메뉴 건너뛰기




Volumn 73, Issue 2, 2005, Pages 106-112

Inducible nitric oxide synthase activity and expression in liver and hepatocytes of diabetic rats

Author keywords

Diabetes; Liver; Nitric oxide synthase; Phosphatidylinositol 3 kinase; Reactive oxygen species; Superoxide dismutase

Indexed keywords

AMINOGUANIDINE; COPPER ZINC SUPEROXIDE DISMUTASE; DRINKING WATER; INDUCIBLE NITRIC OXIDE SYNTHASE; INSULIN; PHOSPHATIDYLINOSITOL 3 KINASE;

EID: 11444256883     PISSN: 00317012     EISSN: None     Source Type: Journal    
DOI: 10.1159/000081952     Document Type: Article
Times cited : (24)

References (29)
  • 2
    • 0028349156 scopus 로고
    • Nitric oxide synthases in mammals
    • Knowles RG, Moncada S: Nitric oxide synthases in mammals. Biochem J 1994;298:249-258.
    • (1994) Biochem J , vol.298 , pp. 249-258
    • Knowles, R.G.1    Moncada, S.2
  • 6
    • 0344643456 scopus 로고    scopus 로고
    • Peroxynitrite-induced cytotoxicity: Mechanism and opportunities for intervention
    • Virag L, Szabo E, Gergely P, Szabo C: Peroxynitrite-induced cytotoxicity: Mechanism and opportunities for intervention. Toxicol Lett 2003;140-141:113- 124.
    • (2003) Toxicol Lett , vol.140-141 , pp. 113-124
    • Virag, L.1    Szabo, E.2    Gergely, P.3    Szabo, C.4
  • 8
    • 0033994409 scopus 로고    scopus 로고
    • Radicals and oxidative stress in diabetes
    • West IC: Radicals and oxidative stress in diabetes. Diabet Med 2000;17:171-180.
    • (2000) Diabet Med , vol.17 , pp. 171-180
    • West, I.C.1
  • 9
    • 0029875833 scopus 로고    scopus 로고
    • High glucose induces antioxidant enzymes in human endothelial cells in culture. Evidence linking hyperglycemia and oxidative stress
    • Ceriello A, dello Russo P, Amstad P, Cerutti P: High glucose induces antioxidant enzymes in human endothelial cells in culture. Evidence linking hyperglycemia and oxidative stress. Diabetes 1996;45:471-477.
    • (1996) Diabetes , vol.45 , pp. 471-477
    • Ceriello, A.1    Dello Russo, P.2    Amstad, P.3    Cerutti, P.4
  • 10
    • 0033806188 scopus 로고    scopus 로고
    • Protective effect of boldine on oxidative mitochondrial damage in streptozotocin-induced diabetic rats
    • Jang YY, Song JH, Shin YK, Han ES, Lee CS: Protective effect of boldine on oxidative mitochondrial damage in streptozotocin-induced diabetic rats. Pharmacol Res 2000;42:361-371.
    • (2000) Pharmacol Res , vol.42 , pp. 361-371
    • Jang, Y.Y.1    Song, J.H.2    Shin, Y.K.3    Han, E.S.4    Lee, C.S.5
  • 11
    • 0035113190 scopus 로고    scopus 로고
    • Oxidative stress and nitric oxide related parameters in type II diabetes mellitus: Effects of glycemic control
    • Aydin A, Orhan H, Sayal A, Ozata M, Sahin G, Isimer A: Oxidative stress and nitric oxide related parameters in type II diabetes mellitus: Effects of glycemic control. Clin Biochem 2001;34:65-70.
    • (2001) Clin Biochem , vol.34 , pp. 65-70
    • Aydin, A.1    Orhan, H.2    Sayal, A.3    Ozata, M.4    Sahin, G.5    Isimer, A.6
  • 12
  • 13
    • 0037451703 scopus 로고    scopus 로고
    • Decreased activity and impaired induction of nitric oxide synthase by lipopolysaccharides in streptozotocin-induced diabetic rats
    • Khandelwal RL, Gupta D, Sulakhe PV: Decreased activity and impaired induction of nitric oxide synthase by lipopolysaccharides in streptozotocin-induced diabetic rats. Biochim Biophys Acta 2003;1620:259-266.
    • (2003) Biochim Biophys Acta , vol.1620 , pp. 259-266
    • Khandelwal, R.L.1    Gupta, D.2    Sulakhe, P.V.3
  • 14
    • 0020037296 scopus 로고
    • Intracellular compartmentation and control of alanine metabolism in rat liver parenchymal cells
    • Groen AK, Sips HJ, Vervoorn RC, Tager JM: Intracellular compartmentation and control of alanine metabolism in rat liver parenchymal cells. Eur J Biochem 1982;122:87-93.
    • (1982) Eur J Biochem , vol.122 , pp. 87-93
    • Groen, A.K.1    Sips, H.J.2    Vervoorn, R.C.3    Tager, J.M.4
  • 15
    • 0025895399 scopus 로고
    • Widespread tissue distribution, species distribution and changes in activity of Ca(2+)-dependent and Ca(2+)-independent nitric oxide synthases
    • Salter M, Knowles RG, Moncada S: Widespread tissue distribution, species distribution and changes in activity of Ca(2+)-dependent and Ca(2+)-independent nitric oxide synthases. FEBS Lett 1991;291:145-149.
    • (1991) FEBS Lett , vol.291 , pp. 145-149
    • Salter, M.1    Knowles, R.G.2    Moncada, S.3
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976;72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 17
    • 0022684839 scopus 로고
    • Overproduction of human Cu/Zn-superoxide dismutase in transfected cells: Extenuation of paraquat-mediated cytotoxicity and enhancement of lipid peroxidation
