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Volumn 280, Issue 1 49-1, 2001, Pages

Cytochrome P-450 as a source of catalytic iron in minimal change nephrotic syndrome in rats

Author keywords

Cytochrome P 450 inhibitors; Glomerular epithelial cells; Puromycin aminonucleoside; Reactive oxygen metabolites

Indexed keywords

CIMETIDINE; CYTOCHROME P450; CYTOCHROME P450 INHIBITOR; HEMOPROTEIN; HYDROXYL RADICAL; IRON; PIPERONYL BUTOXIDE; PUROMYCIN AMINONUCLEOSIDE; REACTIVE OXYGEN METABOLITE;

EID: 0035000022     PISSN: 1931857X     EISSN: 15221466     Source Type: Journal    
DOI: 10.1152/ajprenal.2001.280.1.f88     Document Type: Article
Times cited : (20)

References (35)
  • 1
    • 0027264897 scopus 로고
    • Regulation of cytochrome P-450 isozymes by methylenedioxyphenyl compounds
    • Adams NH, Levi PE, and Hodgson E. Regulation of cytochrome P-450 isozymes by methylenedioxyphenyl compounds. Chem Biol Interact 86: 255-274, 1993.
    • (1993) Chem Biol Interact , vol.86 , pp. 255-274
    • Adams, N.H.1    Levi, P.E.2    Hodgson, E.3
  • 2
    • 0023547062 scopus 로고
    • Lack of inhibition of mouse catalase activity by cimetidine: An argument against a relevant general effect of cimetidine upon home metabolic pathways
    • Baird MB, Sfeir GT, and Slade-Pacini CD. Lack of inhibition of mouse catalase activity by cimetidine: an argument against a relevant general effect of cimetidine upon home metabolic pathways. Biochem Pharmacol 36: 4366-4369, 1987.
    • (1987) Biochem Pharmacol , vol.36 , pp. 4366-4369
    • Baird, M.B.1    Sfeir, G.T.2    Slade-Pacini, C.D.3
  • 4
    • 0027324385 scopus 로고
    • Increase in bleomycin-detectable iron in ischemia/reperfusion injury to rat kidneys
    • Baliga R, Ueda N, and Shah SV. Increase in bleomycin-detectable iron in ischemia/reperfusion injury to rat kidneys. Biochem J 291: 901-905, 1993.
    • (1993) Biochem J , vol.291 , pp. 901-905
    • Baliga, R.1    Ueda, N.2    Shah, S.V.3
  • 5
    • 0000926039 scopus 로고    scopus 로고
    • Oxidant mechanisms in glomerular disease
    • Chicago, IL: Year Book
    • Baliga R, Ueda N, and Shah SV. Oxidant mechanisms in glomerular disease. In: Current Nephrology. Chicago, IL: Year Book, 1997, vol. 20, p. 135-151.
    • (1997) Current Nephrology , vol.20 , pp. 135-151
    • Baliga, R.1    Ueda, N.2    Shah, S.V.3
  • 6
    • 0030033983 scopus 로고    scopus 로고
    • Evidence for cytochrome 450 as a source of catalytic iron in the myoglobinuric acute renal failure
    • Baliga R, Zhang Z, Baliga M, and Shah SV. Evidence for cytochrome 450 as a source of catalytic iron in the myoglobinuric acute renal failure. Kidney Int 49: 362-369, 1996.
    • (1996) Kidney Int , vol.49 , pp. 362-369
    • Baliga, R.1    Zhang, Z.2    Baliga, M.3    Shah, S.V.4
  • 7
    • 0031933285 scopus 로고    scopus 로고
    • In vitro and in vivo evidence suggesting a role for iron in cisplatin-induced nephrotoxicity
    • Baliga R, Zhang Z, Baliga M, Ueda N, and Shah SV. In vitro and in vivo evidence suggesting a role for iron in cisplatin-induced nephrotoxicity. Kidney Int 53: 394-401, 1998.
    • (1998) Kidney Int , vol.53 , pp. 394-401
    • Baliga, R.1    Zhang, Z.2    Baliga, M.3    Ueda, N.4    Shah, S.V.5
  • 8
    • 0031758531 scopus 로고    scopus 로고
    • Role of cytochrome P-450 as a source of catalytic iron in cisplatin-induced nephrotoxicity
    • Baliga R, Zhang Z, Baliga M, Ueda N, and Shah SV. Role of cytochrome P-450 as a source of catalytic iron in cisplatin-induced nephrotoxicity. Kidney Int 54: 1562-1569, 1998.
    • (1998) Kidney Int , vol.54 , pp. 1562-1569
    • Baliga, R.1    Zhang, Z.2    Baliga, M.3    Ueda, N.4    Shah, S.V.5
  • 11
  • 12
    • 0018533128 scopus 로고
    • The interaction of aliphatic analogs of methylenedioxyphenyl compounds with cytochromes P-450 and P-420
    • Dahl AR and Hodgson E. The interaction of aliphatic analogs of methylenedioxyphenyl compounds with cytochromes P-450 and P-420. Chem Biol Interact 27: 163-175, 1979.
