메뉴 건너뛰기




Volumn 49, Issue 10, 2010, Pages 1534-1541

Carbon monoxide-releasing molecule CORM-3 suppresses vascular endothelial cell SOD-1/SOD-2 activity while up-regulating the cell surface levels of SOD-3 in a heparin-dependent manner

Author keywords

Antioxidant enzymes; Cell culture; Free radicals; Heparin; Inflammation; Oxidative stress; Vascular endothelium

Indexed keywords

ANTIOXIDANT; CARBON MONOXIDE; CARBON MONOXIDE RELEASING MOLECULE 3; CARBONYL DERIVATIVE; COPPER ZINC SUPEROXIDE DISMUTASE; EXTRACELLULAR SUPEROXIDE DISMUTASE; HEPARIN; MANGANESE SUPEROXIDE DISMUTASE; OXIDOREDUCTASE; RUTHENIUM; UNCLASSIFIED DRUG;

EID: 77957753616     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2010.08.017     Document Type: Article
Times cited : (18)

References (46)
  • 2
    • 23044459608 scopus 로고    scopus 로고
    • Carbon monoxide-releasing molecules (CO-RMs) attenuate the inflammatory response elicited by lipopolysaccharide in RAW264.7 murine macrophages
    • Sawle P., Foresti R., Mann B.E., Johnson T.R., Green C.J., Motterlini R. Carbon monoxide-releasing molecules (CO-RMs) attenuate the inflammatory response elicited by lipopolysaccharide in RAW264.7 murine macrophages. Br. J. Pharmacol. 2005, 145:800-810.
    • (2005) Br. J. Pharmacol. , vol.145 , pp. 800-810
    • Sawle, P.1    Foresti, R.2    Mann, B.E.3    Johnson, T.R.4    Green, C.J.5    Motterlini, R.6
  • 3
    • 38349171767 scopus 로고    scopus 로고
    • Carbon monoxide liberated from carbon monoxide-releasing molecule CORM-2 attenuates inflammation in the liver of septic mice
    • Cepinskas G., Katada K., Bihari A., Potter R.F. Carbon monoxide liberated from carbon monoxide-releasing molecule CORM-2 attenuates inflammation in the liver of septic mice. Am. J. Physiol. 2008, 294:G184-G191.
    • (2008) Am. J. Physiol. , vol.294
    • Cepinskas, G.1    Katada, K.2    Bihari, A.3    Potter, R.F.4
  • 4
    • 38149008232 scopus 로고    scopus 로고
    • Heme oxygenase-1-derived carbon monoxide enhances the host defense response to microbial sepsis in mice
    • Chung S.W., Liu X., Macias A.A., Baron R.M., Perrella M.A. Heme oxygenase-1-derived carbon monoxide enhances the host defense response to microbial sepsis in mice. J. Clin. Invest. 2008, 118:239-247.
    • (2008) J. Clin. Invest. , vol.118 , pp. 239-247
    • Chung, S.W.1    Liu, X.2    Macias, A.A.3    Baron, R.M.4    Perrella, M.A.5
  • 6
    • 77952586011 scopus 로고    scopus 로고
    • Carbon monoxide liberated from CO-releasing molecule (CORM-2) attenuates ischemia/reperfusion (I/R)-induced inflammation in the small intestine
    • Katada K., Bihari A., Mizuguchi S., Yoshida N., Yoshikawa T., Fraser D.D., Potter R.F., Cepinskas G. Carbon monoxide liberated from CO-releasing molecule (CORM-2) attenuates ischemia/reperfusion (I/R)-induced inflammation in the small intestine. Inflammation 2010, 33:92-100.
    • (2010) Inflammation , vol.33 , pp. 92-100
    • Katada, K.1    Bihari, A.2    Mizuguchi, S.3    Yoshida, N.4    Yoshikawa, T.5    Fraser, D.D.6    Potter, R.F.7    Cepinskas, G.8
  • 7
    • 36749043642 scopus 로고    scopus 로고
    • Carbon monoxide-releasing molecules (CO-RMs): vasodilatory, anti-ischaemic and anti-inflammatory activities
    • Motterlini R. Carbon monoxide-releasing molecules (CO-RMs): vasodilatory, anti-ischaemic and anti-inflammatory activities. Biochem. Soc. Trans. 2007, 35:1142-1146.
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 1142-1146
    • Motterlini, R.1
  • 11
    • 61649124114 scopus 로고    scopus 로고
    • Water-soluble CO-releasing molecules reduce the development of postoperative ileus via modulation of MAPK/HO-1 signalling and reduction of oxidative stress
