메뉴 건너뛰기




Volumn 27, Issue 2, 2012, Pages 486-493

Low hydrogen sulphide and chronic kidney disease: A dangerous liaison

Author keywords

chronic kidney disease; chronic kidney failure; cysteine; homocysteine; hydrogen sulphide

Indexed keywords

3 MERCAPTOPYRUVATE SULPHURTRANSFERASE; CYSTATHIONINE BETA SYNTHASE; CYSTATHIONINE GAMMA LYASE; HYDROGEN SULFIDE; TRANSFERASE; UNCLASSIFIED DRUG;

EID: 84856886249     PISSN: 09310509     EISSN: 14602385     Source Type: Journal    
DOI: 10.1093/ndt/gfr737     Document Type: Review
Times cited : (49)

References (61)
  • 1
    • 77749271091 scopus 로고    scopus 로고
    • Hydrogen sulfide as a gasotransmitter
    • Gadalla MM, Snyder SH. Hydrogen sulfide as a gasotransmitter. J Neurochem 2010; 113: 14-26
    • (2010) J Neurochem , vol.113 , pp. 14-26
    • Gadalla, M.M.1    Snyder, S.H.2
  • 2
    • 79961076132 scopus 로고    scopus 로고
    • The therapeutic potential of hydrogen sulfide: Separating hype from hope
    • Olson KR. The therapeutic potential of hydrogen sulfide: separating hype from hope. Am J Physiol Regul Integr Comp Physiol 2011; 301: R297-R312
    • (2011) Am J Physiol Regul Integr Comp Physiol , vol.301
    • Olson, K.R.1
  • 3
    • 54949084607 scopus 로고    scopus 로고
    • H2S as a physiologic vasorelaxant: Hypertension in mice with deletion of cystathionine gamma-lyase
    • Yang G, Wu L, Jiang B et al. H2S as a physiologic vasorelaxant: hypertension in mice with deletion of cystathionine gamma-lyase. Science 2008; 322: 587-590
    • (2008) Science , vol.322 , pp. 587-590
    • Yang, G.1    Wu, L.2    Jiang, B.3
  • 4
    • 70349750278 scopus 로고    scopus 로고
    • No facilitator required for membrane transport of hydrogen sulfide
    • Mathai JC, Missner A, Kugler P et al. No facilitator required for membrane transport of hydrogen sulfide. Proc Natl Acad Sci USA 2009; 106: 16633-16638
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 16633-16638
    • Mathai, J.C.1    Missner, A.2    Kugler, P.3
  • 5
    • 79959530805 scopus 로고    scopus 로고
    • The quantitative significance of the transsulfuration enzymes for H2S production in murine tissues
    • Kabil O, Vitvitski V, Xie P et al. The quantitative significance of the transsulfuration enzymes for H2S production in murine tissues. Antioxid Redox Signal 2011; 15: 363-372
    • (2011) Antioxid Redox Signal , vol.15 , pp. 363-372
    • Kabil, O.1    Vitvitski, V.2    Xie, P.3
  • 6
    • 79953175962 scopus 로고    scopus 로고
    • Production of H2S by 3-mercaptopyruvate sulphurtransferase
    • Tanizawa K. Production of H2S by 3-mercaptopyruvate sulphurtransferase. J Biochem 2011; 149: 357-359
    • (2011) J Biochem , vol.149 , pp. 357-359
    • Tanizawa, K.1
  • 7
    • 77954579286 scopus 로고    scopus 로고
    • The redox biochemistry of hydrogen sulfide
    • Kabil O, Banerjee R. The redox biochemistry of hydrogen sulfide. J Biol Chem 2010; 285: 21903-21907
    • (2010) J Biol Chem , vol.285 , pp. 21903-21907
    • Kabil, O.1    Banerjee, R.2
  • 8
    • 63049105151 scopus 로고    scopus 로고
    • Hydrogen sulfide and the vasculature: A novel vasculoprotective entity and regulator of nitric oxide bioavailability?
