메뉴 건너뛰기




Volumn 277, Issue 5 40-5, 1999, Pages

Carbon monoxide overproduced by heme oxygenase-1 causes a reduction of vascular resistance in perfused rat liver

Author keywords

Cytochrome P 450; Heat shock protein 32; Hemoglobin; Hepatic sinusoids; Methemoglobin

Indexed keywords

CARBON MONOXIDE; ENDOTHELIN 1; HEME OXYGENASE; HEMIN; LIPOSOME; METHEMOGLOBIN; NITRIC OXIDE; OXYHEMOGLOBIN;

EID: 18244420268     PISSN: 01931857     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpgi.1999.277.5.g1088     Document Type: Article
Times cited : (62)

References (42)
  • 2
    • 0029848180 scopus 로고    scopus 로고
    • Evidence for a functional link between stress response and vascular control in hepatic portal circulation
    • Gastrointest. Liver Physiol. 34
    • Bauer, M., B. H. J. Pannen, I. Bauer, C. Herzog, G. A. Wanner, R. Hanselmann, J. X. Zhang, M. G. Clemens, and R. Larsen. Evidence for a functional link between stress response and vascular control in hepatic portal circulation. Am. J. Physiol. 271 (Gastrointest. Liver Physiol. 34): G929-G935, 1996.
    • (1996) Am. J. Physiol. , vol.271
    • Bauer, M.1    Pannen, B.H.J.2    Bauer, I.3    Herzog, C.4    Wanner, G.A.5    Hanselmann, R.6    Zhang, J.X.7    Clemens, M.G.8    Larsen, R.9
  • 3
    • 0028052485 scopus 로고
    • ET-1 induced alterations of hepatic microcirculation: Sinusoidal and extrasinusoidal sites of action
    • Gastrointest. Liver Physiol. 30
    • Bauer, M., J. X. Zhang, and M. G. Clemens. ET-1 induced alterations of hepatic microcirculation: sinusoidal and extrasinusoidal sites of action. Am. J. Physiol. 267 (Gastrointest. Liver Physiol. 30): G143-G149, 1994.
    • (1994) Am. J. Physiol. , vol.267
    • Bauer, M.1    Zhang, J.X.2    Clemens, M.G.3
  • 4
    • 0023490534 scopus 로고
    • Inhibition of platelet aggregation by carbon monoxide mediated by activation of guanylate cyclase
    • Brüne, B., and V. Ullrich. Inhibition of platelet aggregation by carbon monoxide mediated by activation of guanylate cyclase. Mol. Pharmacol. 32: 497-504, 1987.
    • (1987) Mol. Pharmacol. , vol.32 , pp. 497-504
    • Brüne, B.1    Ullrich, V.2
  • 5
    • 0025953506 scopus 로고
    • Interleukin-1 and tumour necrosis factor induce hepatic haem oxygenase
    • Cantoni, L., C. Rossi, M. Rizzardini, M. Gadina, and P. Ghezzi. Interleukin-1 and tumour necrosis factor induce hepatic haem oxygenase. Biochem. J. 279: 891-894, 1991.
    • (1991) Biochem. J. , vol.279 , pp. 891-894
    • Cantoni, L.1    Rossi, C.2    Rizzardini, M.3    Gadina, M.4    Ghezzi, P.5
  • 6
    • 0030188587 scopus 로고    scopus 로고
    • Heme oxygenase-1: Function, regulation and implication of a novel stress-inducible protein in oxidant-induced lung injury
    • Choi, A. M. K., and J. Alam. Heme oxygenase-1: Function, regulation and implication of a novel stress-inducible protein in oxidant-induced lung injury. Am. J. Respir. Cell Mol. Biol. 15: 9-19, 1996.
    • (1996) Am. J. Respir. Cell Mol. Biol. , vol.15 , pp. 9-19
    • Choi, A.M.K.1    Alam, J.2
  • 8
    • 0021859552 scopus 로고
    • Hepatic heme metabolism and cytochrome P450 in cirrhotic rat liver
    • Farrell, G. C., and L. Zaluzny. Hepatic heme metabolism and cytochrome P450 in cirrhotic rat liver. Gastroenterology 89: 172-179, 1985.
    • (1985) Gastroenterology , vol.89 , pp. 172-179
    • Farrell, G.C.1    Zaluzny, L.2
  • 9
    • 0032991092 scopus 로고    scopus 로고
    • Increased heme oxygenase-1 gene expression in liver cells and splanchnic organs from portal hypertensive rats
    • Fernandez, M., and H. L. Bonkovsky. Increased heme oxygenase-1 gene expression in liver cells and splanchnic organs from portal hypertensive rats. Hepatology 29: 1672-1679, 1999.
    • (1999) Hepatology , vol.29 , pp. 1672-1679
    • Fernandez, M.1    Bonkovsky, H.L.2
  • 10
    • 0032005790 scopus 로고    scopus 로고
