메뉴 건너뛰기




Volumn 70, Issue 1, 2006, Pages 88-96

Inhibition of ceramide-redox signaling pathway blocks glomerular injury in hyperhomocysteinemic rats

Author keywords

End stage renal disease; Homocysteine; Kidney; Oxidative stress; Sphingolipid

Indexed keywords

APOCYNIN; CERAMIDE; GUANOSINE TRIPHOSPHATASE; HOMOCYSTEINE; MATRIX METALLOPROTEINASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SPHINGOLIPID; THERMOZYMOCIDIN; TISSUE INHIBITOR OF METALLOPROTEINASE 1;

EID: 33745711919     PISSN: 00852538     EISSN: 15231755     Source Type: Journal    
DOI: 10.1038/sj.ki.5001517     Document Type: Article
Times cited : (84)

References (42)
  • 1
    • 0030762686 scopus 로고    scopus 로고
    • Hyperhomocysteinemia in end-stage renal disease: Prevalence, etiology, and potential relationship to arteriosclerotic outcomes
    • Bostom AG, Lathrop L. Hyperhomocysteinemia in end-stage renal disease: prevalence, etiology, and potential relationship to arteriosclerotic outcomes. Kidney Int 1997; 52: 10-20.
    • (1997) Kidney Int , vol.52 , pp. 10-20
    • Bostom, A.G.1    Lathrop, L.2
  • 2
    • 0030929483 scopus 로고    scopus 로고
    • Hyperhomocysteinemia: Detection, risk assessment, and treatment
    • Dennis VW, Nurko S, Robinson K. Hyperhomocysteinemia: detection, risk assessment, and treatment. Curr Opin Nephrol Hypertens 1997; 6: 483-488.
    • (1997) Curr Opin Nephrol Hypertens , vol.6 , pp. 483-488
    • Dennis, V.W.1    Nurko, S.2    Robinson, K.3
  • 3
    • 33745730836 scopus 로고    scopus 로고
    • Homocysteinemia and vascular disease in end-stage renal in patients with chronic renal failure
    • Dennis VW, Robinson K. Homocysteinemia and vascular disease in end-stage renal in patients with chronic renal failure. Kidney Int 1997; 52: 495-502.
    • (1997) Kidney Int , vol.52 , pp. 495-502
    • Dennis, V.W.1    Robinson, K.2
  • 4
    • 0032916658 scopus 로고    scopus 로고
    • Homocysteine, a new crucial element in the pathogenesis of uremic cardiovascular complications
    • Perna AF, Ingrosso D, Castaldo P et al. Homocysteine, a new crucial element in the pathogenesis of uremic cardiovascular complications. Miner Electrolyte Metab 1999; 25: 95-99.
    • (1999) Miner Electrolyte Metab , vol.25 , pp. 95-99
    • Perna, A.F.1    Ingrosso, D.2    Castaldo, P.3
  • 5
    • 0028987132 scopus 로고
    • Hyperhomocystinemia and traditional cardiovascular disease risk factors in end-stage renal disease patients on dialysis: A case-control study
    • Bostom AG, Shemin D, Lapane KL et al. Hyperhomocystinemia and traditional cardiovascular disease risk factors in end-stage renal disease patients on dialysis: a case-control study. Atherosclerosis 1995; 114: 93-103.
    • (1995) Atherosclerosis , vol.114 , pp. 93-103
    • Bostom, A.G.1    Shemin, D.2    Lapane, K.L.3
  • 6
    • 0033980289 scopus 로고    scopus 로고
    • Serum total homocysteine and cardiovascular disease occurrence in chronic, stable renal transplant recipients: A prospective study
    • Ducloux D, Motte G, Challier B et al. Serum total homocysteine and cardiovascular disease occurrence in chronic, stable renal transplant recipients: a prospective study. J Am Soc Nephrol 2000; 11: 134-137.
    • (2000) J Am Soc Nephrol , vol.11 , pp. 134-137
    • Ducloux, D.1    Motte, G.2    Challier, B.3
  • 7
    • 0036175422 scopus 로고    scopus 로고
    • Implications of hyperhomocysteinemia in glomerular sclerosis in hypertension
    • Li N, Chen YF, Zou AP. Implications of hyperhomocysteinemia in glomerular sclerosis in hypertension. Hypertension 2002; 39: 443-448.