    • Whiteman M, Moore PK. Hydrogen sulfide and the vasculature: a novel vasculoprotective entity and regulator of nitric oxide bioavailability? J Cell Mol Med 2009; 13: 488-507
    • (2009) J Cell Mol Med , vol.13 , pp. 488-507
    • Whiteman, M.1    Moore, P.K.2
  • 9
    • 0032864302 scopus 로고    scopus 로고
    • Homocysteine metabolism in cardiovascular cells and tissues: Implications for hyperhomocysteinemia and cardiovascular disease
    • Chen P, Poddar R, Tipa EV et al. Homocysteine metabolism in cardiovascular cells and tissues: implications for hyperhomocysteinemia and cardiovascular disease. Adv Enzyme Regul 1999; 39: 93-109
    • (1999) Adv Enzyme Regul , vol.39 , pp. 93-109
    • Chen, P.1    Poddar, R.2    Tipa, E.V.3
  • 10
    • 10644254287 scopus 로고    scopus 로고
    • Production of the neuromodulator H2S by cystathionine ß-synthase via the condensation of cysteine and homocysteine
    • Chen X, Jhee K, Kruger WD. Production of the neuromodulator H2S by cystathionine ß-synthase via the condensation of cysteine and homocysteine. J Biol Chem 2004; 279: 52082-52086
    • (2004) J Biol Chem , vol.279 , pp. 52082-52086
    • Chen, X.1    Jhee, K.2    Kruger, W.D.3
  • 11
    • 66449109703 scopus 로고    scopus 로고
    • H2S biogenesis by human cystathionine c-lyase leads to the novel sulfur metabolites lanthionine and homolanthionine and is responsive to the grade of hyperhomocysteinemia
    • Chiku T, Padovani D, Zhu W et al. H2S biogenesis by human cystathionine c-lyase leads to the novel sulfur metabolites lanthionine and homolanthionine and is responsive to the grade of hyperhomocysteinemia. J Biol Chem 2009; 284: 11601-11612
    • (2009) J Biol Chem , vol.284 , pp. 11601-11612
    • Chiku, T.1    Padovani, D.2    Zhu, W.3
  • 12
    • 67651174552 scopus 로고    scopus 로고
    • Bile-acid-activated farnesoid X receptor regulates hydrogen sulfide production and hepatic microcirculation
    • Renga B, Mencarelli A, Migliorati M et al. Bile-acid-activated farnesoid X receptor regulates hydrogen sulfide production and hepatic microcirculation. World J Gastroenterol 2009; 15: 2097-2108
    • (2009) World J Gastroenterol , vol.15 , pp. 2097-2108
    • Renga, B.1    Mencarelli, A.2    Migliorati, M.3
  • 13
    • 70449686289 scopus 로고    scopus 로고
    • Vascular endothelium expresses 3-mercaptopyruvate sulfurtransferase and produces hydrogen sulfide
    • Shibuya N, Mikami Y, Kimura Y et al. Vascular endothelium expresses 3-mercaptopyruvate sulfurtransferase and produces hydrogen sulfide. J Biochem 2009; 146: 623-626
    • (2009) J Biochem , vol.146 , pp. 623-626
    • Shibuya, N.1    Mikami, Y.2    Kimura, Y.3
  • 14
    • 78651457395 scopus 로고    scopus 로고
    • Hydrogen sulfide: Its production, release and functions
    • Kimura H. Hydrogen sulfide: its production, release and functions. Amino Acids 2011; 41: 113-121
    • (2011) Amino Acids , vol.41 , pp. 113-121
    • Kimura, H.1
  • 16
    • 67849135882 scopus 로고    scopus 로고
    • Actions and interactions of nitric oxide, carbon monoxide and hydrogen sulphide in the cardiovascular system and in inflammation-a tale of three gases!
    • Li L, Hsu A, Moore PK. Actions and interactions of nitric oxide, carbon monoxide and hydrogen sulphide in the cardiovascular system and in inflammation-a tale of three gases!. Pharmacol Ther 2009; 123: 386-400
    • (2009) Pharmacol Ther , vol.123 , pp. 386-400
    • Li, L.1    Hsu, A.2    Moore, P.K.3
  • 17
    • 67649265267 scopus 로고    scopus 로고
    • Is hydrogen sulfide a circulating "gasotransmitter" in vertebrate blood?