    • Distribution of heme oxygenase isoforms in rat liver: Topographic basis for carbon monoxide-mediated microvascular relaxation
    • Goda, N., K. Suzuki, M. Naito, S. Takeoka, E. Tsuchida, Y. Ishimura, T. Tamatani, and M. Suematsu. Distribution of heme oxygenase isoforms in rat liver: topographic basis for carbon monoxide-mediated microvascular relaxation. J. Clin. Invest. 101: 604-612, 1998.
    • (1998) J. Clin. Invest. , vol.101 , pp. 604-612
    • Goda, N.1    Suzuki, K.2    Naito, M.3    Takeoka, S.4    Tsuchida, E.5    Ishimura, Y.6    Tamatani, T.7    Suematsu, M.8
  • 11
    • 0031952913 scopus 로고    scopus 로고
    • Endothelin-1-induced vasoconstriction causes a significant increase in portal pressure of rat liver: Local constrictive effect on the distal segment of preterminal portal venules as revealed by light and electron microscopy and serial reconstruction
    • Kaneda, K., W. Ekataksin, M. Sogawa, A. Matsumura, A. Cho, and N. Kawada. Endothelin-1-induced vasoconstriction causes a significant increase in portal pressure of rat liver: local constrictive effect on the distal segment of preterminal portal venules as revealed by light and electron microscopy and serial reconstruction. Hepatology 27: 735-747, 1998.
    • (1998) Hepatology , vol.27 , pp. 735-747
    • Kaneda, K.1    Ekataksin, W.2    Sogawa, M.3    Matsumura, A.4    Cho, A.5    Kawada, N.6
  • 12
    • 0023835962 scopus 로고
    • Rat liver cytochrome P-450b, P-420b, and P-420c are degraded to biliverdin by heme oxygenase
    • Kutty, R. K., R. F. Daniel, D. E. Ryan, W. Levin, and M. D. Maines. Rat liver cytochrome P-450b, P-420b, and P-420c are degraded to biliverdin by heme oxygenase. Arch. Biochem. Biophys. 260: 638-644, 1988.
    • (1988) Arch. Biochem. Biophys. , vol.260 , pp. 638-644
    • Kutty, R.K.1    Daniel, R.F.2    Ryan, D.E.3    Levin, W.4    Maines, M.D.5
  • 14
    • 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
  • 15
    • 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
  • 16
    • 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 W.K., Jr.1    Huang, T.J.2    Maines, M.D.3
  • 17
    • 0033042822 scopus 로고    scopus 로고
    • Carbon monoxide-mediated alterations in paracellular permeability and vesicular transport in acetaminophen-treated perfused rat liver
    • Mori, M., M. Suematsu, T. Kyokane, T. Sano, H. Suzuki, T. Yamaguchi, Y. Ishimura, and H. Ishii. Carbon monoxide-mediated alterations in paracellular permeability and vesicular transport in acetaminophen-treated perfused rat liver. Hepatology 30: 160-168, 1999.
    • (1999) Hepatology , vol.30 , pp. 160-168
    • Mori, M.1    Suematsu, M.2    Kyokane, T.3    Sano, T.4    Suzuki, H.5    Yamaguchi, T.6    Ishimura, Y.7    Ishii, H.8
  • 18
    • 0018091233 scopus 로고
    • Filtration effect of endothelial fenestrations on chylomicron transport in neonatal rat liver sinusoids
    • Naito, M., and E. Wisse. Filtration effect of endothelial fenestrations on chylomicron transport in neonatal rat liver sinusoids. Cell Tissue Res. 190: 371-382, 1978.
    • (1978) Cell Tissue Res. , vol.190 , pp. 371-382
    • Naito, M.1    Wisse, E.2
  • 19
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsome
    • Omura, T., and R. Sato. The carbon monoxide-binding pigment of liver microsome. J. Biol. Chem. 239: 2370-2378, 1964.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 20
    • 0030886054 scopus 로고    scopus 로고
    • Reduced stress defense in heme oxygenase 1-deficient cells
    • Poss, K. D., and S. Tonegawa. Reduced stress defense in heme oxygenase 1-deficient cells. Proc. Natl. Acad. Sci. USA 94: 10925-10930, 1997.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10925-10930
    • Poss, K.D.1    Tonegawa, S.2
  • 21
    • 0028015605 scopus 로고
    • Carbon monoxide stimulates a potassium-selective current in rabbit corneal epithelial cells
    • Cell Physiol. 36
