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Volumn 99, Issue 1, 2006, Pages 59-66

Heme oxygenase-carbon monoxide (HO-CO) system in rat uterus: Effect of sexual steroids and prostaglandins

Author keywords

Carbon monoxide; cGMP; Heme oxygenase; Oxidative stress; Pregnancy; Prostaglandins; Steroids; Uterus

Indexed keywords

BILIRUBIN; CARBON MONOXIDE; CYCLIC GMP; ESTRADIOL; ESTROGEN; HEME OXYGENASE; LIPID; PROGESTERONE; PROSTAGLANDIN; PROSTAGLANDIN F2 ALPHA; PROSTAGLANDIN SYNTHASE; PROTOPORPHYRIN; TAMOXIFEN; THIOBARBITURIC ACID REACTIVE SUBSTANCE;

EID: 33646511516     PISSN: 09600760     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsbmb.2005.11.007     Document Type: Article
Times cited : (7)

References (39)
  • 1
    • 0014348401 scopus 로고
    • The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase
    • Tenhunen R., Marver H.S., and Schmid R. The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase. Proc. Natl. Acad. Sci. U.S.A. 61 (1968) 748-755
    • (1968) Proc. Natl. Acad. Sci. U.S.A. , vol.61 , pp. 748-755
    • Tenhunen, R.1    Marver, H.S.2    Schmid, R.3
  • 2
    • 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 (1988) 2557-2568
    • (1988) FASEB J. , vol.2 , pp. 2557-2568
    • Maines, M.D.1
  • 3
    • 8544246393 scopus 로고    scopus 로고
    • Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3
    • McCoubrey Jr. W.K., Huang T.J., and Maines M.D. Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3. Eur. J. Biochem. 247 (1997) 725-732
    • (1997) Eur. J. Biochem. , vol.247 , pp. 725-732
    • McCoubrey Jr., W.K.1    Huang, T.J.2    Maines, M.D.3
  • 4
    • 0024497521 scopus 로고
    • Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite
    • Keyse S.M., and Tyrrell R.M. Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite. Proc. Natl. Acad. Sci. U.S.A. 86 (1989) 99-103
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 99-103
    • Keyse, S.M.1    Tyrrell, R.M.2
  • 5
    • 0026542512 scopus 로고
    • Normal and heat-induced patterns of expression of heme oxygenase-1 (HSP32) in rat brain: hyperthermia causes rapid induction of mRNA and protein
    • Ewing J.F., Haber S.N., and Maines M.D. Normal and heat-induced patterns of expression of heme oxygenase-1 (HSP32) in rat brain: hyperthermia causes rapid induction of mRNA and protein. J. Neurochem. 58 (1992) 1140-1149
    • (1992) J. Neurochem. , vol.58 , pp. 1140-1149
    • Ewing, J.F.1    Haber, S.N.2    Maines, M.D.3
  • 6
    • 0027523219 scopus 로고
    • Glutathione depletion induces heme-oxygenase-1 (HSP32) mRNA and protein in rat brain
    • Ewing J.F., and Maines M.D. Glutathione depletion induces heme-oxygenase-1 (HSP32) mRNA and protein in rat brain. J. Neurochem. 60 (1993) 1512-1519
    • (1993) J. Neurochem. , vol.60 , pp. 1512-1519
    • Ewing, J.F.1    Maines, M.D.2
  • 7
    • 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., Mayer R.D., Ewing J.F., and McCoubrey Jr. W.K. 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 (1993) 457-462
    • (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
  • 8
    • 0031396912 scopus 로고    scopus 로고
    • Histochemical localization of heme oxygenase-2 protein and mRNA expression in rat brain
    • Ewing J.F., and Maines M.D. Histochemical localization of heme oxygenase-2 protein and mRNA expression in rat brain. Brain Res. Prot. 1 (1997) 165-174
    • (1997) Brain Res. Prot. , vol.1 , pp. 165-174
    • Ewing, J.F.1    Maines, M.D.2
  • 9
    • 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 (1997) 517-554
    • (1997) Annu. Rev. Pharmacol. Toxicol. , vol.37 , pp. 517-554
    • Maines, M.D.1
  • 11
    • 0023490534 scopus 로고
    • Inhibition of platelet aggregation by carbon monoxide is mediated by activation of guanylate cyclase
    • Brune B., and Ullrich V. Inhibition of platelet aggregation by carbon monoxide is mediated by activation of guanylate cyclase. Mol. Pharmacol. 32 (1987) 497-504