    • Olson KR. Is hydrogen sulfide a circulating "gasotransmitter" in vertebrate blood? Biochim Biophys Acta 2009; 1787: 856-863
    • (2009) Biochim Biophys Acta , vol.1787 , pp. 856-863
    • Olson, K.R.1
  • 18
    • 79953246240 scopus 로고    scopus 로고
    • Measurement of plasma hydrogen sulfide in vivo and in vivo
    • Shen X, Pattillo CB, Pardue S et al. Measurement of plasma hydrogen sulfide in vivo and in vivo. Free Radic Biol Med 2011; 50: 1021-1031
    • (2011) Free Radic Biol Med , vol.50 , pp. 1021-1031
    • Shen, X.1    Pattillo, C.B.2    Pardue, S.3
  • 19
    • 74949103637 scopus 로고    scopus 로고
    • H2S signals through protein S-sulfhydration
    • Mustafa AK, Gadalla MM, Sen N et al. H2S signals through protein S-sulfhydration. Sci Signal 2009; 2: ra72
    • (2009) Sci Signal , vol.2
    • Mustafa, A.K.1    Gadalla, M.M.2    Sen, N.3
  • 20
    • 79959515287 scopus 로고    scopus 로고
    • Free and acid-labile hydrogen sulfide concentrations in mouse tissues: Anomalously high free hydrogen sulfide in aortic tissue
    • Levitt MD, Abdel-Rehim MS, Furne J. Free and acid-labile hydrogen sulfide concentrations in mouse tissues: anomalously high free hydrogen sulfide in aortic tissue. Antioxid Redox Signal 2011; 15: 373-378
    • (2011) Antioxid Redox Signal , vol.15 , pp. 373-378
    • Levitt, M.D.1    Abdel-Rehim, M.S.2    Furne, J.3
  • 21
    • 77957718685 scopus 로고    scopus 로고
    • Hydrogen sulfide is an endogenous inhibitor of phophodiesterase activity
    • Bucci M, Papapetropulos A, Vellecco V et al. Hydrogen sulfide is an endogenous inhibitor of phophodiesterase activity. Arterioscler Thromb Vasc Biol 2010; 30: 1998-2004
    • (2010) Arterioscler Thromb Vasc Biol , vol.30 , pp. 1998-2004
    • Bucci, M.1    Papapetropulos, A.2    Vellecco, V.3
  • 22
    • 77952743516 scopus 로고    scopus 로고
    • Endogenous hydrogen sulfide is involved in the pathogenesis of atherosclerosis
    • Qiao W, Chaoshu T, Hongfang J et al. Endogenous hydrogen sulfide is involved in the pathogenesis of atherosclerosis. Biochem Biophys Res Commun 2010; 396: 182-186
    • (2010) Biochem Biophys Res Commun , vol.396 , pp. 182-186
    • Qiao, W.1    Chaoshu, T.2    Hongfang, J.3
  • 23
    • 59449083925 scopus 로고    scopus 로고
    • Role of hydrogen sulfide in the development of atherosclerotic lesions in apolipoprotein e knockout mice
    • Wang Y, Zhao X, Jin H et al. Role of hydrogen sulfide in the development of atherosclerotic lesions in apolipoprotein E knockout mice. Arterioscler Thromb Vasc Biol 2008; 29: 173-179
    • (2008) Arterioscler Thromb Vasc Biol , vol.29 , pp. 173-179
    • Wang, Y.1    Zhao, X.2    Jin, H.3
  • 24
    • 9444263079 scopus 로고    scopus 로고
    • Hydrogen sulfide protects neurons from oxidative stress
    • Kimura Y, Kimura H. Hydrogen sulfide protects neurons from oxidative stress. FASEB J 2004; 18: 1165-1167
    • (2004) FASEB J , vol.18 , pp. 1165-1167
    • Kimura, Y.1    Kimura, H.2
  • 25
    • 2442499521 scopus 로고    scopus 로고
    • Endogenous hydrogen sulfide regulation of myocardial injury induced by isoproterenol
    • Geng B, Chang L, Pan C et al. Endogenous hydrogen sulfide regulation of myocardial injury induced by isoproterenol. Biochem Biophys Res Commun 2004; 318: 756-763
    • (2004) Biochem Biophys Res Commun , vol.318 , pp. 756-763
    • Geng, B.1    Chang, L.2    Pan, C.3
  • 26
    • 3343017187 scopus 로고    scopus 로고
    • The novel neuromodulator hydrogen sulfide: An endogenous peroxynitrite 'scavenger'?