    • (1979) Chem Biol Interact , vol.27 , pp. 163-175
    • Dahl, A.R.1    Hodgson, E.2
  • 15
    • 0019847498 scopus 로고
    • Superoxide-dependent formation of hydroxyl radicals in the presence of iron salts
    • Gutteridge JM, Rowley DA, and Halliwell B. Superoxide-dependent formation of hydroxyl radicals in the presence of iron salts. Biochem J 199: 263-265, 1981.
    • (1981) Biochem J , vol.199 , pp. 263-265
    • Gutteridge, J.M.1    Rowley, D.A.2    Halliwell, B.3
  • 16
    • 0020422695 scopus 로고
    • Superoxide-dependent formation by hydroxyl radicals and lipid peroxidation in the presence of iron salts
    • Gutteridge JM, Rowley DA, and Halliwell B. Superoxide-dependent formation by hydroxyl radicals and lipid peroxidation in the presence of iron salts. Biochem J 206: 605-609, 1982.
    • (1982) Biochem J , vol.206 , pp. 605-609
    • Gutteridge, J.M.1    Rowley, D.A.2    Halliwell, B.3
  • 17
    • 0025126555 scopus 로고
    • Role of free radicals and catalytic metal ions in human disease: An overview
    • Halliwell B and Gutteridge JM. Role of free radicals and catalytic metal ions in human disease: an overview. Methods Enzymol 186: 1-85, 1990.
    • (1990) Methods Enzymol , vol.186 , pp. 1-85
    • Halliwell, B.1    Gutteridge, J.M.2
  • 18
    • 0001435384 scopus 로고
    • Metabolic reactions: Role of cytochrome P450 in the formation of reactive oxygen species
    • Kappus H. Metabolic reactions: role of cytochrome P450 in the formation of reactive oxygen species. Handb Exp Pharm 105: 145-154, 1993.
    • (1993) Handb Exp Pharm , vol.105 , pp. 145-154
    • Kappus, H.1
  • 19
    • 0028099510 scopus 로고
    • Hydrogen peroxide-mediated inactivation of microsomal cytochrome P450 during monooxygenase reactions
    • Karuzina II and Archakov AI. Hydrogen peroxide-mediated inactivation of microsomal cytochrome P450 during monooxygenase reactions. Free Radic Biol Med 17: 557-567, 1994.
    • (1994) Free Radic Biol Med , vol.17 , pp. 557-567
    • Karuzina, I.I.1    Archakov, A.I.2
  • 20
    • 0028917414 scopus 로고
    • Effect of insulin on high-glucose medium-induced changes in rat glomerular epithelial cell metabolism of glycoconjugates
    • Kasinath BS. Effect of insulin on high-glucose medium-induced changes in rat glomerular epithelial cell metabolism of glycoconjugates. Arch Biochem Biophys 318: 286-294, 1995.
    • (1995) Arch Biochem Biophys , vol.318 , pp. 286-294
    • Kasinath, B.S.1
  • 21
    • 0026578971 scopus 로고
    • Role of active oxygen species in glomerular epithelial cell injury in vitro caused by puromycin aminonucleoside
    • Kawaguchi M, Yamada M, Wada H, and Okigaki T. Role of active oxygen species in glomerular epithelial cell injury in vitro caused by puromycin aminonucleoside. Toxicology 72: 329-340, 1992.
    • (1992) Toxicology , vol.72 , pp. 329-340
    • Kawaguchi, M.1    Yamada, M.2    Wada, H.3    Okigaki, T.4
  • 22
    • 0028256192 scopus 로고
    • Increased expression of heme oxygenase-1 in human retinal pigment epithelial cells by transforming growth factor-beta
    • Kutty RK, Nagineni CN, Kutty G, Hooks JJ, Chader GJ, and Wiggert B. Increased expression of heme oxygenase-1 in human retinal pigment epithelial cells by transforming growth factor-beta. J Cell Physiol 159: 371-378, 1994.
    • (1994) J Cell Physiol , vol.159 , pp. 371-378
    • Kutty, R.K.1    Nagineni, C.N.2    Kutty, G.3    Hooks, J.J.4    Chader, G.J.5    Wiggert, B.6
  • 23
    • 0011332257 scopus 로고
    • The effect of a single intravenous injection of aminonucleoside of puromycin on the rat kidney: A light and electronmicroscope study
    • Lannigan R, Kark R, and Pollak VE. The effect of a single intravenous injection of aminonucleoside of puromycin on the rat kidney: a light and electronmicroscope study. J Pathol Bacteriol 83: 357-362, 1962.