    • (1987) Mol. Pharmacol. , vol.32 , pp. 497-504
    • Brune, B.1    Ullrich, V.2
  • 12
    • 0024229085 scopus 로고
    • Vasodilating effects of carbon monoxide
    • Lin H., and McGrath J.J. Vasodilating effects of carbon monoxide. Drug Chem. Toxicol. 11 (1988) 371-385
    • (1988) Drug Chem. Toxicol. , vol.11 , pp. 371-385
    • Lin, H.1    McGrath, J.J.2
  • 14
    • 0027142920 scopus 로고
    • Nitric oxide synthase activity in pregnant rabbit uterus decreases on the last day of pregnancy
    • Sladek S.M., Regenestein A.C., Lykins D., and Roberts J.M. Nitric oxide synthase activity in pregnant rabbit uterus decreases on the last day of pregnancy. Am. J. Obstet. Gynecol. 169 (1993) 1285-1291
    • (1993) Am. J. Obstet. Gynecol. , vol.169 , pp. 1285-1291
    • Sladek, S.M.1    Regenestein, A.C.2    Lykins, D.3    Roberts, J.M.4
  • 15
    • 0028265735 scopus 로고
    • An l-arginine-nitric oxide-cyclic guanosine monophosphate system exists in the uterus and inhibits contractility during pregnancy
    • Yallampalli C., Izumi H., Byam-Smith M., and Garfield R.E. An l-arginine-nitric oxide-cyclic guanosine monophosphate system exists in the uterus and inhibits contractility during pregnancy. Am. J. Obstet. Gynecol. 170 (1993) 175-185
    • (1993) Am. J. Obstet. Gynecol. , vol.170 , pp. 175-185
    • Yallampalli, C.1    Izumi, H.2    Byam-Smith, M.3    Garfield, R.E.4
  • 17
    • 0034752069 scopus 로고    scopus 로고
    • Identification of heme oxygenase in human endometrium
    • Yoshiki N., Kubota T., and Aso T. Identification of heme oxygenase in human endometrium. J. Clin. Endocrinol. Metab. 86 (2001) 5033-5038
    • (2001) J. Clin. Endocrinol. Metab. , vol.86 , pp. 5033-5038
    • Yoshiki, N.1    Kubota, T.2    Aso, T.3
  • 18
    • 0032032945 scopus 로고    scopus 로고
    • Hemeoxygenase-1 inhibits human myometrial contractility via carbon monoxide and is upregulated by progesterone during pregnancy
    • Acevedo C.H., and Ahmed A. Hemeoxygenase-1 inhibits human myometrial contractility via carbon monoxide and is upregulated by progesterone during pregnancy. J. Clin. Invest. 101 5 (1998) 949-955
    • (1998) J. Clin. Invest. , vol.101 , Issue.5 , pp. 949-955
    • Acevedo, C.H.1    Ahmed, A.2
  • 19
    • 0028032449 scopus 로고
    • Pregnancy increases guanosine 3′,5′-monophosphate in the myometrium independent of nitric oxide synthesis
    • Weiner C.P., Knowles R.G., Nelson S.E., and Stegink L.D. Pregnancy increases guanosine 3′,5′-monophosphate in the myometrium independent of nitric oxide synthesis. Endocrinology 135 (1994) 2473-2478
    • (1994) Endocrinology , vol.135 , pp. 2473-2478
    • Weiner, C.P.1    Knowles, R.G.2    Nelson, S.E.3    Stegink, L.D.4
  • 20
    • 0030061289 scopus 로고    scopus 로고
    • Meloxicam: influence on arachidonic acid metabolism. Part II. In vivo findings
    • Engelhardt G., Bogel R., Schnitzlerc C., et al. Meloxicam: influence on arachidonic acid metabolism. Part II. In vivo findings. Biochem. Pharmacol. 51 (1996) 29-38
    • (1996) Biochem. Pharmacol. , vol.51 , pp. 29-38
    • Engelhardt, G.1    Bogel, R.2    Schnitzlerc, C.3
  • 21
    • 0034280755 scopus 로고    scopus 로고
    • Role of prostanoids and nitric oxide inhibition in rats with experimental hepatic fibrosis
    • Criado M., Flores O., Vazquez M.J., et al. Role of prostanoids and nitric oxide inhibition in rats with experimental hepatic fibrosis. J. Physiol. Biochem. 56 (2000) 181-188
    • (2000) J. Physiol. Biochem. , vol.56 , pp. 181-188
    • Criado, M.1    Flores, O.2    Vazquez, M.J.3
  • 23
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 24
    • 0342419503 scopus 로고    scopus 로고
    • Daily variations in cGMP, guanylate cyclase and phosphodiesterase in the golden hamster retina
    • Faillace M.P., Keller Sarmiento M.I., and Rosenstein R.E. Daily variations in cGMP, guanylate cyclase and phosphodiesterase in the golden hamster retina. Vision Res. 36 (1996) 1365-1369