    • Whiteman M, Armstrong JS, Chu SH et al. The novel neuromodulator hydrogen sulfide: an endogenous peroxynitrite 'scavenger'? J Neurochem 2004; 90: 765-768
    • (2004) J Neurochem , vol.90 , pp. 765-768
    • Whiteman, M.1    Armstrong, J.S.2    Chu, S.H.3
  • 27
    • 79960320543 scopus 로고    scopus 로고
    • Hydrogen sulfide protects against chemical hypoxia-induced cytotoxicity and inflammation in HaCaT cells through inhibition of ROS/NF-kB/COX-2 pathway
    • doi:10.1371/journal.pone.0021971
    • Yang C, Yang Z, Zhang M et al. Hydrogen sulfide protects against chemical hypoxia-induced cytotoxicity and inflammation in HaCaT cells through inhibition of ROS/NF-kB/COX-2 pathway. PLoS One 2011; 6: e21971. doi:10.1371/journal.pone. 0021971
    • (2011) PLoS One , vol.6
    • Yang, C.1    Yang, Z.2    Zhang, M.3
  • 28
    • 79955901952 scopus 로고    scopus 로고
    • Hydrogen sulfide attenuated tumor necrosis factor-a-induced inflammatory signaling and dysfunction in vascular endothelial cells
    • doi:10.1371/journal.pone.0019766
    • Pan LL, Liu XH, Gong QH et al. Hydrogen sulfide attenuated tumor necrosis factor-a-induced inflammatory signaling and dysfunction in vascular endothelial cells. PLoS One 2011; 6: e19766. doi:10.1371/journal.pone.0019766
    • (2011) PLoS One , vol.6
    • Pan, L.L.1    Liu, X.H.2    Gong, Q.H.3
  • 29
    • 76749132000 scopus 로고    scopus 로고
    • Hydrogen sulfide protects against ischemia-reperfusion injury in an in vitro model of cutaneous tissue transplantation
    • Henderson PW, Singh SP, Belkin D et al. Hydrogen sulfide protects against ischemia-reperfusion injury in an in vitro model of cutaneous tissue transplantation. J Surg Res 2010; 159: 451-455
    • (2010) J Surg Res , vol.159 , pp. 451-455
    • Henderson, P.W.1    Singh, S.P.2    Belkin, D.3
  • 30
    • 34848828558 scopus 로고    scopus 로고
    • Hydrogen sulfide attenuates myocardial ischemia-reperfusion injury by preservation of mitochondrial function
    • Elrod JW, Calvert JW, Morrison J et al. Hydrogen sulfide attenuates myocardial ischemia-reperfusion injury by preservation of mitochondrial function. Proc Natl Acad Sci USA 2007; 104: 15560-15565
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 15560-15565
    • Elrod, J.W.1    Calvert, J.W.2    Morrison, J.3
  • 31
    • 52049083691 scopus 로고    scopus 로고
    • Cardioprotective role of sodium thiosulfate on chronic heart failure by modulating endogenous H2S generation
    • Sen U, Vacek TP, Hughes WM et al. Cardioprotective role of sodium thiosulfate on chronic heart failure by modulating endogenous H2S generation. Pharmacology 2008; 82: 201-213
    • (2008) Pharmacology , vol.82 , pp. 201-213
    • Sen, U.1    Vacek, T.P.2    Hughes, W.M.3
  • 32
    • 0348111406 scopus 로고    scopus 로고
    • The possible role of hydrogen sulfide on the pathogenesis of spontaneous hypertension in rats
    • Yan H, Du J, Tang C. The possible role of hydrogen sulfide on the pathogenesis of spontaneous hypertension in rats. Biochem Biophys Res Commun 2004; 313: 22-27
    • (2004) Biochem Biophys Res Commun , vol.313 , pp. 22-27
    • Yan, H.1    Du, J.2    Tang, C.3
  • 33
    • 0035503695 scopus 로고    scopus 로고