    • (2002) Hypertension , vol.39 , pp. 443-448
    • Li, N.1    Chen, Y.F.2    Zou, A.P.3
  • 9
    • 0027493344 scopus 로고
    • Chemical pathology of homocysteine. I atherogenesis. II Carcinogenesis and homocysteine thiolacton metabolism. III Cellular function and aging
    • McCully KS. Chemical pathology of homocysteine. I atherogenesis. II Carcinogenesis and homocysteine thiolacton metabolism. III Cellular function and aging. Ann Clin Lab Sci 1993; 23: 477-493.
    • (1993) Ann Clin Lab Sci , vol.23 , pp. 477-493
    • McCully, K.S.1
  • 10
    • 0025277817 scopus 로고
    • Atherosclerosis, serum cholesterol and the homocysteine theory: A study of 194 consecutive autopsies
    • McCully KS. Atherosclerosis, serum cholesterol and the homocysteine theory: a study of 194 consecutive autopsies. Am J Med Sci 1990; 299: 217-221.
    • (1990) Am J Med Sci , vol.299 , pp. 217-221
    • McCully, K.S.1
  • 11
    • 0029664555 scopus 로고    scopus 로고
    • Homocysteine antagonism of nitric oxide-related cytostasis in Salmonella typhimurium
    • De Groote MA, Testerman T, Xu Y et al. Homocysteine antagonism of nitric oxide-related cytostasis in Salmonella typhimurium. Science 1996; 272: 414-417.
    • (1996) Science , vol.272 , pp. 414-417
    • De Groote, M.A.1    Testerman, T.2    Xu, Y.3
  • 12
    • 0017197285 scopus 로고
    • Homocystine-induced arteriosclerosis. The role of endothelial cell injury and platelet response in its genesis
    • Harker LA, Ross R, Slichter SJ, Scott CR. Homocystine-induced arteriosclerosis. The role of endothelial cell injury and platelet response in its genesis. J Clin Invest 1976; 58: 731-741.
    • (1976) J Clin Invest , vol.58 , pp. 731-741
    • Harker, L.A.1    Ross, R.2    Slichter, S.J.3    Scott, C.R.4
  • 13
    • 0033554459 scopus 로고    scopus 로고
    • Role of oxidant stress in endothelial dysfunction produced by experimental hyperhomocyst(e) inemia in humans
    • Kanani PM, Sinkey CA, Browning RL et al. Role of oxidant stress in endothelial dysfunction produced by experimental hyperhomocyst(e) inemia in humans. Circulation 1999; 100: 1161-1168.
    • (1999) Circulation , vol.100 , pp. 1161-1168
    • Kanani, P.M.1    Sinkey, C.A.2    Browning, R.L.3
  • 14
    • 0037336095 scopus 로고    scopus 로고
    • Homocysteine enhances TIMP-1 expression and cell proliferation associated with NADH oxidase in rat mesangial cells
    • Yang ZZ, Zou AP. Homocysteine enhances TIMP-1 expression and cell proliferation associated with NADH oxidase in rat mesangial cells. Kidney Int 2003; 63: 1012-1020.
    • (2003) Kidney Int , vol.63 , pp. 1012-1020
    • Yang, Z.Z.1    Zou, A.P.2
  • 15
    • 21644461236 scopus 로고    scopus 로고
    • Homocysteine activate NADH/NADPH oxidase through ceramide-stimulated rac activity in rat mesangial cells
    • Yi F, Zhang AY, Janscha J et al. Homocysteine activate NADH/NADPH oxidase through ceramide-stimulated rac activity in rat mesangial cells. Kidney Int 2004; 66: 1977-1987.
    • (2004) Kidney Int , vol.66 , pp. 1977-1987
    • Yi, F.1    Zhang, A.Y.2    Janscha, J.3
  • 16
    • 0030755466 scopus 로고    scopus 로고
    • Tissue-specific pattern of stress kinase activation in ischemic/reperfused heart and kidney
    • Yin T, Sandhu G, Wolfgang CD et al. Tissue-specific pattern of stress kinase activation in ischemic/reperfused heart and kidney. J Biol Chem 1997; 272: 19943-19950.