    • De Backer O., Elinck E., Blanckaert B., Leybaert L., Motterlini R., Lefebvre R.A. Water-soluble CO-releasing molecules reduce the development of postoperative ileus via modulation of MAPK/HO-1 signalling and reduction of oxidative stress. Gut 2009, 58:347-356.
    • (2009) Gut , vol.58 , pp. 347-356
    • De Backer, O.1    Elinck, E.2    Blanckaert, B.3    Leybaert, L.4    Motterlini, R.5    Lefebvre, R.A.6
  • 12
    • 1542314436 scopus 로고    scopus 로고
    • Carbon monoxide in biology and medicine
    • Ryter S.W., Otterbein L.E. Carbon monoxide in biology and medicine. Bioessays 2004, 26:270-280.
    • (2004) Bioessays , vol.26 , pp. 270-280
    • Ryter, S.W.1    Otterbein, L.E.2
  • 17
    • 67650462907 scopus 로고    scopus 로고
    • The evolution of carbon monoxide into medicine
    • Otterbein L.E. The evolution of carbon monoxide into medicine. Respir. Care 2009, 54:925-932.
    • (2009) Respir. Care , vol.54 , pp. 925-932
    • Otterbein, L.E.1
  • 18
    • 3943073829 scopus 로고    scopus 로고
    • Vascular protection: superoxide dismutase isoforms in the vessel wall
    • Faraci F.M., Didion S.P. Vascular protection: superoxide dismutase isoforms in the vessel wall. Arterioscler. Thromb. Vasc. Biol. 2004, 24:1367-1373.
    • (2004) Arterioscler. Thromb. Vasc. Biol. , vol.24 , pp. 1367-1373
    • Faraci, F.M.1    Didion, S.P.2
  • 19
    • 0036667555 scopus 로고    scopus 로고
    • Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression
    • Zelko I.N., Mariani T.J., Folz R.J. Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression. Free Radic. Biol. Med. 2002, 33:337-349.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 337-349
    • Zelko, I.N.1    Mariani, T.J.2    Folz, R.J.3
  • 20
    • 0034635133 scopus 로고    scopus 로고
    • Characterization of heparin binding of human extracellular superoxide dismutase
    • Lookene A., Stenlund P., Tibell L.A. Characterization of heparin binding of human extracellular superoxide dismutase. Biochemistry 2000, 39:230-236.
    • (2000) Biochemistry , vol.39 , pp. 230-236
    • Lookene, A.1    Stenlund, P.2    Tibell, L.A.3
  • 21
    • 0006157248 scopus 로고
    • Human copper-containing superoxide dismutase of high molecular weight
    • Marklund S.L. Human copper-containing superoxide dismutase of high molecular weight. Proc. Natl Acad. Sci. USA 1982, 79:7634-7638.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 7634-7638
    • Marklund, S.L.1
  • 22
    • 0036069786 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase and cardiovascular disease
    • Fukai T., Folz R.J., Landmesser U., Harrison D.G. Extracellular superoxide dismutase and cardiovascular disease. Cardiovasc. Res. 2002, 55:239-249.
    • (2002) Cardiovasc. Res. , vol.55 , pp. 239-249
    • Fukai, T.1    Folz, R.J.2    Landmesser, U.3    Harrison, D.G.4
  • 24
  • 25
    • 0037598583 scopus 로고    scopus 로고
    • PMN transendothelial migration decreases nuclear NFkappaB in IL-1beta-activated endothelial cells: role of PECAM-1
    • Cepinskas G., Savickiene J., Ionescu C.V., Kvietys P.R. PMN transendothelial migration decreases nuclear NFkappaB in IL-1beta-activated endothelial cells: role of PECAM-1. J. Cell Biol. 2003, 161:641-651.
    • (2003) J. Cell Biol. , vol.161 , pp. 641-651
    • Cepinskas, G.1    Savickiene, J.2    Ionescu, C.V.3    Kvietys, P.R.4
  • 27
    • 69249137126 scopus 로고    scopus 로고
    • Focus on carbon monoxide: a modulator of neutrophil oxidants and elastase spatial localization?
    • Ganta V.C., Alexander J.S. Focus on carbon monoxide: a modulator of neutrophil oxidants and elastase spatial localization?. Am. J. Physiol. Heart Circ. Physiol. 2009, 297:H902-H904.
    • (2009) Am. J. Physiol. Heart Circ. Physiol. , vol.297
    • Ganta, V.C.1    Alexander, J.S.2
  • 28