    • (1962) J Pathol Bacteriol , vol.83 , pp. 357-362
    • Lannigan, R.1    Kark, R.2    Pollak, V.E.3
  • 24
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature
    • Omura T and Sato R. The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature. J Biol Chem 239: 2370-2378, 1964.
    • (1964) J Biol Chem , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 25
    • 0023755521 scopus 로고
    • Hemoglobin- and myoglobin-induced acute renal failure in rats: Role of iron in nephrotoxicity
    • Paller MS. Hemoglobin- and myoglobin-induced acute renal failure in rats: role of iron in nephrotoxicity. Am J Physiol Renal Fluid Electrolyte Physiol 255: F539-F544, 1988.
    • (1988) Am J Physiol Renal Fluid Electrolyte Physiol , vol.255
    • Paller, M.S.1
  • 26
    • 0028321518 scopus 로고
    • Cytochrome P-450 mediates tissue damaging hydroxyl radical formation during reoxygenation of the kidney
    • Paller MS and Jacob HS. Cytochrome P-450 mediates tissue damaging hydroxyl radical formation during reoxygenation of the kidney. Proc Natl Acad Sci USA 91: 7002-7006, 1994.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 7002-7006
    • Paller, M.S.1    Jacob, H.S.2
  • 27
    • 0032964289 scopus 로고    scopus 로고
    • Cellular iron metabolism
    • Ponka P. Cellular iron metabolism. Kidney Int 69: S2-S11, 1999.
    • (1999) Kidney Int , vol.69
    • Ponka, P.1
  • 28
    • 0027991761 scopus 로고
    • Treatment of the nephrotic syndrome associated with primary glomerulonephritis
    • Ponticelli C and Passerini P. Treatment of the nephrotic syndrome associated with primary glomerulonephritis. Kidney Int 46: 595-604, 1994.
    • (1994) Kidney Int , vol.46 , pp. 595-604
    • Ponticelli, C.1    Passerini, P.2
  • 29
    • 0020541473 scopus 로고
    • Characterization of cimetidine, ranitidine, and related structures' interaction with cytochrome P450
    • Rendic S, Kajfez F, and Ruf HH. Characterization of cimetidine, ranitidine, and related structures' interaction with cytochrome P450. Drug Metab Dispos 11: 137-142, 1983.
    • (1983) Drug Metab Dispos , vol.11 , pp. 137-142
    • Rendic, S.1    Kajfez, F.2    Ruf, H.H.3
  • 30
    • 0028145046 scopus 로고
    • Reactive oxygen species in puromycin amnonucleoside nephrosis: In vitro studies
    • Ricardo SD, Bertram JF, and Ryan GB. Reactive oxygen species in puromycin amnonucleoside nephrosis: in vitro studies. Kidney Int 45: 1057-1069, 1994.
    • (1994) Kidney Int , vol.45 , pp. 1057-1069
    • Ricardo, S.D.1    Bertram, J.F.2    Ryan, G.B.3
  • 31
    • 0024379914 scopus 로고
    • Role of reactive oxygen metabolites in experimental glomerular disease
    • Shah SV. Role of reactive oxygen metabolites in experimental glomerular disease. Kidney Int 35: 1093-1106, 1989.
    • (1989) Kidney Int , vol.35 , pp. 1093-1106
    • Shah, S.V.1
  • 32
    • 0022977615 scopus 로고
    • Purification and characterization of the major constitutive form of testicular heme oxygenase
    • Trakshel GM, Kutty RK, and Maines MD. Purification and characterization of the major constitutive form of testicular heme oxygenase. J Biol Chem 261: 11131-11137, 1986.
    • (1986) J Biol Chem , vol.261 , pp. 11131-11137
    • Trakshel, G.M.1    Kutty, R.K.2    Maines, M.D.3
  • 33
    • 0030052563 scopus 로고    scopus 로고
    • Role of "catalytic" iron in animal model of minimal change nephrotic syndrome
    • Ueda N, Baliga R, and Shah SV. Role of "catalytic" iron in animal model of minimal change nephrotic syndrome. Kidney Int 49: 370-373, 1996.
    • (1996) Kidney Int , vol.49 , pp. 370-373
    • Ueda, N.1    Baliga, R.2    Shah, S.V.3
  • 35
    • 0030887448 scopus 로고    scopus 로고
    • 2, and terminal mitochondrial electron transport
    • 2, and terminal mitochondrial electron transport. Kidney Int 51: 728-738, 1997.
    • (1997) Kidney Int , vol.51 , pp. 728-738
    • Zager, R.A.1    Burkhart, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.