Multiple NADPH-cytochrome P450 reductases from Trypanosoma cruzi. Suggested role on drug resistance

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Cytochrome P450 hemoproteins (CYPs) are involved in the synthesis of endogenous compounds such as steroids, fatty acids and prostaglandins as well as in the activation and detoxification of foreign compounds including therapeutic drugs. Cytochrome P450 reductase (CPR, E.C.1.6.2.4) transfers electron...

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Detalles Bibliográficos
Autor principal: Portal, P.
Otros Autores: Villamil, S.F, Alonso, G.D, De Vas, M.G, Flawiá, M.M, Torres, H.N, Paveto, C.
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 2008
Acceso en línea:Registro en Scopus
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Aporte de:Registro referencial: Solicitar el recurso aquí
Biblioteca Central Dr. Luis F. Leloir (FCEN) de Universidad de Buenos Aires
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024 7 |2 scopus  |a 2-s2.0-43949098939 
024 7 |2 Molecular Sequence Numbers  |a GENBANK: AAC19133, AAF02110, AAF89959, AAG31350, AAG31351, AAK43730, AAK83069, AAQ02989, AAQ10794, AAS92623, AAT76449, AAX55669, ABI15738, ABJ09678, ABJ09679, ABJ97709, ABL09938, ABN65609, AC009755, AF193061, AF193062, AF195660, AF288780, AF396968, BAA02090, BAA95684, BAD24850, CAA46814, CAA46815, CAA89837, CAB58576, CAE09055, CAJ05350, CAJ07987, EAT45397, NP_000611, NP_000932, NP_011908, NP_032924, NP_055249, NP_723173, S38427, XP_720425, XP_827553, XP_828830, XP_828912, XP_843361, XP_844345; SWISSPROT: O61608, P29474, P36587, Q26240; 
024 7 |2 cas  |a amino acid, 65072-01-7; benznidazole, 22994-85-0; cytochrome c, 9007-43-6, 9064-84-0; cytochrome P450, 9035-51-2; diphenyliodonium salt, 1483-72-3, 1483-73-4; flavine adenine nucleotide, 146-14-5; flavine mononucleotide, 130-40-5, 146-17-8; nifurtimox, 23256-30-6; protein, 67254-75-5; reduced nicotinamide adenine dinucleotide phosphate ferrihemoprotein reductase, 9023-03-4; reduced nicotinamide adenine dinucleotide phosphate, 53-57-6; DNA, Protozoan; NADPH-Ferrihemoprotein Reductase, EC 1.6.2.4; Recombinant Proteins 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a MBIPD 
100 1 |a Portal, P. 
245 1 0 |a Multiple NADPH-cytochrome P450 reductases from Trypanosoma cruzi. Suggested role on drug resistance 
260 |c 2008 
270 1 0 |m Paveto, C.; Instituto de Investigaciones en Ingeniería Genética y Biología Molecular, Consejo Nacional de Investigaciones Científicas y Técnicas, Departamento de Fisiología, Biología Molecular y Celular, Vuelta de Obligado 2490, 1428 Buenos Aires, Argentina; email: cpaveto@dna.uba.ar 
506 |2 openaire  |e Política editorial 
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520 3 |a Cytochrome P450 hemoproteins (CYPs) are involved in the synthesis of endogenous compounds such as steroids, fatty acids and prostaglandins as well as in the activation and detoxification of foreign compounds including therapeutic drugs. Cytochrome P450 reductase (CPR, E.C.1.6.2.4) transfers electrons from NADPH to a number of hemoproteins such as CYPs, cytochrome c, cytochrome b5, and heme oxygenase. This work presents the complete sequences of three non-allelic CPR genes from Trypanosoma cruzi. The encoded proteins named TcCPR-A, TcCPR-B and TcCPR-C have calculated molecular masses of 68.6 kDa, 78.4 kDa and 71.3 kDa, respectively. Deduced amino acid sequences share 11% amino acid identity, possess the conserved binding domains for FMN, FAD and NADPH and differ in the hydrophobic 27-amino acid residues of the N-terminal extension, which is absent in TcCPR-A. Every T. cruzi CPRs, TcCPR-A, TcCPR-B and TcCPR-C, were cloned and expressed in Escherichia coli. All of the recombinant enzymes reduced cytochrome c in a NADPH absolutely dependent manner with low Km values for this cofactor. They all were also strongly inhibited by diphenyleneiodonium, a classical flavoenzyme inhibitor. In addition, TcCPRs could support CYP activities when assayed in reconstituted systems containing rat liver microsomes. Polyclonal antiserum rose against the recombinant enzymes TcCPR-A and TcCPR-B demonstrated its presence in every T. cruzi developmental stages, with a remarkable expression of TcCPR-A in cell-cultured trypomastigotes. Overexpression of TcCPR-B in T. cruzi epimastigotes increased its resistance to the typical chemotherapeutic agents Nifurtimox and Benznidazole. We suggest a participation of TcCPR-B in the detoxification metabolism of the parasite. © 2008 Elsevier B.V. All rights reserved.  |l eng 
536 |a Detalles de la financiación: Universidad de Buenos Aires 
536 |a Detalles de la financiación: Agencia Nacional de Promoción Científica y Tecnológica 
536 |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas 
536 |a Detalles de la financiación: We are grateful to The Institute for Genomic Research (TIGR) genome projects and the Sanger institute genome project (GeneDB). We also thank Lic. Cristian Meyer for the critical reading of the manuscript and Dr. M. Dubin for the aminopyrine demethylase assay. We are indebted to Ms. Berta Franke de Cazzulo for trypomastigote and amastigote supply. We thank Consejo Nacional de Investigaciones Científicas y Técnicas (Argentina), University of Buenos Aires (Argentina) and Agencia Nacional de Promoción Científica y Tecnológica (Argentina), for supporting this study. S.F.V., G.D.A., M.G.M.F., H.N.T. and C.P. are members of Scientific Investigator Career of CONICET, Argentina. P.P. and M.G.D.V. are research fellows. 