    • 21844468521 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain and NAD(P)H oxidase are targets for the antiproliferative effect of carbon monoxide in human airway smooth muscle
    • Taille C., El-Benna J., Lanone S., Boczkowski J., Motterlini R. Mitochondrial respiratory chain and NAD(P)H oxidase are targets for the antiproliferative effect of carbon monoxide in human airway smooth muscle. J. Biol. Chem. 2005, 280:25350-25360.
    • (2005) J. Biol. Chem. , vol.280 , pp. 25350-25360
    • Taille, C.1    El-Benna, J.2    Lanone, S.3    Boczkowski, J.4    Motterlini, R.5
  • 29
    • 33947628672 scopus 로고    scopus 로고
    • D'Avila, J. C.; Rao, J.; Billiar, T. R.; Otterbein, L. E. Carbon monoxide signals via inhibition of cytochrome c oxidase and generation of mitochondrial reactive oxygen species
    • Zuckerbraun B.S., Chin B.Y., Bilban M. d'Avila, J. C.; Rao, J.; Billiar, T. R.; Otterbein, L. E. Carbon monoxide signals via inhibition of cytochrome c oxidase and generation of mitochondrial reactive oxygen species. FASEB J. 2007, 21:1099-1106.
    • (2007) FASEB J. , vol.21 , pp. 1099-1106
    • Zuckerbraun, B.S.1    Chin, B.Y.2    Bilban, M.3
  • 30
    • 43349092136 scopus 로고    scopus 로고
    • Use of carbon monoxide as a therapeutic agent: promises and challenges
    • Foresti R., Bani-Hani M.G., Motterlini R. Use of carbon monoxide as a therapeutic agent: promises and challenges. Intens. Care Med. 2008, 34:649-658.
    • (2008) Intens. Care Med. , vol.34 , pp. 649-658
    • Foresti, R.1    Bani-Hani, M.G.2    Motterlini, R.3
  • 32
    • 48549090696 scopus 로고    scopus 로고
    • Carbon monoxide, reactive oxygen signaling, and oxidative stress
    • Piantadosi C.A. Carbon monoxide, reactive oxygen signaling, and oxidative stress. Free Radic. Biol. Med. 2008, 45:562-569.
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 562-569
    • Piantadosi, C.A.1
  • 34
    • 27744564577 scopus 로고    scopus 로고
    • Carbon monoxide reduces the expression and activity of matrix metalloproteinases 1 and 2 in alveolar epithelial cells
    • Desmard M., Amara N., Lanone S., Motterlini R., Boczkowski J. Carbon monoxide reduces the expression and activity of matrix metalloproteinases 1 and 2 in alveolar epithelial cells. Cell. Mol. Biol. (Noisy-le-Grand) 2005, 51:403-408.
    • (2005) Cell. Mol. Biol. (Noisy-le-Grand) , vol.51 , pp. 403-408
    • Desmard, M.1    Amara, N.2    Lanone, S.3    Motterlini, R.4    Boczkowski, J.5
  • 35
    • 0037131241 scopus 로고    scopus 로고
    • A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase
    • Doukov T.I., Iverson T.M., Seravalli J., Ragsdale S.W., Drennan C.L. A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Science 2002, 298:567-572.
    • (2002) Science , vol.298 , pp. 567-572
    • Doukov, T.I.1    Iverson, T.M.2    Seravalli, J.3    Ragsdale, S.W.4    Drennan, C.L.5
  • 36
    • 85140279476 scopus 로고    scopus 로고
    • Copper-carbon bonds in mechanistic and structural probing of proteins as well as in situations where copper is a catalytic or receptor site
    • Lucas H.R., Karlin K.D. Copper-carbon bonds in mechanistic and structural probing of proteins as well as in situations where copper is a catalytic or receptor site. Metal Ions Life Sci. 2009, 6:295-361.
    • (2009) Metal Ions Life Sci. , vol.6 , pp. 295-361
    • Lucas, H.R.1    Karlin, K.D.2
  • 37
    • 70349631632 scopus 로고    scopus 로고
    • Carbon monoxide and nitrogen monoxide ligand dynamics in synthetic heme and heme-copper complex systems
    • Lucas H.R., Meyer G.J., Karlin K.D. Carbon monoxide and nitrogen monoxide ligand dynamics in synthetic heme and heme-copper complex systems. J. Am. Chem. Soc. 2009, 131:13924-13925.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 13924-13925
    • Lucas, H.R.1    Meyer, G.J.2    Karlin, K.D.3
  • 39
