Bilirubin: Its role in cytoprotection against oxidative stress
Bilirubin, the end product of heme catabolism in mammals, is generally regarded as a potentially cytotoxic, lipid-soluble waste product that needs to be excreted. However, in the last 10 years, in vitro and in vivo studies, have demonstrated that bilirubin exhibits potent anti-oxidant properties pre...
Guardado en:
| Autor principal: | |
|---|---|
| Otros Autores: | |
| Formato: | Capítulo de libro |
| Lenguaje: | Inglés |
| Publicado: |
Elsevier Ltd
2002
|
| Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
| Aporte de: | Registro referencial: Solicitar el recurso aquí |
| LEADER | 08272caa a22008417a 4500 | ||
|---|---|---|---|
| 001 | PAPER-5432 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518203504.0 | ||
| 008 | 190411s2002 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-0036179681 | |
| 024 | 7 | |2 cas |a bilirubin, 18422-02-1, 635-65-4 | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a IJBBF | ||
| 100 | 1 | |a Tomaro, M.L. | |
| 245 | 1 | 0 | |a Bilirubin: Its role in cytoprotection against oxidative stress |
| 260 | |b Elsevier Ltd |c 2002 | ||
| 270 | 1 | 0 | |m Tomaro, M.L.; Departamento de Quimica Biologica, Facultad de Farmacia y Bioquimica, Universidad de Buenos Aires, Junin 956, 1113 Buenos Aires, Argentina; email: ptomaro@ffyb.uba.ar |
| 506 | |2 openaire |e Política editorial | ||
| 504 | |a Maines, M.D., Traskhel, G.M., Kutty, R.K., Characterization of two constitutive forms of rat microsomal heme oxygenase: Only one molecular species of the enzyme is inducible (1986) J. Biol. Chem., 261, pp. 411-419 | ||
| 504 | |a McCoubry, W.J., Huang, T.J., Maines, M.D., Isolation and characterization of a cDNA from rat brain that encodes hemoprotein heme oxygenase-3 (1997) Eur. J. Biochem., 247, pp. 725-732 | ||
| 504 | |a Tomaro, M.L., Frydman, J., Frydman, R.B., Heme oxygenase induction by CoCl2, Co-protoporphyrin IX, phenylhydrazine, and diamide: Evidence for oxidative stress involvement (1991) Arch. Biochem. Biophys., 226, pp. 610-617 | ||
| 504 | |a Keyse, S.M., 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 (1989) Proc. Natl. Acad. Sci. U.S.A., 86, pp. 99-103 | ||
| 504 | |a Clark, J.E., Foresti, R., Sarathchandra, P., Kaur, H., Green, C., Motterlini, R., Heme oxygenase-1-derived bilirubin ameliorates postischemic myocardiual dysfunction (2000) Am. J. Physiol. Heart. Circ. Physiol., 278, pp. H643-H651 | ||
| 504 | |a Abraham, N.G., Drummed, G.S., Lutton, J.D., Kappas, A., The biological significance and physiological role of heme oxygenase (1996) Cell Physiol. Biochem., 6, pp. 129-168 | ||
| 504 | |a Maines, M.D., Kappas, A., Cobalt induction of hepatic heme oxygenase, with evidence that cytochrome P-450 is not essential for this enzyme activity (1974) Proc. Natl. Acad. Sci. U.S.A., 71, pp. 4293-4297 | ||
| 504 | |a Lane, N.J., Blood ties - A family of molecules with an unsavoury reputation could aid victims of conditions as diverse as heart disease, malaria and cancer (1998) Science, 280, pp. 24-29 | ||
| 504 | |a Bernard, K., Ritzel, G., Steiner, K.U., Uber eine biologische bedeuting der gallenfarbstoffe: Bilirubin und biliverdin als antioxidantien fur das vitamin A nd die essentiellen fettsauren (1954) Helv. Chim. Acta, 37, pp. 306-313 | ||
| 504 | |a Stocker, R., Yamamoto, Y., Mc Donagh, A.F., Glazer, A.N., Ames, B.N., Bilirubin is an antioxidant of possible physiological importance (1987) Science, 235, pp. 1043-1046 | ||
| 504 | |a Llesuy, S.F., Tomaro, M.L., Heme oxygenase and oxidative stress: Evidence of involvement of bilirubin as physiological protector against oxidative damage (1994) Biochim. Biophys. Acta, 1223, pp. 9-14 | ||
| 504 | |a Ossola, J.O., Tomaro, M.L., Heme oxygenase induction by cadmium chloride: Evidence for oxidative stress involvement (1995) Toxicology, 104, pp. 141-147 | ||
| 504 | |a Ossola, J.O., Tomaro, M.L., Heme oxygenase induction by UVA radiation: A response to oxidative stress in rat liver (1998) Int. J. Biochem. Cell Biol., 30, pp. 285-292 | ||
| 504 | |a Ossola, J.O., Groppa, M.D., Tomaro, M.L., Relationship between oxidative stress and heme oxygenase induction by copper sulfate (1997) Arch. Biochem. Biophys., 337 (2), pp. 332-337 | ||
| 504 | |a Ossola, J.O., Kristoff, G., Tomaro, M.L., Heme oxygenase induction by menadione bisulfite adduct-generated oxidative stress in rat liver (2000) Comp. Biochem. Phys., 127, pp. 91-99 | ||
