메뉴 건너뛰기




Volumn 275, Issue 4 44-4, 1998, Pages

Heme oxygenase-1 induction in skeletal muscle cells: Hemin and sodium nitroprusside are regulators in vitro

Author keywords

Heat shock protein 32; Heine; Heme proteins; Hydroxocobalamin; Myoglobin

Indexed keywords

HEME OXYGENASE; HEMIN; MYOGLOBIN; NITROPRUSSIDE SODIUM;

EID: 0031722008     PISSN: 03636143     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpcell.1998.275.4.c1087     Document Type: Article
Times cited : (67)

References (37)
  • 2
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P., and N. Sacchi. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162: 156-159, 1987.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 3
    • 0030961521 scopus 로고    scopus 로고
    • Nitric oxide induces heme oxygenase-1 gene expression and carbon monoxide production in vascular smooth muscle cells
    • Durante, W., M. H. Kroll, N. Christodoulides, K. J. Peyton, and A. I. Schafer. Nitric oxide induces heme oxygenase-1 gene expression and carbon monoxide production in vascular smooth muscle cells. Circ. Res. 80: 557-564, 1997.
    • (1997) Circ. Res. , vol.80 , pp. 557-564
    • Durante, W.1    Kroll, M.H.2    Christodoulides, N.3    Peyton, K.J.4    Schafer, A.I.5
  • 4
    • 0031028451 scopus 로고    scopus 로고
    • Induction of heme oxygenase-1 (HSP32) mRNA in skeletal muscle following contractions
    • Cell Physiol. 41
    • Essig, D. A., D. R. Borger, and D. A. Jackson. Induction of heme oxygenase-1 (HSP32) mRNA in skeletal muscle following contractions. Am. J. Physiol. 272 (Cell Physiol. 41): C59-C67, 1997.
    • (1997) Am. J. Physiol. , vol.272
    • Essig, D.A.1    Borger, D.R.2    Jackson, D.A.3
  • 5
    • 0030875968 scopus 로고    scopus 로고
    • Thiol compounds interact with nitric oxide in regulating heme oxygenase-1 induction in endothelial cells. Involvement of superoxide and peroxynitrite anions
    • Foresti, R., J. E. Clark, C. J. Green, and R. Motterlini. Thiol compounds interact with nitric oxide in regulating heme oxygenase-1 induction in endothelial cells. Involvement of superoxide and peroxynitrite anions. J. Biol. Chem. 272: 18411-18417, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18411-18417
    • Foresti, R.1    Clark, J.E.2    Green, C.J.3    Motterlini, R.4
  • 6
    • 0026034934 scopus 로고
    • Endothelium-dependent and -independent vasodilation involving cyclic GMP: Relaxation induced by nitric oxide, carbon monoxide and light
    • Furchgott, R. F., and D. Jothianandan. Endothelium-dependent and -independent vasodilation involving cyclic GMP: relaxation induced by nitric oxide, carbon monoxide and light. Blood Vessels 28: 52-61, 1991.
    • (1991) Blood Vessels , vol.28 , pp. 52-61
    • Furchgott, R.F.1    Jothianandan, D.2
  • 7
    • 0022469346 scopus 로고
    • Iron promoters of the Fenton reaction and lipid peroxidation can be released from haemoglobin by peroxides
    • Gutteridge, J. M. Iron promoters of the Fenton reaction and lipid peroxidation can be released from haemoglobin by peroxides. FEBS Lett. 201: 291-295, 1986.
    • (1986) FEBS Lett. , vol.201 , pp. 291-295
    • Gutteridge, J.M.1
  • 8
    • 0028818098 scopus 로고
    • Expression of the mRNA of heme-binding protein 23 is coordinated with that of heme oxygenase-1 by heme and heavy metals in primary rat hepatocytes and hepatoma cells
    • Immenschuh, S., S. Iwahara, H. Satoh, C. Nell, N. Katz, and U. Muller Eberhard. Expression of the mRNA of heme-binding protein 23 is coordinated with that of heme oxygenase-1 by heme and heavy metals in primary rat hepatocytes and hepatoma cells. Biochemistry 34: 13407-13411, 1995.