    • The vasorelaxant effect of H2S as a novel endogenous gaseous KATP channel opener
    • Zhao W, Zhang J, Lu Y et al. The vasorelaxant effect of H2S as a novel endogenous gaseous KATP channel opener. EMBO J 2001; 20: 6008-6016
    • (2001) EMBO J , vol.20 , pp. 6008-6016
    • Zhao, W.1    Zhang, J.2    Lu, Y.3
  • 34
    • 79953035492 scopus 로고    scopus 로고
    • Hydrogen sulfide-a potent multichannel anti-arrythmic drug
    • Zhoung G. Hydrogen sulfide-a potent multichannel anti-arrythmic drug. J Cardiovasc Dis Res 2010; 1: 37-39
    • (2010) J Cardiovasc Dis Res , vol.1 , pp. 37-39
    • Zhoung, G.1
  • 35
    • 79958859576 scopus 로고    scopus 로고
    • Intermittent hypoxia in rats increases myogenic tone through loss of hydrogen sulfide activation of large-conductance Ca(21)-activated potassium channels
    • Jackson-Weaver O, Paredes DA, Gonzales Bosc LV et al. Intermittent hypoxia in rats increases myogenic tone through loss of hydrogen sulfide activation of large-conductance Ca(21)-activated potassium channels. Circ Res 2011; 108: 1439-1447
    • (2011) Circ Res , vol.108 , pp. 1439-1447
    • Jackson-Weaver, O.1    Paredes, D.A.2    Gonzales Bosc, L.V.3
  • 36
    • 34548104580 scopus 로고    scopus 로고
    • Changes of the new gaseous transmitter H2S in patients with coronary heart disease
    • Jiang HL, Wu HC, Li ZL et al. Changes of the new gaseous transmitter H2S in patients with coronary heart disease. Di Yi Jun Yi Da Xue Bao 2005; 25: 951-954
    • (2005) Di Yi Jun Yi da Xue Bao , vol.25 , pp. 951-954
    • Jiang, H.L.1    Wu, H.C.2    Li, Z.L.3
  • 37
    • 33947686073 scopus 로고    scopus 로고
    • Imbalance of endogenous homocysteine and hydrogen sulfide metabolic pathway in essential hypertensive children
    • Li C, Sumou I, Ya-guang D et al. Imbalance of endogenous homocysteine and hydrogen sulfide metabolic pathway in essential hypertensive children. Chin Med J (Engl) 2007; 120: 389-393
    • (2007) Chin Med J (Engl) , vol.120 , pp. 389-393
    • Li, C.1    Sumou, I.2    Ya-Guang, D.3
  • 38
    • 81855184659 scopus 로고    scopus 로고
    • 1,25-dihydroxyvitamin D(3) influences cellular homocysteine levels in murine preosteoblastic MC3T3-E1 cells by direct regulation of cystathionine b-synthase
    • doi: 10.1002/jbmr.493
    • Kriebitzsch C, Verlinden L, Eelen G et al. 1,25-dihydroxyvitamin D(3) influences cellular homocysteine levels in murine preosteoblastic MC3T3-E1 cells by direct regulation of cystathionine b-synthase. J Bone Miner Res 2011; doi: 10.1002/jbmr.493
    • (2011) J Bone Miner Res
    • Kriebitzsch, C.1    Verlinden, L.2    Eelen, G.3
  • 39
    • 71049167707 scopus 로고    scopus 로고
    • Hydrogen sulfide-generating pathways in haemodialysis patients: A study on relevant metabolites and transcriptional regulation of genes encoding for key enzymes
    • Perna AF, Luciano MG, Ingrosso D et al. Hydrogen sulfide-generating pathways in haemodialysis patients: a study on relevant metabolites and transcriptional regulation of genes encoding for key enzymes. Nephrol Dial Transplant 2009; 24: 3756-3763
    • (2009) Nephrol Dial Transplant , vol.24 , pp. 3756-3763
    • Perna, A.F.1    Luciano, M.G.2    Ingrosso, D.3
