메뉴 건너뛰기




Volumn 61, Issue 2, 1997, Pages 136-142

New physiological importance of two classic residual products: Carbon monoxide and bilirubin

Author keywords

[No Author keywords available]

Indexed keywords

BILIRUBIN; CARBON MONOXIDE; NITRIC OXIDE;

EID: 0031214204     PISSN: 10773150     EISSN: None     Source Type: Journal    
DOI: 10.1006/bmme.1997.2610     Document Type: Article
Times cited : (70)

References (43)
  • 1
    • 0028928004 scopus 로고
    • Smooth muscle cell-derived carbon monoxide is a regulator of vascular cGMP
    • Morita T, Perrella M A, Lee M, Kourembanas S. Smooth muscle cell-derived carbon monoxide is a regulator of vascular cGMP. Proc Natl Acad Sci USA. 92:1995;1475-1479.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1475-1479
    • Morita, T.1    Perrella, M.A.2    Lee, M.3    Kourembanas, S.4
  • 3
    • 0030045835 scopus 로고    scopus 로고
    • Heme oxygenase: A novel target for the modulation of the inflamatory response
    • Willis D, Moore A R, Frederick R, Willoughby D A. Heme oxygenase: A novel target for the modulation of the inflamatory response. Nat Med USA. 2:1996;87-90.
    • (1996) Nat Med USA , vol.2 , pp. 87-90
    • Willis, D.1    Moore, A.R.2    Frederick, R.3    Willoughby, D.A.4
  • 4
    • 0027320610 scopus 로고
    • Free radicals in inflamation second messengers and mediators of tissue destruction
    • Winrow V R, Winyard P G, Morris C J, Blake D R. Free radicals in inflamation second messengers and mediators of tissue destruction. Br Med Bull. 40:1993;506-522.
    • (1993) Br Med Bull , vol.40 , pp. 506-522
    • Winrow, V.R.1    Winyard, P.G.2    Morris, C.J.3    Blake, D.R.4
  • 5
    • 0028293023 scopus 로고
    • Chromosomal localisation of the human heme oxygenase genes: Heme oxygenase (HMOX1) maps to chromosome 22q12 and heme oxygenase-2 (HMOX2) maps to chromosome 16p13.3
    • Kutty R K, Kutty G, Rodriguez I R, Chader G J, Wiggert B. Chromosomal localisation of the human heme oxygenase genes: Heme oxygenase (HMOX1) maps to chromosome 22q12 and heme oxygenase-2 (HMOX2) maps to chromosome 16p13.3. Genomics. 20:1994;513-516.
    • (1994) Genomics , vol.20 , pp. 513-516
    • Kutty, R.K.1    Kutty, G.2    Rodriguez, I.R.3    Chader, G.J.4    Wiggert, B.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, Alam J. Heme oxygenase-1: Function, regulation, and implication of a novel stress-inducible protein in oxidant-induced lung injury. Am J Respir Cell Mol Biol. 15:1996;9-19.
    • (1996) Am J Respir Cell Mol Biol , vol.15 , pp. 9-19
    • Choi, A.M.1    Alam, J.2
  • 7
    • 0030051948 scopus 로고    scopus 로고
    • Heme oxygenase-2: Endothelial and neuronal localization and role in endothelium-dependent relaxation
    • Zakhary, Gaine S P, Dinerman J L, Ruat M, Flavan N A, Snyder S H. Heme oxygenase-2: Endothelial and neuronal localization and role in endothelium-dependent relaxation. Proc Natl Acad Sci USA. 93:1996;795-798.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 795-798
    • Zakhary1    Gaine, S.P.2    Dinerman, J.L.3    Ruat, M.4    Flavan, N.A.5    Snyder, S.H.6
  • 8
    • 0029411321 scopus 로고
    • Parallel induction of heme oxygenase-1 and Chemoprotective phase 2 enzymes by electrophyles and antioxidants: Regulation by upstream antioxidant-responsive elements (AREs)
    • Prestera T, Talalay P, Alam J, Ahn Y I, Lee P J, Choi A M. Parallel induction of heme oxygenase-1 and Chemoprotective phase 2 enzymes by electrophyles and antioxidants: Regulation by upstream antioxidant-responsive elements (AREs). Mol Med. 1:1995;827-837.