    • 0029848789 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase: a regulator of nitric oxide bioavailability
    • Oury T.D., Day B.J., Crapo J.D. Extracellular superoxide dismutase: a regulator of nitric oxide bioavailability. Lab. Invest. 1996, 75:617-636.
    • (1996) Lab. Invest. , vol.75 , pp. 617-636
    • Oury, T.D.1    Day, B.J.2    Crapo, J.D.3
  • 40
    • 0021218456 scopus 로고
    • Extracellular superoxide dismutase and other superoxide dismutase isoenzymes in tissues from nine mammalian species
    • Marklund S.L. Extracellular superoxide dismutase and other superoxide dismutase isoenzymes in tissues from nine mammalian species. Biochem. J. 1984, 222:649-655.
    • (1984) Biochem. J. , vol.222 , pp. 649-655
    • Marklund, S.L.1
  • 41
    • 38049027217 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase (ecSOD) in vascular biology: an update on exogenous gene transfer and endogenous regulators of ecSOD
    • Qin Z., Reszka K.J., Fukai T., Weintraub N.L. Extracellular superoxide dismutase (ecSOD) in vascular biology: an update on exogenous gene transfer and endogenous regulators of ecSOD. Transl. Res. 2008, 151:68-78.
    • (2008) Transl. Res. , vol.151 , pp. 68-78
    • Qin, Z.1    Reszka, K.J.2    Fukai, T.3    Weintraub, N.L.4
  • 42
    • 0026667737 scopus 로고
    • The heparin-binding domain of extracellular superoxide dismutase C and formation of variants with reduced heparin affinity
    • Sandstrom J., Carlsson L., Marklund S.L., Edlund T. The heparin-binding domain of extracellular superoxide dismutase C and formation of variants with reduced heparin affinity. J. Biol. Chem. 1992, 267:18205-18209.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18205-18209
    • Sandstrom, J.1    Carlsson, L.2    Marklund, S.L.3    Edlund, T.4
  • 43
    • 0023109883 scopus 로고
    • Heparin-induced release of extracellular superoxide dismutase to human blood plasma
    • Karlsson K., Marklund S.L. Heparin-induced release of extracellular superoxide dismutase to human blood plasma. Biochem. J. 1987, 242:55-59.
    • (1987) Biochem. J. , vol.242 , pp. 55-59
    • Karlsson, K.1    Marklund, S.L.2
  • 44
    • 34347271912 scopus 로고    scopus 로고
    • The sulfate groups of chondroitin sulfate- and heparan sulfate-containing proteoglycans in neutrophil plasma membranes are novel binding sites for human leukocyte elastase and cathepsin G
    • Campbell E.J., Owen C.A. The sulfate groups of chondroitin sulfate- and heparan sulfate-containing proteoglycans in neutrophil plasma membranes are novel binding sites for human leukocyte elastase and cathepsin G. J. Biol. Chem. 2007, 282:14645-14654.
    • (2007) J. Biol. Chem. , vol.282 , pp. 14645-14654
    • Campbell, E.J.1    Owen, C.A.2
  • 45
    • 0032589128 scopus 로고    scopus 로고
    • Characterization of [3H]-heparin binding in human vascular smooth muscle cells and its relationship to the inhibition of DNA synthesis
    • Patel M.K., Refson J.S., Schachter M., Hughes A.D. Characterization of [3H]-heparin binding in human vascular smooth muscle cells and its relationship to the inhibition of DNA synthesis. Br. J. Pharmacol. 1999, 127:361-368.
    • (1999) Br. J. Pharmacol. , vol.127 , pp. 361-368
    • Patel, M.K.1    Refson, J.S.2    Schachter, M.3    Hughes, A.D.4
  • 46
    • 25444498833 scopus 로고    scopus 로고
    • Carbon monoxide inhibits superoxide dismutase and stimulates reactive oxygen species production by Desulfovibrio desulfuricans 1388
    • Davydova M.N., Tarasova N.B. Carbon monoxide inhibits superoxide dismutase and stimulates reactive oxygen species production by Desulfovibrio desulfuricans 1388. Anaerobe 2005, 11:335-338.
    • (2005) Anaerobe , vol.11 , pp. 335-338
    • Davydova, M.N.1    Tarasova, N.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.