| 504 | |a Noriega, G.O., Ossola, J.O., Tomaro, M.L., Del Batlle, A.M.C., Effect of acetaminophen on heme metabolism in rat liver (2000) Int. J. Biochem. Cell Biol., 32, pp. 983-991 | ||
| 504 | |a Clark, J.E., Foresti, R., Green, C.J., Motterlini, R., Dynamics of heme oxygenase-1 expression and bilirubin production in cellular protection against oxidative stress (2000) Biochem. J., 348, pp. 615-619 | ||
| 504 | |a Doré, S., Takahashi, M., Ferris, C.D., Hester, L.D., Guastella, D., Snyder, S.H., Bilirubin, formed by activation of heme oxygenase-2, protects neurons against oxidative stress injury (1999) Proc. Nat. Acad. Sci. U.S.A., 96, pp. 2445-2450 | ||
| 504 | |a Yachie, A., Niida, Y., Wada, T., Igarashi, N., Kaneda, H., Toma, T., Ohta, K., Koizumi, S., Oxidative stress causes enhanced endothelial cell injury in human heme-oxygenase-1 deficiency (1999) J. Clin. Invest., 103, pp. 129-135 | ||
| 504 | |a Oren, D., Bilirubin REM sleep and phototransduction of environmental time cues: A hypothesis (1997) Chronobiol. Intl., 14, pp. 319-329 | ||
| 504 | |a Ryter, S.W., Tyrrell, R.M., The heme synthesis and degradation pathways: Role in oxidant sensitivity (2000) Free Rad. Biol. Med., 28, pp. 289-309 | ||
| 504 | |a Matz, P., Turner, C., Weinstein, P.R., Massa, S.M., Panter, S.S., Sharp, F.R., Heme oxygenase-1 induction in glia throughout rat brain following experimental subarachnoid hemorrhage (1996) Brain Res., 713, pp. 211-222 | ||
| 520 | 3 | |a Bilirubin, the end product of heme catabolism in mammals, is generally regarded as a potentially cytotoxic, lipid-soluble waste product that needs to be excreted. However, in the last 10 years, in vitro and in vivo studies, have demonstrated that bilirubin exhibits potent anti-oxidant properties preventing the oxidative damage triggered by a wide range of oxidant-related stimuli. Therefore, the idea of a beneficial and physiological role for bilirubin in cytoprotection against short and long-lasting oxidant-mediated cell injury is highlighted here. © 2002 Elsevier Science Ltd. All rights reserved. |l eng | |
| 536 | |a Detalles de la financiación: Universidad de Buenos Aires | ||
| 536 | |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas | ||
| 536 | |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas | ||
| 536 | |a Detalles de la financiación: Studies were supported by grants from the Universidad de Buenos Aires (Argentina) and the Consejo Nacional de Investigaciones Cientı́ficas y Técnicas (CONICET) (Argentina), MLT and AB are members of the Career of Scientific Researcher at the CONICET. | ||
| 593 | |a Departamento De Química Biológica, Facultad De Farmacia Y Bioquímica, Universidad De Buenos Aires, Junín 956, 1113 Buenos Aires, Argentina | ||
| 593 | |a Centro De Investigaciones Sobre Porfirinas Y Porfirias (CIPYP), CONICET-Facultad De Ciencias Exactas Y Naturales, Universidad De Buenos Aires, Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a ANTI-OXIDANT DEFENSES |
| 690 | 1 | 0 | |a BILIRUBIN |
| 690 | 1 | 0 | |a HEME CATABOLISM |
| 690 | 1 | 0 | |a HEME OXYGENASE |
| 690 | 1 | 0 | |a OXIDATIVE STRESS |
| 690 | 1 | 0 | |a BILIRUBIN |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a CATABOLISM |
| 690 | 1 | 0 | |a CELL DAMAGE |
| 690 | 1 | 0 | |a CELL PROTECTION |
| 690 | 1 | 0 | |a CHEMICAL STRUCTURE |
| 690 | 1 | 0 | |a HUMAN |
| 690 | 1 | 0 | |a MAMMAL |
| 690 | 1 | 0 | |a OXIDATION |
| 690 | 1 | 0 | |a OXIDATIVE STRESS |
| 690 | 1 | 0 | |a PHYSIOLOGY |
| 690 | 1 | 0 | |a MAMMALIA |
| 700 | 1 | |a Batlle, A.M.D.C. | |
| 773 | 0 | |d Elsevier Ltd, 2002 |g v. 34 |h pp. 216-220 |k n. 3 |p Int. J. Biochem. Cell Biol. |x 13572725 |w (AR-BaUEN)CENRE-5218 |t International Journal of Biochemistry and Cell Biology | |
| 856 | 4 | 1 | |u https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036179681&doi=10.1016%2fS1357-2725%2801%2900130-3&partnerID=40&md5=f94750e4c5b2942330cb3a1fb0da1732 |y Registro en Scopus |
| 856 | 4 | 0 | |u https://doi.org/10.1016/S1357-2725(01)00130-3 |y DOI |
| 856 | 4 | 0 | |u https://hdl.handle.net/20.500.12110/paper_13572725_v34_n3_p216_Tomaro |y Handle |
| 856 | 4 | 0 | |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13572725_v34_n3_p216_Tomaro |y Registro en la Biblioteca Digital |
| 961 | |a paper_13572725_v34_n3_p216_Tomaro |b paper |c PE | ||
| 962 | |a info:eu-repo/semantics/article |a info:ar-repo/semantics/artículo |b info:eu-repo/semantics/publishedVersion | ||
| 999 | |c 66385 | ||