    • (1995) Mol Med , vol.1 , pp. 827-837
    • Prestera, T.1    Talalay, P.2    Alam, J.3    Ahn, Y.I.4    Lee, P.J.5    Choi, A.M.6
  • 9
    • 0029880726 scopus 로고    scopus 로고
    • Differential regulation of cardiac heme oxygenase-1 and vascular endothelial growth factor mRNA expressions by hemin, heavy metals, heat shock and anoxia
    • Eyssen-Hernandez R, Ladoux A, Frelin C. Differential regulation of cardiac heme oxygenase-1 and vascular endothelial growth factor mRNA expressions by hemin, heavy metals, heat shock and anoxia. FEBS Lett. 382:1996;229-233.
    • (1996) FEBS Lett , vol.382 , pp. 229-233
    • Eyssen-Hernandez, R.1    Ladoux, A.2    Frelin, C.3
  • 10
    • 0027485237 scopus 로고
    • Induction of kidney heme oxygenase-1 (HSP32) mRNA and protein by ischemia/reperfusion: Possible role of heme as both promoter of tissue damage and regulator of HSP32
    • Maines M D, Mayer R D, Ewing, McCoubrey W K. Induction of kidney heme oxygenase-1 (HSP32) mRNA and protein by ischemia/reperfusion: Possible role of heme as both promoter 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    Ewing3    McCoubrey, W.K.4
  • 12
    • 0029162965 scopus 로고
    • Identification of a cis-regulatory element for delta 12-prostaglandin J2-induced expression of the rat heme oxygenase gene
    • Koizumi T, Odani N, Okuyama T, Ichikawa A, Negishi M. Identification of a cis-regulatory element for delta 12-prostaglandin J2-induced expression of the rat heme oxygenase gene. J Biol Chem. 270:1995;21779-21784.
    • (1995) J Biol Chem , vol.270 , pp. 21779-21784
    • Koizumi, T.1    Odani, N.2    Okuyama, T.3    Ichikawa, A.4    Negishi, M.5
  • 13
    • 0028989004 scopus 로고
    • Induction by prostaglandin A1 of haem oxygenase in myoblastic cells: An effect independent of expression of the 70 kDa het shock protein
    • Rossi A, Santoro M G. Induction by prostaglandin A1 of haem oxygenase in myoblastic cells: An effect independent of expression of the 70 kDa het shock protein. Biochem J. 308:1995;455-463.
    • (1995) Biochem J , vol.308 , pp. 455-463
    • Rossi, A.1    Santoro, M.G.2
  • 14
    • 0029410648 scopus 로고    scopus 로고
    • Hemoglobin provides protection against lethal endotoxemia in rats: The role of heme oxygenase-1
    • 601
    • L, Otterbein, S, L, Sylvester, 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.
    • Am J Respir Cell Mol Biol , vol.13 , pp. 595
    • Otterbein, L.1    Sylvester, S.L.2    Choi, A.M.3
  • 15
    • 0029135055 scopus 로고
    • Expression and modulatory effects of heme oxygenase in acute inflamation in the rat
    • Willis D. Expression and modulatory effects of heme oxygenase in acute inflamation in the rat. Inflamm Res. 44:1995;S218-220.
    • (1995) Inflamm Res , vol.44 , pp. 218-220
    • Willis, D.1
  • 16
    • 0029590042 scopus 로고
    • Direct demonstration of a physiological role for carbon monoxide in olfactor receptor neurons
    • Ingi T, Ronnet G V. Direct demonstration of a physiological role for carbon monoxide in olfactor receptor neurons. J Neurosci. 15:1995;8214-8222.