  • 40
    • 84856933273 scopus 로고    scopus 로고
    • Down-regulation of the renal and hepatic hydrogen sulfide (H2S) producing enzymes and capacity in chronic kidney disease
    • Aminzadeh M, Vaziri N. Down-regulation of the renal and hepatic hydrogen sulfide (H2S) producing enzymes and capacity in chronic kidney disease. Nephrol Dial Transplant 2012; 27: 498-504
    • (2012) Nephrol Dial Transplant , vol.27 , pp. 498-504
    • Aminzadeh, M.1    Vaziri, N.2
  • 41
    • 66749144844 scopus 로고    scopus 로고
    • Production and actions of hydrogen sulfide, a novel gaseous bioactive substance, in the kidneys
    • Xia M, Chen L, Muh RW et al. Production and actions of hydrogen sulfide, a novel gaseous bioactive substance, in the kidneys. J Exp Pharmacol Exp Ther 2009; 329: 1056-1062
    • (2009) J Exp Pharmacol Exp Ther , vol.329 , pp. 1056-1062
    • Xia, M.1    Chen, L.2    Muh, R.W.3
  • 42
    • 83655163852 scopus 로고    scopus 로고
    • Interdependency of cystathionine c-lyase and cystathionine b-synthase in hydrogen sulfide-induced blood pressure regulation in rats
    • doi:10.1038/ajh.2011.149
    • Roy A, Khan AH, Islam MT et al. Interdependency of cystathionine c-lyase and cystathionine b-synthase in hydrogen sulfide-induced blood pressure regulation in rats. Am J Hypertens 2011; doi:10.1038/ajh.2011.149
    • (2011) Am J Hypertens
    • Roy, A.1    Khan, A.H.2    Islam, M.T.3
  • 43
    • 77954920936 scopus 로고    scopus 로고
    • Hypoxia in the renal medulla: Implications for hydrogen sulfide signaling
    • Beltowski J. Hypoxia in the renal medulla: Implications for hydrogen sulfide signaling. J Pharmacol Exp Ther 2010; 334: 358-363
    • (2010) J Pharmacol Exp Ther , vol.334 , pp. 358-363
    • Beltowski, J.1
  • 44
    • 77952982977 scopus 로고    scopus 로고
    • Hydrogen sulfide inhibits plasma renin activity
    • Lu M, Liu Y, Goh HS et al. Hydrogen sulfide inhibits plasma renin activity. J Am Soc Nephrol 2010; 21: 993-1002
    • (2010) J Am Soc Nephrol , vol.21 , pp. 993-1002
    • Lu, M.1    Liu, Y.2    Goh, H.S.3
  • 45
    • 80052855735 scopus 로고    scopus 로고
    • Hydrogen sulfide inhibits the calcification and osteoblastic differentiation of vascular smooth muscle cells
    • doi:10.1038/ki.2011.212
    • Zavaczki E, Jeney V, Agarwal A et al. Hydrogen sulfide inhibits the calcification and osteoblastic differentiation of vascular smooth muscle cells. Kidney Int 2011; doi:10.1038/ki.2011.212
    • (2011) Kidney Int
    • Zavaczki, E.1    Jeney, V.2    Agarwal, A.3
  • 46
    • 68049105295 scopus 로고    scopus 로고
    • Hydrogen sulfide ameliorates hyperhomocysteinemia-associated chronic renal failure
    • Sen U, Basu P, Abe OA et al. Hydrogen sulfide ameliorates hyperhomocysteinemia-associated chronic renal failure. Am J Physiol Renal Physiol 2009; 297: F410-F419
    • (2009) Am J Physiol Renal Physiol , vol.297
    • Sen, U.1    Basu, P.2    Abe, O.A.3
  • 47
    • 77952260852 scopus 로고    scopus 로고
    • Hydrogen sulfide regulates homocysteine-mediated glomerulosclerosis
    • Sen U, Munjal C, Qipshidze N et al. Hydrogen sulfide regulates homocysteine-mediated glomerulosclerosis. Am J Nephrol 2010; 31: 442-455
