 0026012407 scopus 로고
    • Regulation of cholesterol and bile acid homoeostasis in bile-obstructed rats
    • S. Dueland, J. Reichen, and G.T. Everson Regulation of cholesterol and bile acid homoeostasis in bile-obstructed rats Biochem J 280 1991 373 377
    • (1991) Biochem J , vol.280 , pp. 373-377
    • Dueland, S.1    Reichen, J.2    Everson, G.T.3
  • 29
    • 0030249353 scopus 로고    scopus 로고
    • Bile acid synthesis and biliary hydrophobicity during obstructive jaundice in rats
    • T. Naito, S. Kuroki, and K. Chijiiwa Bile acid synthesis and biliary hydrophobicity during obstructive jaundice in rats J Surg Res 65 1996 70 76
    • (1996) J Surg Res , vol.65 , pp. 70-76
    • Naito, T.1    Kuroki, S.2    Chijiiwa, K.3
  • 30
    • 0042825756 scopus 로고    scopus 로고
    • Role of farnesoid X receptor in determining hepatic ABC transporter expression and liver injury in bile duct-ligated mice
    • M. Wagner, P. Fickert, and G. Zollner Role of farnesoid X receptor in determining hepatic ABC transporter expression and liver injury in bile duct-ligated mice Gastroenterology 125 2003 825 838
    • (2003) Gastroenterology , vol.125 , pp. 825-838
    • Wagner, M.1    Fickert, P.2    Zollner, G.3
  • 31
    • 65249104853 scopus 로고    scopus 로고
    • Bile acid signaling pathways increase stability of small heterodimer partner (SHP) by inhibiting ubiquitin-proteasomal degradation
    • J. Miao, Z. Xiao, and D. Kanamaluru Bile acid signaling pathways increase stability of small heterodimer partner (SHP) by inhibiting ubiquitin-proteasomal degradation Genes Dev 23 2009 986 996
    • (2009) Genes Dev , vol.23 , pp. 986-996
    • Miao, J.1    Xiao, Z.2    Kanamaluru, D.3
  • 32
    • 70449712602 scopus 로고    scopus 로고
    • Novel roles for GAPDH in cell death and carcinogenesis
    • A. Colell, D.R. Green, and J.-E. Ricci Novel roles for GAPDH in cell death and carcinogenesis Cell Death Differ 16 2009 1573 1581
    • (2009) Cell Death Differ , vol.16 , pp. 1573-1581
    • Colell, A.1    Green, D.R.2    Ricci, J.-E.3
  • 34
    • 78149239781 scopus 로고    scopus 로고
    • GAPDH regulates cellular heme insertion into inducible nitric oxide synthase
    • R. Chakravarti, K.S. Aulak, and P.L. Fox GAPDH regulates cellular heme insertion into inducible nitric oxide synthase Proc Natl Acad Sci 107 2010 18004 18009
    • (2010) Proc Natl Acad Sci , vol.107 , pp. 18004-18009
    • Chakravarti, R.1    Aulak, K.S.2    Fox, P.L.3
  • 35
    • 2442693140 scopus 로고    scopus 로고
    • Nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase: A role in high glucose-induced apoptosis in retinal Müller cells
    • L.L. Kusner, V.P. Sarthy, and S. Mohr Nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase: a role in high glucose-induced apoptosis in retinal Müller cells Invest Ophthalmol Vis Sci 45 2004 1553 1561
    • (2004) Invest Ophthalmol Vis Sci , vol.45 , pp. 1553-1561
    • Kusner, L.L.1    Sarthy, V.P.2    Mohr, S.3
  • 36
    • 65449177586 scopus 로고    scopus 로고
    • High expression of the bile salt-homeostatic hormone fibroblast growth factor 19 in the liver of patients with extrahepatic cholestasis
    • F.G. Schaap, N.A. van der Gaag, and D.J. Gouma High expression of the bile salt-homeostatic hormone fibroblast growth factor 19 in the liver of patients with extrahepatic cholestasis Hepatology 49 2009 1228 1235
    • (2009) Hepatology , vol.49 , pp. 1228-1235
    • Schaap, F.G.1    Van Der Gaag, N.A.2    Gouma, D.J.3
  • 37
    • 70350606061 scopus 로고    scopus 로고
    • FXR acetylation is normally dynamically regulated by p300 and SIRT1 but constitutively elevated in metabolic disease states
    • J.K. Kemper, Z. Xiao, B. Ponugoti, and J. Miao FXR acetylation is normally dynamically regulated by p300 and SIRT1 but constitutively elevated in metabolic disease states Cell Metab 10 2009 392 404
    • (2009) Cell Metab , vol.10 , pp. 392-404
    • Kemper, J.K.1    Xiao, Z.2    Ponugoti, B.3    Miao, J.4
  • 38
    • 35649000891 scopus 로고    scopus 로고
    • Functional interaction of hepatic nuclear factor-4 and peroxisome proliferator-activated receptor-γ coactivator 1α in CYP7A1 regulation is inhibited by a key lipogenic activator, sterol regulatory element-binding protein-1c
    • B. Ponugoti, S. Fang, and J.K. Kemper Functional interaction of hepatic nuclear factor-4 and peroxisome proliferator-activated receptor-γ coactivator 1α in CYP7A1 regulation is inhibited by a key lipogenic activator, sterol regulatory element-binding protein-1c Mol Endocrinol 21 2007 2698 2712
    • (2007) Mol Endocrinol , vol.21 , pp. 2698-2712
    • Ponugoti, B.1    Fang, S.2    Kemper, J.K.3
  • 39
    • 84876553118 scopus 로고    scopus 로고
    • Prox1 directly interacts with LSD1 and recruits the LSD1/NuRD complex to epigenetically co-repress CYP7A1 transcription
    • H. Ouyang, Y. Qin, and Y. Liu Prox1 directly interacts with LSD1 and recruits the LSD1/NuRD complex to epigenetically co-repress CYP7A1 transcription PLoS One 8 2013 e62192
    • (2013) PLoS One , vol.8 , pp. 62192
    • Ouyang, H.1    Qin, Y.2    Liu, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.