How does hexachlorobenzene treatment affect liver uroporphyrinogen decarboxylase?

The aims of the present work were: (1) to investigate whether the strong decrease of liver uroporphyrinogen decarboxylase (UroD) activity observed in experimental porphyria cutanea tarda is due to alteration of the enzymatic protein and (2) to improve the knowledge about the normal liver enzyme. Wit...

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Detalles Bibliográficos
Autor principal: Chaufan, G.
Otros Autores: Ríos de Molina, María del Carmen, San Martín de Viale, L.C
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 2001
Materias:
PH
Acceso en línea:Registro en Scopus
DOI
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Registro en la Biblioteca Digital
Aporte de:Registro referencial: Solicitar el recurso aquí
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024 7 |2 scopus  |a 2-s2.0-0034990683 
024 7 |2 cas  |a Antigens; Fungicides, Industrial; Hexachlorobenzene, 118-74-1; Uroporphyrinogen Decarboxylase, EC 4.1.1.37 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a IJBBF 
100 1 |a Chaufan, G. 
245 1 4 |a How does hexachlorobenzene treatment affect liver uroporphyrinogen decarboxylase? 
260 |c 2001 
270 1 0 |m San Martín de Viale, L.C.; Departamento de Quimica Biologica, Fac. de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina; email: smartin@qb.fcen.uba.ar 
506 |2 openaire  |e Política editorial 
504 |a Mauzerall, D., Granick, S., Porphyrin biosynthesis in erythrocytes. Uroporphyrinogen and its decarboxylase (1958) J. Biol. Chem., 232, pp. 1141-1162 
504 |a San Martín de Viale, L.C., Ríos de Molina, M.C., Wainstok de Calmanovici, R., Tomio, J.M., Porphyrins and porphyrinogen carboxylyase in hexachlorobenzene-induced porphyria (1977) Biochem. J., 168, pp. 393-400 
504 |a De Salamanca, R.E., Batlle, A.M.D.C., Chinarro, S., Stella, A.M., Wider, E.A., Estudio comparativo de la Porfiria Experimental inducida por hexaclorobenceno y la Porfiria cutánea Tardía Humana (1985) An. Med. Int., 2, pp. 319-329 
504 |a Elder, G.H., Porphyria cutanea tarda (1998) Semin. Liver Dis., 18, pp. 67-75 
504 |a García, R.C., San Martín de Viale, L.C., Tomio, M.J., Grinstein, M., Porphyrin biosynthesis. Porphyrinogen carboxy-lyase from avian erythrocytes. Further properties (1973) Biochem. Biophys. Acta, 209, pp. 203-210 
504 |a Tomio, J.M., García, R.C., San Martín de Viale, L.C., Grinstein, M., Porphyrin biosynthesis. Porphyrinogen carboxy-lyase from avian erythrocytes. Purification and properties (1970) Biochem. Biophys. Acta, 198, pp. 353-363 
504 |a De Verneuil, H., Grandchamp, B., Nordmann, Y., Some kinetic properties of human red cell uroporphyrinogen decarboxylase (1980) Biochem. Biophys. Acta, 611, pp. 174-186 
504 |a Straka, J.G., Kushner, J.P., Purification and characterization of bovine hepatic uroporphyrinogen decarboxylase (1983) Biochemistry, 22, pp. 4664-4672 
504 |a Ríos de Molina, M.C., Billi, S.C., San Martín de Viale, L.M., Does feeding of hexachlorobenzene promote structural changes in rat-liver porphyrinogen carboxy-lyase? (1986) Hexachlorobenzene Proceeding of an International Symposium, 77, pp. 481-486. , IARC Scientific Publications 
504 |a Billi de Catabbi, S., Ríos de Molina, M.C., San Martín de Viale, L.C., Studies on the active center of rat liver porphyrinogen carboxy-lyase in-vivo effect of hexachlorobenzene (1991) Int. J. Biochem., 23, pp. 675-679 
504 |a Kawanishi, S., Seki, Y., Sano, S., Uroporphyrinogen decarboxylase. Purification, properties and inhibition by polychlorinated biphenyl isomers (1983) J. Biol. Chem., 258, pp. 4285-4292 
504 |a Elder, G.H., Tovey, J.A., Sheppard, D.M., Purification of uroporphyrinogen decarboxylase from human erythrocytes (1983) Biochem. J., 215, pp. 46-55 
504 |a Koopman, G.E., Juknat de Geralnik, A.A., Batlle, A.M.D.C., Porphyrin biosynthesis in Rhodopseudomonas palustris - V. Purification of porphyrinogen decarboxylase and some unusual properties (1986) Int. J. Biochem., 18, pp. 935-944 