    • (1995) J Neurosci , vol.15 , pp. 8214-8222
    • Ingi, T.1    Ronnet, G.V.2
  • 17
    • 0030021905 scopus 로고    scopus 로고
    • Binding of NO and CO to soluble guanylate cyclase as observed with Resonance Raman Spectroscopy
    • Deinum G, Stone J R, Babcock G T, Marletta M A. Binding of NO and CO to soluble guanylate cyclase as observed with Resonance Raman Spectroscopy. Biochemistry. 35:1996;1540-1547.
    • (1996) Biochemistry , vol.35 , pp. 1540-1547
    • Deinum, G.1    Stone, J.R.2    Babcock, G.T.3    Marletta, M.A.4
  • 18
    • 0026643197 scopus 로고
    • NO, CO and OH endogenous soluble guanylyl cyclase-activating factors
    • Schmidt H HW. NO, CO and OH endogenous soluble guanylyl cyclase-activating factors. FEBS Lett. 307:1992;102-107.
    • (1992) FEBS Lett , vol.307 , pp. 102-107
    • Schmidt, H.H.W.1
  • 19
    • 0030476908 scopus 로고    scopus 로고
    • Sensitizing soluble guanylyl cyclase to become a highly CO-sensitive enzyme
    • Friebe A, Schultz G, Koesling D. Sensitizing soluble guanylyl cyclase to become a highly CO-sensitive enzyme. EMBO J. 15:1996;6863-6868.
    • (1996) EMBO J , vol.15 , pp. 6863-6868
    • Friebe, A.1    Schultz, G.2    Koesling, D.3
  • 20
    • 0028211791 scopus 로고
    • Inhibition of aldosterone release by hypoxiain vitro:
    • Raff H, Jankowski B. Inhibition of aldosterone release by hypoxiain vitro: J Appl Physiol. 76:1994;689-693.
    • (1994) J Appl Physiol , vol.76 , pp. 689-693
    • Raff, H.1    Jankowski, B.2
  • 22
    • 0027282347 scopus 로고
    • EPR characterization of molecular target for NO in mamalian cells and organelles
    • Henry J, Lepoivre M, Dropier J C, Ducrocq C, Boucher J L, Guissani A. EPR characterization of molecular target for NO in mamalian cells and organelles. FASEB J. 71:1993;1124-1134.
    • (1993) FASEB J , vol.71 , pp. 1124-1134
    • Henry, J.1    Lepoivre, M.2    Dropier, J.C.3    Ducrocq, C.4    Boucher, J.L.5    Guissani, A.6
  • 23
    • 0028362110 scopus 로고
    • Nitric oxide and carbon monoxide as possible retrograde messengers in hippocampal long-term potentiation
    • Hawkins R D, Zhuo M, Arancio O. Nitric oxide and carbon monoxide as possible retrograde messengers in hippocampal long-term potentiation. J Neurobiol. 25:1994;652-665.
    • (1994) J Neurobiol , vol.25 , pp. 652-665
    • Hawkins, R.D.1    Zhuo, M.2    Arancio, O.3
  • 24
    • 0028541213 scopus 로고
    • Heme oxygenase: The physiological role of one of its metabolites, carbon monoxide and interactions with zinc protoporphyrin, cobalt protpporphyrin and other metalloporphyrins
    • Marks G S. Heme oxygenase: The physiological role of one of its metabolites, carbon monoxide and interactions with zinc protoporphyrin, cobalt protpporphyrin and other metalloporphyrins. Cell Mol Biol. 40:1994;863-870.
    • (1994) Cell Mol Biol , vol.40 , pp. 863-870
    • Marks, G.S.1
  • 25
    • 0027971914 scopus 로고
    • Investigations of the possible role for carbon monoxide (CO) in thermal and mechanical hyperalgesia in the rat
    • Meller S T, Dykstra C L, Gebhart G F. Investigations of the possible role for carbon monoxide (CO) in thermal and mechanical hyperalgesia in the rat. Neuroreport. 5:1994;2337-2341.