    • Elroy-Stein O, Bernstein Y, Groner Y: Overproduction of human Cu/Zn-superoxide dismutase in transfected cells: Extenuation of paraquat-mediated cytotoxicity and enhancement of lipid peroxidation. EMBO J 1986;5:615-622.
    • (1986) EMBO J , vol.5 , pp. 615-622
    • Elroy-Stein, O.1    Bernstein, Y.2    Groner, Y.3
  • 18
    • 0141483042 scopus 로고    scopus 로고
    • Suppressive effects of a selective inducible nitric oxide synthase (iNOS) inhibitor on pancreatic beta-cell dysfunction
    • Kato Y, Miura Y, Yamamoto N, Ozaki N, Oiso Y: Suppressive effects of a selective inducible nitric oxide synthase (iNOS) inhibitor on pancreatic beta-cell dysfunction. Diabetologia 2003;46:1228-1233.
    • (2003) Diabetologia , vol.46 , pp. 1228-1233
    • Kato, Y.1    Miura, Y.2    Yamamoto, N.3    Ozaki, N.4    Oiso, Y.5
  • 20
    • 0032213596 scopus 로고    scopus 로고
    • Effect of L-arginine-nitric oxide system on chemical-induced diabetes mellitus
    • Mohan IK, Das UN: Effect of L-arginine-nitric oxide system on chemical-induced diabetes mellitus. Free Radic Biol Med 1998;25:757-765.
    • (1998) Free Radic Biol Med , vol.25 , pp. 757-765
    • Mohan, I.K.1    Das, U.N.2
  • 21
    • 0037213776 scopus 로고    scopus 로고
    • Effects of diabetes, insulin and antioxidants on NO synthase abundance and NO interaction with reactive oxygen species
    • Koo JR, Vaziri ND: Effects of diabetes, insulin and antioxidants on NO synthase abundance and NO interaction with reactive oxygen species. Kidney Int 2003;63:195-201.
    • (2003) Kidney Int , vol.63 , pp. 195-201
    • Koo, J.R.1    Vaziri, N.D.2
  • 22
    • 0034452396 scopus 로고    scopus 로고
    • Interactions between phosphatidylinositol 3-kinase and nitric oxide: Explaining the paradox
    • Wright KL, Ward SG: Interactions between phosphatidylinositol 3-kinase and nitric oxide: Explaining the paradox. Mol Cell Biol Res Commun 2000;4:137-143.
    • (2000) Mol Cell Biol Res Commun , vol.4 , pp. 137-143
    • Wright, K.L.1    Ward, S.G.2
  • 23
    • 0031774262 scopus 로고    scopus 로고
    • Insulin inhibits inducible nitric oxide synthase in skeletal muscle cells
    • Bedard S, Marcotte B, Marette A: Insulin inhibits inducible nitric oxide synthase in skeletal muscle cells. Diabetologia 1998;41:1523-1527.
    • (1998) Diabetologia , vol.41 , pp. 1523-1527
    • Bedard, S.1    Marcotte, B.2    Marette, A.3
  • 25
    • 0027771348 scopus 로고
    • Aminoguanidine, an inhibitor of nitric oxide formation, fails to protect against insulitis and hyperglycemia induced by multiple low dose streptozotocin injections in mice
    • Holstad M, Sandler S: Aminoguanidine, an inhibitor of nitric oxide formation, fails to protect against insulitis and hyperglycemia induced by multiple low dose streptozotocin injections in mice. Autoimmunity 1993;15:311-314.
    • (1993) Autoimmunity , vol.15 , pp. 311-314
    • Holstad, M.1    Sandler, S.2
  • 26
    • 0025194579 scopus 로고
    • New perspectives on the biochemistry of superoxide anion and the efficiency of superoxide dismutases
    • Deby C, Goutier R: New perspectives on the biochemistry of superoxide anion and the efficiency of superoxide dismutases. Biochem Pharmacol 1990;39:399-405.
    • (1990) Biochem Pharmacol , vol.39 , pp. 399-405
    • Deby, C.1    Goutier, R.2
  • 27
    • 0031587934 scopus 로고    scopus 로고
    • Renal cortical expression of mRNAs for antioxidant enzymes in normal and diabetic rats
    • Reddi AS, Bollineni JS: Renal cortical expression of mRNAs for antioxidant enzymes in normal and diabetic rats. Biochem Biophys Res Commun 1997;235:598-601.
    • (1997) Biochem Biophys Res Commun , vol.235 , pp. 598-601
    • Reddi, A.S.1    Bollineni, J.S.2
  • 28
    • 0023582040 scopus 로고
    • Glycation and inactivation of human Cu-Zn-superoxide dismutase. Identification of the in vitro glycated sites
    • Arai K, Maguchi S, Fujii S, Ishibashi H, Oikawa K, Taniguchi N: Glycation and inactivation of human Cu-Zn-superoxide dismutase. Identification of the in vitro glycated sites. J Biol Chem 1987;262:16969-16972.
    • (1987) J Biol Chem , vol.262 , pp. 16969-16972
    • Arai, K.1    Maguchi, S.2    Fujii, S.3    Ishibashi, H.4    Oikawa, K.5    Taniguchi, N.6
  • 29
    • 0029554381 scopus 로고
    • Hormonal regulation of superoxide dismutase, catalase, and glutathione peroxidase activities in rat macrophages
    • Pereira B, Rosa LF, Safi DA, Bechara EJ, Curi R: Hormonal regulation of superoxide dismutase, catalase, and glutathione peroxidase activities in rat macrophages. Biochem Pharmacol 1995;50:2093-2098.
    • (1995) Biochem Pharmacol , vol.50 , pp. 2093-2098
    • Pereira, B.1    Rosa, L.F.2    Safi, D.A.3    Bechara, E.J.4    Curi, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.