    • (1997) J Biol Chem , vol.272 , pp. 19943-19950
    • Yin, T.1    Sandhu, G.2    Wolfgang, C.D.3
  • 17
    • 0031919843 scopus 로고    scopus 로고
    • Identification of caspase (ICE-like proteases) gene family in rat kidney and altered expression in ischemia/reperfusion injury
    • Kaushal GP, Singh AB, Shah SV. Identification of caspase (ICE-like proteases) gene family in rat kidney and altered expression in ischemia/reperfusion injury. Am J Physiol 1998; 274: F587-F595.
    • (1998) Am J Physiol , vol.274
    • Kaushal, G.P.1    Singh, A.B.2    Shah, S.V.3
  • 18
    • 0034175876 scopus 로고    scopus 로고
    • Apoptotic mechanisms in acute renal failure
    • Ueda N, Kaushal GP, Shah SV. Apoptotic mechanisms in acute renal failure. Am J Med 2000; 108: 403-415.
    • (2000) Am J Med , vol.108 , pp. 403-415
    • Ueda, N.1    Kaushal, G.P.2    Shah, S.V.3
  • 19
    • 0037306287 scopus 로고    scopus 로고
    • Ceramide-induced activation of NADPH oxidase and endothelial dysfunction in small coronary arteries
    • Zhang DX, Zou AP, Li PL. Ceramide-induced activation of NADPH oxidase and endothelial dysfunction in small coronary arteries. Am J Physiol Heart Circ Physiol 2003; 284: H605-H612.
    • (2003) Am J Physiol Heart Circ Physiol , vol.284
    • Zhang, D.X.1    Zou, A.P.2    Li, P.L.3
  • 20
    • 0033670837 scopus 로고    scopus 로고
    • Increased uracil misincorporation in lymphocytes from folate-deficient rats
    • Duthie SJ, Grant G, Narayanan S. Increased uracil misincorporation in lymphocytes from folate-deficient rats. Br J Cancer 2000; 83: 1532-1537.
    • (2000) Br J Cancer , vol.83 , pp. 1532-1537
    • Duthie, S.J.1    Grant, G.2    Narayanan, S.3
  • 21
    • 0028347021 scopus 로고
    • Folate-deficiency-induced homocysteinaemia in rats: Disruption of S-adenosylmethionine's co-ordinate regulation of homocysteine metabolism
    • Miller JW, Nadeau MR, Smith J et al. Folate-deficiency-induced homocysteinaemia in rats: disruption of S-adenosylmethionine's co-ordinate regulation of homocysteine metabolism. Biochem J 1994; 298(Part 2): 415-419.
    • (1994) Biochem J , vol.298 , Issue.2 PART , pp. 415-419
    • Miller, J.W.1    Nadeau, M.R.2    Smith, J.3
  • 22
    • 0346787880 scopus 로고    scopus 로고
    • Chronic methionine load-induced hyperhomocysteinemia enhances rat carotid responsiveness for angiotensin II
    • Bonaventura D, Tirapelli CR, Haddad R et al. Chronic methionine load-induced hyperhomocysteinemia enhances rat carotid responsiveness for angiotensin II. Pharmacology 2004; 70: 91-99.
    • (2004) Pharmacology , vol.70 , pp. 91-99
    • Bonaventura, D.1    Tirapelli, C.R.2    Haddad, R.3
  • 23
    • 17944373383 scopus 로고    scopus 로고
    • Ceramide generation by two distinct pathways in tumor necrosis factor alpha-induced cell death
    • Dbaibo GS, El-Assaad W, Krikorian A et al. Ceramide generation by two distinct pathways in tumor necrosis factor alpha-induced cell death. FEBS Lett 2001; 503: 7-12.
    • (2001) FEBS Lett , vol.503 , pp. 7-12
    • Dbaibo, G.S.1    El-Assaad, W.2    Krikorian, A.3
  • 24
    • 0033485457 scopus 로고    scopus 로고
    • Responses of vascular smooth muscle cell to extracellular matrix degradation
    • Tummalapalli CM, Tyagi SC. Responses of vascular smooth muscle cell to extracellular matrix degradation. J Cell Biochem 1999; 75: 515-527.
    • (1999) J Cell Biochem , vol.75 , pp. 515-527
    • Tummalapalli, C.M.1    Tyagi, S.C.2
  • 25
    • 0031756278 scopus 로고    scopus 로고
    • Relevance of extracellular matrix, its receptors, and cell adhesion molecules in mammalian nephrogenesis
    • Wallner EI, Yang Q, Peterson DR et al. Relevance of extracellular matrix, its receptors, and cell adhesion molecules in mammalian nephrogenesis. Am J Physiol Renal Physiol 1998; 275: F467-F477.