    • Rich, A., G. Farrugia, and J. L. Rae. Carbon monoxide stimulates a potassium-selective current in rabbit corneal epithelial cells. Am. J. Physiol. 267 (Cell Physiol. 36): C435-C442, 1994.
    • (1994) Am. J. Physiol. , vol.267
    • Rich, A.1    Farrugia, G.2    Rae, J.L.3
  • 22
    • 0029239607 scopus 로고
    • Histopathologic study following administration of liposome-encapsulated hemoglobin in the normovolemic rats
    • Rudolph, A. S., H. Spielberg, B. J. Spargo, and N. Kossovsky. Histopathologic study following administration of liposome-encapsulated hemoglobin in the normovolemic rats. J. Biomed. Mater. Res. 29: 189-196, 1995.
    • (1995) J. Biomed. Mater. Res. , vol.29 , pp. 189-196
    • Rudolph, A.S.1    Spielberg, H.2    Spargo, B.J.3    Kossovsky, N.4
  • 23
  • 24
    • 0027762222 scopus 로고
    • Purification of concentrated hemoglobin using organic solvent and heat treatment
    • Sakai, H., S. Takeoka, H. Yokohama, Y. Seino, H. Nishide, and Y. Tsuchida. Purification of concentrated hemoglobin using organic solvent and heat treatment. Prot. Exp. Pur. 4: 563-569, 1993.
    • (1993) Prot. Exp. Pur. , vol.4 , pp. 563-569
    • Sakai, H.1    Takeoka, S.2    Yokohama, H.3    Seino, Y.4    Nishide, H.5    Tsuchida, Y.6
  • 25
    • 0030957706 scopus 로고    scopus 로고
    • Endogenous carbon monoxide suppression stimulates bile acid-dependent biliary transport in perfused rat liver
    • Gastrointest. Liver Physiol 35
    • Sano, T., M. Shiomi, Y. Wakabayashi, Y. Shinoda, N. Goda, T. Yamaguchi, Y. Nimura, Y. Ishimura, and M. Suematsu. Endogenous carbon monoxide suppression stimulates bile acid-dependent biliary transport in perfused rat liver. Am. J. Physiol. 272 (Gastrointest. Liver Physiol 35): G1268-G1275, 1997.
    • (1997) Am. J. Physiol. , vol.272
    • Sano, T.1    Shiomi, M.2    Wakabayashi, Y.3    Shinoda, Y.4    Goda, N.5    Yamaguchi, T.6    Nimura, Y.7    Ishimura, Y.8    Suematsu, M.9
  • 26
    • 0026322363 scopus 로고
    • The basal and stimulated release of EDRF inhibits the contractions evoked by endothelin-1 and endothelin-3 in aortae of normotensive and spontaneously hypertensive rats
    • Schini, V. B., N. D. Kim, and P. M. Vanhoutte. The basal and stimulated release of EDRF inhibits the contractions evoked by endothelin-1 and endothelin-3 in aortae of normotensive and spontaneously hypertensive rats. J. Cardiovasc. Pharmacol. 17: S267-S271, 1991.
    • (1991) J. Cardiovasc. Pharmacol. , vol.17
    • Schini, V.B.1    Kim, N.D.2    Vanhoutte, P.M.3
  • 27
    • 0015143002 scopus 로고
    • Endotoxin-induced disseminated intravascular coagulation in nonpregnant rats. A new experimental model
    • Schoendorf, T. H., M. Rosenberg, and F. K. Beller. Endotoxin-induced disseminated intravascular coagulation in nonpregnant rats. A new experimental model. Am. J. Pathol. 65: 51-58, 1971.
    • (1971) Am. J. Pathol. , vol.65 , pp. 51-58
    • Schoendorf, T.H.1    Rosenberg, M.2    Beller, F.K.3
  • 29
    • 0031961808 scopus 로고    scopus 로고
    • Nitric oxide suppression reversibly attenuates mitochondrial dysfunction and cholestasis in endotoxemic rat liver
    • Shiomi, M., Y. Wakabayashi, T. Sano, Y. Shinoda, Y. Nimura, Y. Ishimura, and M. Suematsu. Nitric oxide suppression reversibly attenuates mitochondrial dysfunction and cholestasis in endotoxemic rat liver. Hepatology 27: 108-115, 1998.
    • (1998) Hepatology , vol.27 , pp. 108-115
    • Shiomi, M.1    Wakabayashi, Y.2    Sano, T.3    Shinoda, Y.4    Nimura, Y.5    Ishimura, Y.6    Suematsu, M.7
  • 30
    • 0344451735 scopus 로고
    • The conversion of hematin to bile pigment in the rat
    • Snyder, A. L., and R. Schmid. The conversion of hematin to bile pigment in the rat. J. Lab. Clin. Med. 65: 817-824, 1965.
    • (1965) J. Lab. Clin. Med. , vol.65 , pp. 817-824
    • Snyder, A.L.1    Schmid, R.2
  • 32
    • 0028856163 scopus 로고