    • (1995) Biochemistry , vol.34 , pp. 13407-13411
    • Immenschuh, S.1    Iwahara, S.2    Satoh, H.3    Nell, C.4    Katz, N.5    Muller Eberhard, U.6
  • 10
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685, 1970.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 11
    • 0021984681 scopus 로고
    • Oxygen-derived free radicals in postischemic tissue injury
    • McCord, J. M. Oxygen-derived free radicals in postischemic tissue injury. N. Engl. J. Med. 312: 159-163, 1985.
    • (1985) N. Engl. J. Med. , vol.312 , pp. 159-163
    • McCord, J.M.1
  • 12
    • 8544246393 scopus 로고    scopus 로고
    • Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3
    • McCoubrey, W. K., Jr., T. J. Huang, and M. D. Maines. Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3. Eur. J. Biochem. 247: 725-732, 1997.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 725-732
    • McCoubrey Jr., W.K.1    Huang, T.J.2    Maines, M.D.3
  • 13
    • 0023731036 scopus 로고
    • Heme oxygenase: Function, multiplicity, regulatory mechanisms, and clinical applications
    • Maines, M. D. Heme oxygenase: function, multiplicity, regulatory mechanisms, and clinical applications. FASEB J. 2: 2557-2568, 1988.
    • (1988) FASEB J. , vol.2 , pp. 2557-2568
    • Maines, M.D.1
  • 14
    • 0030923630 scopus 로고    scopus 로고
    • The heme oxygenase system: A regulator of second messenger gases
    • Maines, M. D. The heme oxygenase system: a regulator of second messenger gases. Annu. Rev. Pharmacol. Toxicol. 37: 517-554, 1997.
    • (1997) Annu. Rev. Pharmacol. Toxicol. , vol.37 , pp. 517-554
    • Maines, M.D.1
  • 15
    • 0027485237 scopus 로고
    • Induction of kidney heme oxygenase-1 (HSP32) mRNA and protein by ischemia/reperfusion: Possible role of heme as both promotor of tissue damage and regulator of HSP32
    • Maines, M. D., R. D. Mayer, J. F. Ewing, and W. K. McCoubrey, Jr. Induction of kidney heme oxygenase-1 (HSP32) mRNA and protein by ischemia/reperfusion: possible role of heme as both promotor of tissue damage and regulator of HSP32. J. Pharmacol. Exp. Ther. 264: 457-462, 1993.
    • (1993) J. Pharmacol. Exp. Ther. , vol.264 , pp. 457-462
    • Maines, M.D.1    Mayer, R.D.2    Ewing, J.F.3    McCoubrey Jr., W.K.4
  • 16
    • 0022632224 scopus 로고
    • Characterization of two constitutive forms of rat liver microsomal heme oxygenase. only one molecular species of the enzyme is inducible
    • Maines, M. D., G. M. Trakshel, and R. K. Kutty. Characterization of two constitutive forms of rat liver microsomal heme oxygenase. Only one molecular species of the enzyme is inducible. J. Biol. Chem. 261: 411-419, 1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 411-419
    • Maines, M.D.1    Trakshel, G.M.2    Kutty, R.K.3
  • 17
    • 0030065052 scopus 로고    scopus 로고
    • NO-mediated activation of heme oxygenase: Endogenous cytoprotection against oxidative stress to endothelium
    • Heart Circ. Physiol. 39
    • Motterlini, R., R. Foresti, M. Intaglietta, and R. M. Winslow. NO-mediated activation of heme oxygenase: endogenous cytoprotection against oxidative stress to endothelium. Am. J. Physiol. 270 (Heart Circ. Physiol. 39): H107-H114, 1996.
    • (1996) Am. J. Physiol. , vol.270
    • Motterlini, R.1    Foresti, R.2    Intaglietta, M.3    Winslow, R.M.4
  • 18
    • 0029124111 scopus 로고
    • Oxidative-stress response in vascular endothelial cells exposed to acellular hemoglobin solutions
    • Heart Circ. Physiol. 38
    • Motterlini, R., R. Foresti, K. Vandegriff, M. Intaglietta, and R. M. Winslow. Oxidative-stress response in vascular endothelial cells exposed to acellular hemoglobin solutions. Am. J. Physiol. 269 (Heart Circ. Physiol. 38): H648-H655, 1995.