    • (1998) Am J Physiol Renal Physiol , vol.275
    • Wallner, E.I.1    Yang, Q.2    Peterson, D.R.3
  • 26
    • 0030847461 scopus 로고    scopus 로고
    • Differential regulation of glomerular gelatinase B (MMP-9) and tissue inhibitor of metalloproteinase-1 (TIMP-1) in obese Zucker rats
    • Schaefer L, Han X, August C et al. Differential regulation of glomerular gelatinase B (MMP-9) and tissue inhibitor of metalloproteinase-1 (TIMP-1) in obese Zucker rats. Diabetologia 1997; 40: 1035-1043.
    • (1997) Diabetologia , vol.40 , pp. 1035-1043
    • Schaefer, L.1    Han, X.2    August, C.3
  • 27
    • 0345035265 scopus 로고    scopus 로고
    • Induction of TIMP-1 expression in rat hepatic stellate cells and hepatocytes: A new role for homocysteine in liver fibrosis
    • Torres L, Garcia-Trevijiano ER, Rodriguez JA et al. Induction of TIMP-1 expression in rat hepatic stellate cells and hepatocytes: a new role for homocysteine in liver fibrosis. Biochim Biophys Acta 1999; 1455: 12-22.
    • (1999) Biochim Biophys Acta , vol.1455 , pp. 12-22
    • Torres, L.1    Garcia-Trevijiano, E.R.2    Rodriguez, J.A.3
  • 28
    • 0041842627 scopus 로고    scopus 로고
    • Cytoskeletal rearrangement and signal transduction in TGF-beta1-stimulated mesangial cell collagen accumulation
    • Hubchak SC, Runyan CE, Kreisberg JI, Schnaper HW. Cytoskeletal rearrangement and signal transduction in TGF-beta1-stimulated mesangial cell collagen accumulation. J Am Soc Nephrol 2003; 14: 1969-1980.
    • (2003) J Am Soc Nephrol , vol.14 , pp. 1969-1980
    • Hubchak, S.C.1    Runyan, C.E.2    Kreisberg, J.I.3    Schnaper, H.W.4
  • 29
    • 0029299438 scopus 로고
    • The response-to-retention hypothesis of early atherogenesis
    • Williams KJ, Tabas I. The response-to-retention hypothesis of early atherogenesis. Arterioscler Thromb Vasc Biol 1995; 15: 551-561.
    • (1995) Arterioscler Thromb Vasc Biol , vol.15 , pp. 551-561
    • Williams, K.J.1    Tabas, I.2
  • 30
    • 0028848344 scopus 로고
    • Differential regulation of sphingomyelinase and ceramidase activities by growth factors and cytokines
    • Coroneos E, Martinez M, McKenna S, Kester M. Differential regulation of sphingomyelinase and ceramidase activities by growth factors and cytokines. J Biol Chem 1995; 270: 23305-23309.
    • (1995) J Biol Chem , vol.270 , pp. 23305-23309
    • Coroneos, E.1    Martinez, M.2    McKenna, S.3    Kester, M.4
  • 31
    • 15444367538 scopus 로고    scopus 로고
    • Effect of myriocin on plasma sphingolipid metabolism and atherosclerosis in apoE-deficient mice
    • Hojjati MR, Li Z, Zhou H et al. Effect of myriocin on plasma sphingolipid metabolism and atherosclerosis in apoE-deficient mice. J Biol Chem 2005; 280: 10284-10289.
    • (2005) J Biol Chem , vol.280 , pp. 10284-10289
    • Hojjati, M.R.1    Li, Z.2    Zhou, H.3
  • 32
    • 20844435949 scopus 로고    scopus 로고
    • Inhibition of sphingomyelin synthesis reduces atherogenesis in apolipoprotein E-knockout mice
    • Park TS, Panek RL, Mueller SB et al. Inhibition of sphingomyelin synthesis reduces atherogenesis in apolipoprotein E-knockout mice. Circulation 2005; 110: 34665-34671.