    • Carbon monoxide: An endogenous modulator of sinusoidal tone in the perfused rat liver
    • Suematsu, M., N. Goda, T. Sano, S. Kashiwagi, Y. Shinoda, and Y. Ishimura. Carbon monoxide: an endogenous modulator of sinusoidal tone in the perfused rat liver. J. Clin. Invest. 96: 2431-2437, 1995.
    • (1995) J. Clin. Invest. , vol.96 , pp. 2431-2437
    • Suematsu, M.1    Goda, N.2    Sano, T.3    Kashiwagi, S.4    Shinoda, Y.5    Ishimura, Y.6
  • 34
    • 0028215277 scopus 로고
    • Endothelin-1 stimulates bile acid secretion and vesicular transport in the isolated perfused liver
    • Gastrointest. Liver Physiol. 29
    • Tanaka, A., K. Katagiri, M. Hoshino, T. Hayakawa, K. Tsukada, and T. Takeuchi. Endothelin-1 stimulates bile acid secretion and vesicular transport in the isolated perfused liver. Am. J. Physiol. 266 (Gastrointest. Liver Physiol. 29): G324-G329, 1994.
    • (1994) Am. J. Physiol. , vol.266
    • Tanaka, A.1    Katagiri, K.2    Hoshino, M.3    Hayakawa, T.4    Tsukada, K.5    Takeuchi, T.6
  • 35
    • 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
  • 37
    • 0021858187 scopus 로고
    • The liver sieve: Considerations concerning the structure and function of endothelial fenestrae, the sinusoidal wall and the space of Disse
    • Wisse, E., R. B. DeZanger, K. Charels, P. van der Smissen, and R. S. McCuskey. The liver sieve: considerations concerning the structure and function of endothelial fenestrae, the sinusoidal wall and the space of Disse. Hepatology 5: 683-692, 1985.
    • (1985) Hepatology , vol.5 , pp. 683-692
    • Wisse, E.1    Dezanger, R.B.2    Charels, K.3    Van Der Smissen, P.4    McCuskey, R.S.5
  • 38
    • 0022493183 scopus 로고
    • Incorporation of hemoglobin haem into the rat hepatic heamoproteins tryptophan pyrrolase and cytochrome P-450
    • Wyman, J. F., J. L. Gollan, W. Settle, G. C. Farrell, and M. A. Correia. Incorporation of hemoglobin haem into the rat hepatic heamoproteins tryptophan pyrrolase and cytochrome P-450. Biochem. J. 238: 837-846, 1986.
    • (1986) Biochem. J. , vol.238 , pp. 837-846
    • Wyman, J.F.1    Gollan, J.L.2    Settle, W.3    Farrell, G.C.4    Correia, M.A.5
  • 39
    • 0029162242 scopus 로고
    • Bilirubin is oxidized in rats treated with endotoxin and acts as a physiological antioxidant synergistically with ascorbic acid in vivo
    • Yamaguchi, T., F. Horio, T. Hashizume, M. Tanaka, S. Ikeda, A. Kakinuma, and H. Nakajima. Bilirubin is oxidized in rats treated with endotoxin and acts as a physiological antioxidant synergistically with ascorbic acid in vivo. Biochem. Biophys. Res. Commun. 214: 11-19, 1995.
    • (1995) Biochem. Biophys. Res. Commun. , vol.214 , pp. 11-19
    • Yamaguchi, T.1    Horio, F.2    Hashizume, T.3    Tanaka, M.4    Ikeda, S.5    Kakinuma, A.6    Nakajima, H.7
  • 40
  • 41
    • 0023756855 scopus 로고
    • Anti-bilirubin monoclonal antibody II. Enzyme-linked immunosorbent assay for bilirubin fractions by combination of two monoclonal antibodies
    • Yasuhara, I., M. Yamazaki, S. Shimizu, K. Shimizu, T. Yamaguchi, and H. Nakajima. Anti-bilirubin monoclonal antibody II. Enzyme-linked immunosorbent assay for bilirubin fractions by combination of two monoclonal antibodies. Biochim. Biophys. Acta 967: 261-266, 1988.
    • (1988) Biochim. Biophys. Acta , vol.967 , pp. 261-266
    • Yasuhara, I.1    Yamazaki, M.2    Shimizu, S.3    Shimizu, K.4    Yamaguchi, T.5    Nakajima, H.6
  • 42
    • 0018231096 scopus 로고
    • Reaction of the microsomal heme oxygenase with cobaltic protoporphyrin IX, an extremely poor substrate
    • Yoshida, T., and G. Kikuchi. Reaction of the microsomal heme oxygenase with cobaltic protoporphyrin IX, an extremely poor substrate. J. Biol. Chem. 253: 8479-8482, 1978.
    • (1978) J. Biol. Chem. , vol.253 , pp. 8479-8482
    • Yoshida, T.1    Kikuchi, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.