    • (1994) Neuroreport , vol.5 , pp. 2337-2341
    • Meller, S.T.1    Dykstra, C.L.2    Gebhart, G.F.3
  • 26
    • 0028090560 scopus 로고
    • Carbon monoxide as anovel neuroendocrine modulator: Inhibition of stimulated corticotropin-releasing hormone release from acute rat hypotalamic explants
    • Pozzoli G, Mancuso C, Mirtella A, Preziosi P, Grossman A B, Navarra P. Carbon monoxide as anovel neuroendocrine modulator: Inhibition of stimulated corticotropin-releasing hormone release from acute rat hypotalamic explants. Endocrinology. 135:1994;2314-2317.
    • (1994) Endocrinology , vol.135 , pp. 2314-2317
    • Pozzoli, G.1    Mancuso, C.2    Mirtella, A.3    Preziosi, P.4    Grossman, A.B.5    Navarra, P.6
  • 27
    • 1042263983 scopus 로고    scopus 로고
    • Regulation of gonadotrophin-releasing hormone (GnRH) secretion by heme molecules: A regulatory role for carbon monoxide?
    • Lamar C A, Mahesh V B, Brann D W. Regulation of gonadotrophin-releasing hormone (GnRH) secretion by heme molecules: A regulatory role for carbon monoxide? Endocrinology. 137:1996;790-793.
    • (1996) Endocrinology , vol.137 , pp. 790-793
    • Lamar, C.A.1    Mahesh, V.B.2    Brann, D.W.3
  • 28
    • 0029880726 scopus 로고    scopus 로고
    • Differential regulation of cardiac HO 1 and vascular endothelial groth factor mRNA expressions by hemin, heavy metals, heat shock and anoxia
    • Eyssen-Hernandez R, Ladoux A, Frelin A. Differential regulation of cardiac HO 1 and vascular endothelial groth factor mRNA expressions by hemin, heavy metals, heat shock and anoxia. FEBS Lett. 382:1996;229-233.
    • (1996) FEBS Lett , vol.382 , pp. 229-233
    • Eyssen-Hernandez, R.1    Ladoux, A.2    Frelin, A.3
  • 29
    • 0030438722 scopus 로고    scopus 로고
    • Renal ischemia/reperfusion up-regulates heme oxygenase-1 (HSP32) expression and increase cGMP in rat heart
    • Raju V S, Maines M D. Renal ischemia/reperfusion up-regulates heme oxygenase-1 (HSP32) expression and increase cGMP in rat heart. J Pharmacol Exp Ther. 277:1996;1814-1822.
    • (1996) J Pharmacol Exp Ther , vol.277 , pp. 1814-1822
    • Raju, V.S.1    Maines, M.D.2
  • 30
    • 0028838293 scopus 로고    scopus 로고
    • Endothelial cell expression of vasoconstrictors and growth factors is regulated by smooth muscle cell-derived carbon monoxide
    • Morita T, Kourembanas S. Endothelial cell expression of vasoconstrictors and growth factors is regulated by smooth muscle cell-derived carbon monoxide. J Clin Invest. 96:1996;2676-2682.
    • (1996) J Clin Invest , vol.96 , pp. 2676-2682
    • Morita, T.1    Kourembanas, S.2
  • 31
    • 0028827709 scopus 로고
    • Evidence for a cyclic guanosine monophosphate-dependent, carbon monoxide-mediated, signaling system in the regulation of TNF-alpha production by human pulmonary macrophages
    • Arias-Diaz J, Vara E, Garcia C, Villa N, Balibrea J L. Evidence for a cyclic guanosine monophosphate-dependent, carbon monoxide-mediated, signaling system in the regulation of TNF-alpha production by human pulmonary macrophages. Arch Surg. 130:1995;1287-1293.
    • (1995) Arch Surg , vol.130 , pp. 1287-1293
    • Arias-Diaz, J.1    Vara, E.2    Garcia, C.3    Villa, N.4    Balibrea, J.L.5
  • 33
    • 0011112794 scopus 로고
    • Nitric oxide: A signalling and killer molecule
    • Dinu V, Gilca M. Nitric oxide: A signalling and killer molecule. Rev Roumaine Biochim. 31:1994;289-302.