    • (2005) Circulation , vol.110 , pp. 34665-34671
    • Park, T.S.1    Panek, R.L.2    Mueller, S.B.3
  • 33
    • 0037399439 scopus 로고    scopus 로고
    • Oxidation of tetrahydrobiopterin leads to uncoupling of endothelial cell nitric oxide synthase in hypertension
    • Landmesser S, Dikalov SR, Price L et al. Oxidation of tetrahydrobiopterin leads to uncoupling of endothelial cell nitric oxide synthase in hypertension. J Clin Invest 2003; 111: 1201-1209.
    • (2003) J Clin Invest , vol.111 , pp. 1201-1209
    • Landmesser, S.1    Dikalov, S.R.2    Price, L.3
  • 34
    • 0042379916 scopus 로고    scopus 로고
    • The vascular NAD(P)H oxidases as therapeutic targets in cardiovascular diseases
    • Cai H, Griendling KK, Harrison DG. The vascular NAD(P)H oxidases as therapeutic targets in cardiovascular diseases. Trends Pharmacol Sci 2003; 24: 471-478.
    • (2003) Trends Pharmacol Sci , vol.24 , pp. 471-478
    • Cai, H.1    Griendling, K.K.2    Harrison, D.G.3
  • 35
    • 0033781454 scopus 로고    scopus 로고
    • Modulation of protein kinase activity and gene expression by reactive oxygen species and their role in vascular physiology and pathophysiology
    • Griendling KK, Sorescu D, Lassegue B, Ushio-Fukai M. Modulation of protein kinase activity and gene expression by reactive oxygen species and their role in vascular physiology and pathophysiology. Arteriosder Thromb Vasc Biol 2000; 20: 2175-2183.
    • (2000) Arteriosder Thromb Vasc Biol , vol.20 , pp. 2175-2183
    • Griendling, K.K.1    Sorescu, D.2    Lassegue, B.3    Ushio-Fukai, M.4
  • 36
    • 0042991381 scopus 로고    scopus 로고
    • Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases
    • Takeya RN, Ueno K, Kami M et al. Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases. J Biol Chem 2003; 278: 25234-25246.
    • (2003) J Biol Chem , vol.278 , pp. 25234-25246
    • Takeya, R.N.1    Ueno, K.2    Kami, M.3
  • 37
    • 11144338749 scopus 로고    scopus 로고
    • Vascular NADPH oxidases: Molecular mechanisms of activation
    • Brandes RP, Kreuzer J. Vascular NADPH oxidases: molecular mechanisms of activation. Cardiovasc Res 2005; 65: 16-27.
    • (2005) Cardiovasc Res , vol.65 , pp. 16-27
    • Brandes, R.P.1    Kreuzer, J.2
  • 39
    • 0037108109 scopus 로고    scopus 로고
    • Current molecular models for NADPH oxidase regulation by Rac GTPase
    • Bokoch GM, Diebold BA. Current molecular models for NADPH oxidase regulation by Rac GTPase. Blood 2002; 100: 2692-2696.
    • (2002) Blood , vol.100 , pp. 2692-2696
    • Bokoch, G.M.1    Diebold, B.A.2
  • 40
    • 0025944684 scopus 로고
    • Activation of the NADPH oxidase involves the small GTP-binding protein p21rac1
    • Abo A, Pick E, Hall A et al. Activation of the NADPH oxidase involves the small GTP-binding protein p21rac1. Nature 1991; 353: 668-670.
    • (1991) Nature , vol.353 , pp. 668-670
    • Abo, A.1    Pick, E.2    Hall, A.3
  • 41
    • 0037015259 scopus 로고    scopus 로고
    • Effect of hyperhomocysteinemia on plasma or tissue adenosine levels and renal function
    • Chen YF, Li PL, Zou AP. Effect of hyperhomocysteinemia on plasma or tissue adenosine levels and renal function. Circulation 2002; 106: 1275-1281.
    • (2002) Circulation , vol.106 , pp. 1275-1281
    • Chen, Y.F.1    Li, P.L.2    Zou, A.P.3
  • 42
    • 0037040612 scopus 로고    scopus 로고
    • Separation, identification and quantitation of ceramides in human cancer cells by liquid chromatography-electrospray ionisation tandem mass spectrometry
    • Fillet M, Van Heugen JC, Servais AC et al. Separation, identification and quantitation of ceramides in human cancer cells by liquid chromatography- electrospray ionisation tandem mass spectrometry. J Chromatogr A 2002; 949: 225-233.
    • (2002) J Chromatogr A , vol.949 , pp. 225-233
    • Fillet, M.1    Van Heugen, J.C.2    Servais, A.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.