    • (1995) Am. J. Physiol. , vol.269
    • Motterlini, R.1    Foresti, R.2    Vandegriff, K.3    Intaglietta, M.4    Winslow, R.M.5
  • 19
    • 0025868208 scopus 로고
    • The identification of heme oxygenase as a major hypoxic stress protein in Chinese hamster ovary cells
    • Murphy, B. J., K. R. Laderoute, S. M. Short, and R. M. Sutherland. The identification of heme oxygenase as a major hypoxic stress protein in Chinese hamster ovary cells. Br. J. Cancer 64: 69-73, 1991.
    • (1991) Br. J. Cancer , vol.64 , pp. 69-73
    • Murphy, B.J.1    Laderoute, K.R.2    Short, S.M.3    Sutherland, R.M.4
  • 21
    • 0029114104 scopus 로고
    • Cytokine-stimulated nitric oxide production inhibits mitochondrial activity in cardiac myocytes
    • Oddis, C. V., and M. S. Finkel. Cytokine-stimulated nitric oxide production inhibits mitochondrial activity in cardiac myocytes. Biochem. Biophys. Res. Commun. 213: 1002-1009, 1995.
    • (1995) Biochem. Biophys. Res. Commun. , vol.213 , pp. 1002-1009
    • Oddis, C.V.1    Finkel, M.S.2
  • 22
    • 0029410648 scopus 로고
    • Hemoglobin provides protection against lethal endotoxemia in rats: The role of heme oxygenase-1
    • Otterbein, L., S. L. Sylvester, and A. M. Choi. Hemoglobin provides protection against lethal endotoxemia in rats: the role of heme oxygenase-1. Am. J. Respir. Cell Mol. Biol. 13: 595-601, 1995.
    • (1995) Am. J. Respir. Cell Mol. Biol. , vol.13 , pp. 595-601
    • Otterbein, L.1    Sylvester, S.L.2    Choi, A.M.3
  • 23
    • 0023755521 scopus 로고
    • Hemoglobin- and myoglobin-induced acute renal failure in rats: Role of iron in nephrotoxicity
    • Renal Fluid Electrolyte Physiol. 24
    • Paller, M. S. Hemoglobin- and myoglobin-induced acute renal failure in rats: role of iron in nephrotoxicity. Am. J. Physiol. 255 (Renal Fluid Electrolyte Physiol. 24): F539-F544, 1988.
    • (1988) Am. J. Physiol. , vol.255
    • Paller, M.S.1
  • 24
    • 0024461666 scopus 로고
    • Effects of oxyradicals on oxymyoglobin. Deoxygenation, haem removal and iron release
    • Prasad, M. R., R. M. Engelman, R. M. Jones, and D. K. Das. Effects of oxyradicals on oxymyoglobin. Deoxygenation, haem removal and iron release. Biochem. J. 263: 731-736, 1989.
    • (1989) Biochem. J. , vol.263 , pp. 731-736
    • Prasad, M.R.1    Engelman, R.M.2    Jones, R.M.3    Das, D.K.4
  • 25
    • 0027395550 scopus 로고
    • Differential effects of hydroxocobalamin on NO-mediated relaxations in rat aorta and anococcygeus muscle
    • Rajanayagam, M. A. S., C. G. Li., and M. J. Rand. Differential effects of hydroxocobalamin on NO-mediated relaxations in rat aorta and anococcygeus muscle. Br. J. Pharmacol. 108: 3-5, 1993.
    • (1993) Br. J. Pharmacol. , vol.108 , pp. 3-5
    • Rajanayagam, M.A.S.1    Li, C.G.2    Rand, M.J.3
  • 26
    • 0343773381 scopus 로고    scopus 로고
    • Generation of reactive oxygen species by the redox cycling of nitroprusside
    • Ramakrishna Rao, D. N., and A. I. Cederbaum. Generation of reactive oxygen species by the redox cycling of nitroprusside. Biochim. Biophys. Acta 1289: 195-202, 1996.
    • (1996) Biochim. Biophys. Acta , vol.1289 , pp. 195-202
    • Ramakrishna Rao, D.N.1    Cederbaum, A.I.2
  • 27
    • 0023707789 scopus 로고
    • Evidence suggesting a role for hydroxyl radical in glycerol-induced acute renal failure
    • Renal Fluid Electrolyte Physiol. 24
    • Shah, S. V., and P. D. Walker. Evidence suggesting a role for hydroxyl radical in glycerol-induced acute renal failure. Am. J. Physiol. 255 (Renal Fluid Electrolyte Physiol. 24): F438-F443, 1988.