    • (1996) Vision Res. , vol.36 , pp. 1365-1369
    • Faillace, M.P.1    Keller Sarmiento, M.I.2    Rosenstein, R.E.3
  • 25
    • 0018384650 scopus 로고
    • Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction
    • Ohkawa H., Ohishi N., and Yagi K. Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal. Biochem. 95 (1979) 351-358
    • (1979) Anal. Biochem. , vol.95 , pp. 351-358
    • Ohkawa, H.1    Ohishi, N.2    Yagi, K.3
  • 27
    • 0025281223 scopus 로고
    • Is bilirubin good for you?
    • McDonagh A.F. Is bilirubin good for you?. Clin. Perinatol. 17 (1990) 359-369
    • (1990) Clin. Perinatol. , vol.17 , pp. 359-369
    • McDonagh, A.F.1
  • 28
    • 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., Trakshel G.M., and Kutty R.K. Characterization of two constitutive forms of rat liver microsomal heme oxygenase: only one molecular species of the enzyme is inducible. J. Biol. Chem. 261 (1986) 411-419
    • (1986) J. Biol. Chem. , vol.261 , pp. 411-419
    • Maines, M.D.1    Trakshel, G.M.2    Kutty, R.K.3
  • 29
    • 0019883606 scopus 로고
    • Zinc protoporphyrin is a selective inhibitor of heme oxygenase activity in the neonatal rat
    • Maines M.D. Zinc protoporphyrin is a selective inhibitor of heme oxygenase activity in the neonatal rat. Biochim. Biophys. Acta 673 (1981) 339-350
    • (1981) Biochim. Biophys. Acta , vol.673 , pp. 339-350
    • Maines, M.D.1
  • 30
    • 0015193545 scopus 로고
    • Estrone and estradiol levels in the ovarian venous blood from rats during the estrous cycle and pregnancy
    • Shaikh A.A. Estrone and estradiol levels in the ovarian venous blood from rats during the estrous cycle and pregnancy. Biol. Reprod. 5 3 (1971) 297-307
    • (1971) Biol. Reprod. , vol.5 , Issue.3 , pp. 297-307
    • Shaikh, A.A.1
  • 33
    • 0016734908 scopus 로고
    • Plasma hormones and pituitary luteinizing hormone in the rat during the early stages of pregnancy and after post-coital treatment with tamoxifen (ICI 46,474)
    • Watson J., Anderson F.B., Alam M., O'Grady J.E., and Heald P.J. Plasma hormones and pituitary luteinizing hormone in the rat during the early stages of pregnancy and after post-coital treatment with tamoxifen (ICI 46,474). J. Endocrinol. 65 1 (1975) 7-17
    • (1975) J. Endocrinol. , vol.65 , Issue.1 , pp. 7-17
    • Watson, J.1    Anderson, F.B.2    Alam, M.3    O'Grady, J.E.4    Heald, P.J.5
  • 35
    • 4444350010 scopus 로고    scopus 로고
    • Biosynthesis and catabolism of prostaglandin F2alpha (PGF2alpha) are controlled by progesterone in the rat uterus during pregnancy
    • Farina M., Ribeiro M.L., Weissmann C., Estevez A., Billi S., Vercelli C., and Franchi A. Biosynthesis and catabolism of prostaglandin F2alpha (PGF2alpha) are controlled by progesterone in the rat uterus during pregnancy. J. Steroid. Biochem. Mol. Biol. 91 4/5 (2004) 211-218
    • (2004) J. Steroid. Biochem. Mol. Biol. , vol.91 , Issue.4-5 , pp. 211-218
    • Farina, M.1    Ribeiro, M.L.2    Weissmann, C.3    Estevez, A.4    Billi, S.5    Vercelli, C.6    Franchi, A.7
  • 37
    • 0141988655 scopus 로고    scopus 로고
    • Anti-inflammatory actions of the heme oxygenase-1 pathway
    • Alcaraz M.J., Fernandez P., and Guillen M.I. Anti-inflammatory actions of the heme oxygenase-1 pathway. Curr. Pharm. Des. 9 30 (2003) 2541-2551
    • (2003) Curr. Pharm. Des. , vol.9 , Issue.30 , pp. 2541-2551
    • Alcaraz, M.J.1    Fernandez, P.2    Guillen, M.I.3
  • 39
    • 0032888317 scopus 로고    scopus 로고
    • Hemoxygenase and nitric oxide synthase do not maintain human uterine quiescence during pregnancy
    • Barber A., Courtenay Robson S., and Lyall F. Hemoxygenase and nitric oxide synthase do not maintain human uterine quiescence during pregnancy. Am. J. Pathol. 155 3 (1999) 831-840
    • (1999) Am. J. Pathol. , vol.155 , Issue.3 , pp. 831-840
    • Barber, A.1    Courtenay Robson, S.2    Lyall, F.3


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