504 |a Wyckoff, E.E., Phillips, D.J., Sowa, A.M., Franklin, M.R., Kushner, J.P., Mutational analysis of human uroporphyrinogen decarboxylase (1996) Biochem. Biophys. Acta, 1298, pp. 194-204 
504 |a Franklin, M.R., Phillips, J.D., Kushner, J.P., Cytochrome P450 induction, uroporphyrinogen decarboxylase depression, porphyrins accumulation and excretion, and gender influence in a 3-week rat model of Porphyria Cutanea Tarda (1997) Toxicol. Appl. Pharmacol., 147, pp. 289-299 
504 |a Ríos de Molina, M.C., Wainstok de Calmanovici, R., San Martín de Viale, L.C., Investigation of the presence of porphyrinogen carboxy-lyase inhibitor in liver rats intoxicated with hexachlorobenzene (1980) Int. J. Biochem., 12, pp. 1027-1032 
504 |a Cantoni, L., Dal Fiume, D., Ruggieri, R., Decarboxylation of uroporphyrinogen I and III in 2,3,7,8-tetrachlorodibenzo-p-dioxin induced porphyria in mice (1984) Int. J. Biochem., 16, pp. 561-565 
504 |a Smith, A.G., Francis, J.E., Chemically induced formation of an inhibitor of hepatic uroporphyrinogen decarboxylase in inbred mice with an iron overload (1987) Biochem. J., 246, pp. 221-226 
504 |a Francis, J.E., Smith, A.G., Oxidation of uroporphyrinogen by hydroxyl radicals. Evidence of non porphyrin products as potential inhibitors of uroporphyrinogen decarboxylase (1988) FEBS Lett., 233, pp. 311-314 
504 |a De Mateis, F., Harvey, C., Reed, C., Hempenius, R., Increased oxidation of uroporphyrinogen by an inducible liver microsomal system (1988) Biochem. J., 250, pp. 161-169 
504 |a Lambrecht, R.W., Jacobs, J.M., Sinclair, P.R., Sinclair, J.F., Inhibition of uroporphyrinogen decarboxylase activity. The role of cytochrome P-450 mediated uroporphyrinogen oxidation (1990) Biochem. J., 269, pp. 437-441 
504 |a Billi de Catabbi, S., Wainstok de Calmanovici, R., Minutolo, C., Aldonatti, C., San Martín de Viale, L.C., Porphyria induced hepatic porphyrinogen carboxy-lyase inhibitor and its interaction with the active site (s) of the enzyme (1999) Biochem. Mol. Biol. Int., 47, pp. 945-956 
504 |a Hindmarsh, J.T., Enzyme heterogeneity in the porphyrias (1990) Clin. Biochem., 23, pp. 371-374 
504 |a Mylchreest, E., Charbonneau, M., Studies on the mechanism of uroporphyrinogen decarboxylase inhibition in hexachlorobenzene-induced porphyria in the female rat (1997) Toxicol. Appl. Pharmacol., 145, pp. 23-33 
504 |a De Verneuil, H., Sassa, S., Kappas, A., Purification and properties of uroporphyrinogen decarboxylase from human erythrocytes. A single enzyme catalyzing the four sequential decarboxylations of uroporphyrinogen I and III (1983) J. Biol. Chem., 258, pp. 2454-2460 
504 |a Mukerji, S.K., Pimstone, N.R., Uroporphyrinogen decarboxylase from human erythrocytes: Purification, complete separation and partial characterization of two isoenzymes (1992) Int. J. Biochem., 24, pp. 105-119 
504 |a Phillips, J.D., Whitby, F.G., Kushner, J.P., Hill, C.P., Characterization and crystallization of human uroporphyrinogen decarboxylase (1997) Prot. Sci., 6, pp. 1343-1346 
504 |a Ríos de Molina, M.C., Chaufan, G., Iglesias, S., Billi de Catabbi, S., San Martín de Viale, L.C., Porphyrinogen carboxylase. Studies on the existence of isoenzymes (1996) Acta Physiol. Pharmacol. Ther. Latinoam., 46, pp. 265-275 
504 |a Bradford, M.M., A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal. Biochem., 72, pp. 248-254 
504 |a Billi de Catabbi, S., San Martín de Viale, L.C., Studies on the active center(s) of rat liver porphyrinogen carboxy-lyase. In-vivo effect of hexachlorobenzene on decarboxylation site(s) of porphyrinogens (1994) Int. J. Biochem., 26, pp. 595-600 
504 |a Elder, G.H., Sheppard, D.M., Immunoreactive uroporphyrinogen decarboxylase is unchanged in porphyria caused by TCDD and hexachlorobenzene (1982) Biochem. Biophys. Res. Commun., 109, pp. 113-120 