    • (2010) Am J Nephrol , vol.31 , pp. 442-455
    • Sen, U.1    Munjal, C.2    Qipshidze, N.3
  • 48
    • 78651359752 scopus 로고    scopus 로고
    • Cystathionine b-synthase and cystathionine-c-lyase double gene transfer ameliorate homocysteinemediated mesangial inflammation through hydrogen sulfide generation
    • Sen U, Givvimani S, Abe OA et al. Cystathionine b-synthase and cystathionine-c-lyase double gene transfer ameliorate homocysteinemediated mesangial inflammation through hydrogen sulfide generation. Am J Physiol Cell Physiol 2011; 300: C155-C163
    • (2011) Am J Physiol Cell Physiol , vol.300
    • Sen, U.1    Givvimani, S.2    Abe, O.A.3
  • 49
    • 0038663165 scopus 로고    scopus 로고
    • Folate treatment and unbalanced methylation and changes of allelic expression induced by hyperhomocysteinaemia in patients with uraemia
    • Ingrosso D, Cimmino A, Perna AF et al. Folate treatment and unbalanced methylation and changes of allelic expression induced by hyperhomocysteinaemia in patients with uraemia. Lancet 2003; 361: 1693-1699
    • (2003) Lancet , vol.361 , pp. 1693-1699
    • Ingrosso, D.1    Cimmino, A.2    Perna, A.F.3
  • 50
    • 0028919731 scopus 로고
    • Mechanism of erythrocyte accumulation of methylation inhibitor S-adenosylhomocysteine in uremia
    • Perna AF, Ingrosso D, De Santo NG et al. Mechanism of erythrocyte accumulation of methylation inhibitor S-adenosylhomocysteine in uremia. Kidney Int 1995; 47: 247-253
    • (1995) Kidney Int , vol.47 , pp. 247-253
    • Perna, A.F.1    Ingrosso, D.2    De Santo, N.G.3
  • 51
    • 69249133748 scopus 로고    scopus 로고
    • Hyperhomocysteinemia in uremia-a red flag in a disrupted circuit
    • Perna AF, Ingrosso D, Violetti E et al. Hyperhomocysteinemia in uremia-a red flag in a disrupted circuit. Semin Dial 2009; 22: 351-356
    • (2009) Semin Dial , vol.22 , pp. 351-356
    • Perna, A.F.1    Ingrosso, D.2    Violetti, E.3
  • 52
    • 2942744586 scopus 로고    scopus 로고
    • Accumulation of cyanide and thiocyanate in hemodialysis patients
    • Hasuike Y, Nakanishi T, Moriguchi R et al. Accumulation of cyanide and thiocyanate in hemodialysis patients. Nephrol Dial Transplant 2004; 19: 1474-1479
    • (2004) Nephrol Dial Transplant , vol.19 , pp. 1474-1479
    • Hasuike, Y.1    Nakanishi, T.2    Moriguchi, R.3
  • 53
    • 43349084839 scopus 로고    scopus 로고
    • Hydrogen sulfide inhibits myocardial injury induced by homocysteine in rats
    • Chang L, Geng B, Yu F et al. Hydrogen sulfide inhibits myocardial injury induced by homocysteine in rats. Amino Acids 2008; 34: 573-585
    • (2008) Amino Acids , vol.34 , pp. 573-585
    • Chang, L.1    Geng, B.2    Yu, F.3
  • 54
    • 69249100078 scopus 로고    scopus 로고
    • The relative contributions of cystathionine b-synthase and c-cystathionase to H2S biogenesis via alternative trans-sulfuration reactions
    • Singh S, Padovani D, Leslie RA et al. The relative contributions of cystathionine b-synthase and c-cystathionase to H2S biogenesis via alternative trans-sulfuration reactions. J Biol Chem 2009; 284: 22457-22466
    • (2009) J Biol Chem , vol.284 , pp. 22457-22466
    • Singh, S.1    Padovani, D.2    Leslie, R.A.3