593 |a Instituto de Investigaciones en Ingeniería Genética y Biología Molecular, Consejo Nacional de Investigaciones Científicas y Técnicas, Departamento de Fisiología, Biología Molecular y Celular, Vuelta de Obligado 2490, 1428 Buenos Aires, Argentina 
690 1 0 |a CYTOCHROME P450 REDUCTASE 
690 1 0 |a DRUG RESISTANCE 
690 1 0 |a TRYPANOSOMA CRUZI 
690 1 0 |a AMINO ACID 
690 1 0 |a BENZNIDAZOLE 
690 1 0 |a CYTOCHROME C 
690 1 0 |a CYTOCHROME P450 
690 1 0 |a DIPHENYLIODONIUM SALT 
690 1 0 |a FLAVINE ADENINE NUCLEOTIDE 
690 1 0 |a FLAVINE MONONUCLEOTIDE 
690 1 0 |a NIFURTIMOX 
690 1 0 |a POLYCLONAL ANTISERUM 
690 1 0 |a PROTEIN 
690 1 0 |a RECOMBINANT ENZYME 
690 1 0 |a REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE 
690 1 0 |a REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FERRIHEMOPROTEIN REDUCTASE 
690 1 0 |a AMINO ACID SEQUENCE 
690 1 0 |a AMINO TERMINAL SEQUENCE 
690 1 0 |a ANTIBIOTIC RESISTANCE 
690 1 0 |a ARTICLE 
690 1 0 |a CELL CULTURE 
690 1 0 |a CLONE 
690 1 0 |a DEVELOPMENTAL STAGE 
690 1 0 |a EPIMASTIGOTE 
690 1 0 |a ESCHERICHIA COLI 
690 1 0 |a GENE SEQUENCE 
690 1 0 |a MICROSOME 
690 1 0 |a MOLECULAR WEIGHT 
690 1 0 |a NONHUMAN 
690 1 0 |a NUCLEOTIDE SEQUENCE 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a TRYPANOSOMA CRUZI 
690 1 0 |a AMINO ACID SEQUENCE 
690 1 0 |a ANIMALS 
690 1 0 |a DNA, PROTOZOAN 
690 1 0 |a DRUG RESISTANCE 
690 1 0 |a ESCHERICHIA COLI 
690 1 0 |a MICROSOMES, LIVER 
690 1 0 |a MOLECULAR SEQUENCE DATA 
690 1 0 |a NADPH-FERRIHEMOPROTEIN REDUCTASE 
690 1 0 |a RATS 
690 1 0 |a RECOMBINANT PROTEINS 
690 1 0 |a TRANSFECTION 
690 1 0 |a TRYPANOSOMA CRUZI 
690 1 0 |a ESCHERICHIA COLI 
690 1 0 |a RATTUS 
690 1 0 |a TRYPANOSOMA CRUZI 
700 1 |a Villamil, S.F. 
700 1 |a Alonso, G.D. 
700 1 |a De Vas, M.G. 
700 1 |a Flawiá, M.M. 
700 1 |a Torres, H.N. 
700 1 |a Paveto, C. 
773 0 |d 2008  |g v. 160  |h pp. 42-51  |k n. 1  |p Mol. Biochem. Parasitol.  |x 01666851  |w (AR-BaUEN)CENRE-6136  |t Molecular and Biochemical Parasitology 
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856 4 0 |u https://doi.org/10.1016/j.molbiopara.2008.03.007  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_01666851_v160_n1_p42_Portal  |y Handle 
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