520 3 |a The aims of the present work were: (1) to investigate whether the strong decrease of liver uroporphyrinogen decarboxylase (UroD) activity observed in experimental porphyria cutanea tarda is due to alteration of the enzymatic protein and (2) to improve the knowledge about the normal liver enzyme. With these purposes, several physicochemical studies for enzymatic characterization were carried out comparatively on the 12-fold purified liver enzyme of both normal and hexachlorobenzene porphyric rat. The study shows that the enzyme from porphyric rats has a higher activation energy, lower reactivity index and lower optimum pH than the normal one. In addition, it did not reach the Vmax at any of the substrate concentrations assayed (up to 28 μM uroporphyrinogen III), while the normal enzyme reached the plateau around 14 μM. The porphyric enzyme appears to be more protected than the normal against the inhibitory action of several metals, particularly Cu2+ and Pb2+, and against thermal inactivation. Zn2+ did not affect enzymatic activity, whereas Cu2+, Hg2+, Fe2+, Pb2+, and Cd2+ lowered the activities of both normal and porphyric enzyme in a dose-related way. It was also observed that the larger the atomic radius in its hydrated state, the lower the effect of the metal. Neither glutathione nor dithiothreitol significantly altered enzymatic activity in the range of concentrations assayed. β-Mercaptoethanol had diverse effects, as regards both the concentration assayed and the enzymatic sample used. Assays with cystine showed a dual behaviour of both normal and porphyric enzymatic activity. Western blots for both preparations revealed a single band (65 kDa) with a similar intensity. This study show that hexachlorobenzene treatment modifies the physicochemical properties of liver UroD leading to a sharp decrease of its activity, without affecting its antigenic reactivity probably as a consequence of changes at the conformational level promoted by the binding of its reported inhibitor. © 2001 Elsevier Science Ltd.  |l eng 
536 |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas 
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: This work was partially supported by grants from the Consejo Nacional de Investigaciones Cientı́ficas y Técnicas (CONICET) and from the University of Buenos Aires. We thank Mr. G. Taminelli for his collaboration in some of the experiments, and Mrs. C. Aldonatti (Technical Assistance Career member of the CONICET) for her technical assistance. G. Chaufan has a fellowship from the CONICET, and L.C. San Martı́n de Viale and M.C. Rı́os de Molina are Scientific Research Career members of the CONICET. 
593 |a Laboratorio De Porfirias Experimentales Y Metabolismo del Hemo, Departamento De Química Biológica, Universidad De Buenos Aires, Buenos Aires, Argentina 
593 |a O'Higgins 4332, Capital, C.P. 1429, Buenos Aires, Argentina 
690 1 0 |a ACTIVE SITE 
690 1 0 |a ANTIGENIC DETERMINANTS 
690 1 0 |a HEXACHLOROBENZENE 
690 1 0 |a PORPHYRIA CUTANEA TARDA 
690 1 0 |a UROPORPHYRINOGEN DECARBOXYLASE 
690 1 0 |a CADMIUM 
690 1 0 |a COPPER ION 
690 1 0 |a CYSTINE 
690 1 0 |a DITHIOTHREITOL 
690 1 0 |a GLUTATHIONE 
690 1 0 |a HEXACHLOROBENZENE 
690 1 0 |a LEAD 
690 1 0 |a LIVER ENZYME 
690 1 0 |a MERCAPTOETHANOL 
690 1 0 |a MERCURY 
690 1 0 |a UROPORPHYRINOGEN DECARBOXYLASE 
690 1 0 |a ZINC ION 
690 1 0 |a ANIMAL EXPERIMENT 
690 1 0 |a ANIMAL MODEL 
690 1 0 |a ANTIGENICITY 
690 1 0 |a ARTICLE 
690 1 0 |a ATOM 
690 1 0 |a CONCENTRATION RESPONSE 
690 1 0 |a CONTROLLED STUDY 
690 1 0 |a DRUG ACTIVITY 
690 1 0 |a ENZYME ACTIVITY 
690 1 0 |a ENZYME ANALYSIS 
690 1 0 |a ENZYME BINDING 
690 1 0 |a ENZYME CONFORMATION 
690 1 0 |a ENZYME INHIBITION 
690 1 0 |a HYDRATION 
690 1 0 |a NONHUMAN 
690 1 0 |a PHYSICAL CHEMISTRY 
690 1 0 |a PORPHYRIA CUTANEA TARDA 
690 1 0 |a RAT 
690 1 0 |a ANIMALS 
690 1 0 |a ANTIGENS 
690 1 0 |a FEMALE 
690 1 0 |a FUNGICIDES, INDUSTRIAL 
690 1 0 |a HEXACHLOROBENZENE 
690 1 0 |a HYDROGEN-ION CONCENTRATION 
690 1 0 |a LIVER 
690 1 0 |a RATS 
690 1 0 |a RATS, WISTAR 
690 1 0 |a TEMPERATURE 
690 1 0 |a UROPORPHYRINOGEN DECARBOXYLASE 
650 1 7 |2 spines  |a PH 
700 1 |a Ríos de Molina, María del Carmen 
700 1 |a San Martín de Viale, L.C. 
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