  • 55
    • 79551476925 scopus 로고    scopus 로고
    • Inhibition of hydrogen sulphide formation reduces cisplatin-induced renal damage
    • Della Coletta Francescato H, Cunha FQ, Costa RS et al. Inhibition of hydrogen sulphide formation reduces cisplatin-induced renal damage. Nephrol Dial Transplant 2011; 26: 479-488
    • (2011) Nephrol Dial Transplant , vol.26 , pp. 479-488
    • Della Coletta Francescato, H.1    Cunha, F.Q.2    Costa, R.S.3
  • 56
    • 82355186706 scopus 로고    scopus 로고
    • Role of endogenous hydrogen sulfide on renal damage induced by adriamycin injection
    • doi:10.1007/s00204-011-0717-y
    • Francescato HD, Marin EC, da Queiroz Cunha F et al. Role of endogenous hydrogen sulfide on renal damage induced by adriamycin injection. Arch Toxicol 2011; doi:10.1007/s00204-011-0717-y
    • (2011) Arch Toxicol
    • Francescato, H.D.1    Marin, E.C.2    Da Queiroz Cunha, F.3
  • 57
    • 77953298249 scopus 로고    scopus 로고
    • Ischemia/reperfusion reduces transcription factor SP1 mediated cystathionine b-synthase expression in the kidney
    • Wu N, Siow YL, Karmin O. Ischemia/reperfusion reduces transcription factor SP1 mediated cystathionine b-synthase expression in the kidney. J Biol Chem 2010; 285: 18225-18233
    • (2010) J Biol Chem , vol.285 , pp. 18225-18233
    • Wu, N.1    Siow, Y.L.2    Karmin, O.3
  • 58
    • 52649096364 scopus 로고    scopus 로고
    • Generation of endogenous hydrogen sulfide by cystathionine gamma-lyase limits renal ischemia/reperfusion injury and dysfunction
    • Tripatara P, Patel NSA, Collino M et al. Generation of endogenous hydrogen sulfide by cystathionine gamma-lyase limits renal ischemia/reperfusion injury and dysfunction. Lab Invest 2008; 88: 1038-1048
    • (2008) Lab Invest , vol.88 , pp. 1038-1048
    • Tripatara, P.1    Patel, N.S.A.2    Collino, M.3
  • 59
    • 60949098890 scopus 로고    scopus 로고
    • Characterization of cystathionine gamma-lyase/hydrogen sulfide pathway in ischemia/reperfusion injury of the mouse kidney: An in vivo study
    • Tripatara P, Patel NS, Brancaleone V et al. Characterization of cystathionine gamma-lyase/hydrogen sulfide pathway in ischemia/reperfusion injury of the mouse kidney: an in vivo study. Eur J Pharmacol 2009; 606: 205-209
    • (2009) Eur J Pharmacol , vol.606 , pp. 205-209
    • Tripatara, P.1    Patel, N.S.2    Brancaleone, V.3
  • 60
    • 69849111192 scopus 로고    scopus 로고
    • Hydrogen sulfideinduced hypometabolism prevents renal ischemia/reprfusion injury
    • Bos EM, Leuvenink HGD, Snijder PM et al. Hydrogen sulfideinduced hypometabolism prevents renal ischemia/reprfusion injury. J Am Soc Nephrol 2009; 20: 1901-1905
    • (2009) J Am Soc Nephrol , vol.20 , pp. 1901-1905
    • Bos, E.M.1    Leuvenink, H.G.D.2    Snijder, P.M.3
  • 61
    • 80155151891 scopus 로고    scopus 로고
    • Hydrogen sulfide increases after a single hemodialysis session
    • Perna AF, Sepe I, Lanza D et al. Hydrogen sulfide increases after a single hemodialysis session. Kidney Int 2011; 80: 1108-1109
    • (2011) Kidney Int , vol.80 , pp. 1108-1109
    • Perna, A.F.1    Sepe, I.2    Lanza, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.