    • (1994) Rev Roumaine Biochim , vol.31 , pp. 289-302
    • Dinu, V.1    Gilca, M.2
  • 34
    • 0027831570 scopus 로고
    • Effects of carbon monoxide on isolated heart muscle cells
    • Wittenberg B A, Wittenberg J B. Effects of carbon monoxide on isolated heart muscle cells. Res Rep Health Eff Inst. 62:1993;1-12.
    • (1993) Res Rep Health Eff Inst , vol.62 , pp. 1-12
    • Wittenberg, B.A.1    Wittenberg, J.B.2
  • 35
    • 0027176344 scopus 로고
    • Biliverdin reductase is heat resistant and coexpressed with constitutive and heat shock forms of heme oxygenase in brain
    • Ewing J F, Weber C M, Maines M D. Biliverdin reductase is heat resistant and coexpressed with constitutive and heat shock forms of heme oxygenase in brain. J Neurochem. 61:1993;1015-1023.
    • (1993) J Neurochem , vol.61 , pp. 1015-1023
    • Ewing, J.F.1    Weber, C.M.2    Maines, M.D.3
  • 37
    • 0023132858 scopus 로고
    • Bilirubin is an antioxidant of possible physiological importance
    • Stocker R, Yamato Y, Glazer A N, Ames B N. Bilirubin is an antioxidant of possible physiological importance. Science. 235:1987;1043-1046.
    • (1987) Science , vol.235 , pp. 1043-1046
    • Stocker, R.1    Yamato, Y.2    Glazer, A.N.3    Ames, B.N.4
  • 39
    • 0027948692 scopus 로고
    • Structural basis of antimutagenicity of chemicals towards 4-nitroquinoline-1-oxide in Salmonella typhimurium
    • De Flora S, Rosenkrantz H S, Klopman S. Structural basis of antimutagenicity of chemicals towards 4-nitroquinoline-1-oxide in Salmonella typhimurium. Mutagenesis. 9:1994;39-45.
    • (1994) Mutagenesis , vol.9 , pp. 39-45
    • De Flora, S.1    Rosenkrantz, H.S.2    Klopman, S.3
  • 40
    • 0027490428 scopus 로고
    • Bilirubin attenuates radical-mediated damage to serum albumin
    • Neuzil J, Stocker R. Bilirubin attenuates radical-mediated damage to serum albumin. FEBS Lett. 331:1993;281-284.
    • (1993) FEBS Lett , vol.331 , pp. 281-284
    • Neuzil, J.1    Stocker, R.2
  • 41
    • 0026235894 scopus 로고
    • Albumin-bound bilirubins protect human ventricular myocytes against oxyradical damage
    • Wu T W, Wu J, Li R K, Mickle D, Carey D. Albumin-bound bilirubins protect human ventricular myocytes against oxyradical damage. Biochem Cell Biol. 69:1991;638-688.
    • (1991) Biochem Cell Biol , vol.69 , pp. 638-688
    • Wu, T.W.1    Wu, J.2    Li, R.K.3    Mickle, D.4    Carey, D.5
  • 42
    • 0026542512 scopus 로고
    • Normal and heat-induced patterns of expression of heme oxygenase-1 (HSP32) in rat brain: Hyperthrmia causes rapid induction of mRNA and protein
    • Ewing J F, Haber S N, Maines M D. Normal and heat-induced patterns of expression of heme oxygenase-1 (HSP32) in rat brain: Hyperthrmia 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
  • 43
    • 0027452195 scopus 로고
    • A beneficial role of bile pigments as an endogenous tissue protector: Anti-complement effects of biliverdin and conjugated bilirubin
    • Nagakami T, Toyomura K, Kinoshita T, Morisawa S. A beneficial role of bile pigments as an endogenous tissue protector: anti-complement effects of biliverdin and conjugated bilirubin. Biochim Biophys Acta. 1158:1993;189-193.
    • (1993) Biochim Biophys Acta , vol.1158 , pp. 189-193
    • Nagakami, T.1    Toyomura, K.2    Kinoshita, T.3    Morisawa, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.