    • (1988) Am. J. Physiol. , vol.255
    • Shah, S.V.1    Walker, P.D.2
  • 28
    • 0029067386 scopus 로고
    • Determination of hydroxyl radical formation in the testes of cadmium-treated mice by high-performance liquid-chromatography
    • Shen, S., S. Sangiah, and M. Ye. Determination of hydroxyl radical formation in the testes of cadmium-treated mice by high-performance liquid-chromatography. J. Liq. Chromatogr. 18: 2217-2228, 1995.
    • (1995) J. Liq. Chromatogr. , vol.18 , pp. 2217-2228
    • Shen, S.1    Sangiah, S.2    Ye, M.3
  • 29
    • 0023665016 scopus 로고
    • Transcriptional control of rat heme oxygenase by heat shock
    • Shibahara, S., R. M. Muller, and H. Taguchi. Transcriptional control of rat heme oxygenase by heat shock. J. Biol. Chem. 262: 12889-12892, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12889-12892
    • Shibahara, S.1    Muller, R.M.2    Taguchi, H.3
  • 31
    • 0018104963 scopus 로고
    • Induction of heme oxygenase by hemin in cultured pig alveolar macrophages
    • Shibahara, S., T. Yoshida, and G. Kikuchi. Induction of heme oxygenase by hemin in cultured pig alveolar macrophages. Arch. Biochem. Biophys. 188: 243-250, 1978.
    • (1978) Arch. Biochem. Biophys. , vol.188 , pp. 243-250
    • Shibahara, S.1    Yoshida, T.2    Kikuchi, G.3
  • 32
    • 0023132858 scopus 로고
    • Bilirubin is an antioxidant of possible physiological importance
    • Stocker, R., Y. Yamamoto, A. F. McDonagh, A. N. Glazer, and B. N. Ames. Bilirubin is an antioxidant of possible physiological importance. Science 235: 1043-1046, 1987.
    • (1987) Science , vol.235 , pp. 1043-1046
    • Stocker, R.1    Yamamoto, Y.2    McDonagh, A.F.3    Glazer, A.N.4    Ames, B.N.5
  • 33
    • 0014748520 scopus 로고
    • The enzymatic catabolism of hemoglobin: Stimulation of microsomal heme oxygenase by hemin
    • Tenhunen, R., H. S. Marver, and R. Schmid. The enzymatic catabolism of hemoglobin: stimulation of microsomal heme oxygenase by hemin. J. Lab. Clin. Med. 75: 410-421, 1970.
    • (1970) J. Lab. Clin. Med. , vol.75 , pp. 410-421
    • Tenhunen, R.1    Marver, H.S.2    Schmid, R.3
  • 34
    • 0023029882 scopus 로고
    • Cadmium-mediated inhibition of testicular heme oxygenase activity: The role of NADPH-cytochrome c (P-450) reductase
    • Trakshel, G. M., R. K. Kutty, and M. D. Maines. Cadmium-mediated inhibition of testicular heme oxygenase activity: the role of NADPH-cytochrome c (P-450) reductase. Arch. Biochem. Biophys. 251: 175-187, 1986.
    • (1986) Arch. Biochem. Biophys. , vol.251 , pp. 175-187
    • Trakshel, G.M.1    Kutty, R.K.2    Maines, M.D.3
  • 35
    • 0027997105 scopus 로고
    • Transient enhancement of heme oxygenase 1 mRNA accumulation: A marker of oxidative stress to eukaryotic cells
    • Tyrrell, R. M., and S. Basu Modak. Transient enhancement of heme oxygenase 1 mRNA accumulation: a marker of oxidative stress to eukaryotic cells. Methods Enzymol. 234: 224-235, 1994.
    • (1994) Methods Enzymol. , vol.234 , pp. 224-235
    • Tyrrell, R.M.1    Basu Modak, S.2
  • 36
    • 0028941025 scopus 로고
    • Acquired resistance to acute oxidative stress. Possible role of heme oxygenase and ferritin
    • Vogt, B. A., J. Alam, A. J. Croatt, G. M. Vercellotti, and K. A. Nath. Acquired resistance to acute oxidative stress. Possible role of heme oxygenase and ferritin. Lab. Invest. 72 :474-483, 1995.
    • (1995) Lab. Invest. , vol.72 , pp. 474-483
    • Vogt, B.A.1    Alam, J.2    Croatt, A.J.3    Vercellotti, G.M.4    Nath, K.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.