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[PMID]:25561501
[Au] Autor:MacLeod AK; Fallon PG; Sharp S; Henderson CJ; Wolf CR; Huang JT
[Ad] Endereço:From the ‡Jacqui Wood Cancer Centre, Medical Research Institute, Ninewells Hospital and Medical School, University of Dundee, Dundee DD1 9SY, Scotland;
[Ti] Título:An enhanced in vivo stable isotope labeling by amino acids in cell culture (SILAC) model for quantification of drug metabolism enzymes.
[So] Source:Mol Cell Proteomics;14(3):750-60, 2015 Mar.
[Is] ISSN:1535-9484
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Many of the enzymes involved in xenobiotic metabolism are maintained at a low basal level and are only synthesized in response to activation of upstream sensor/effector proteins. This induction can have implications in a variety of contexts, particularly during the study of the pharmacokinetics, pharmacodynamics, and drug-drug interaction profile of a candidate therapeutic compound. Previously, we combined in vivo SILAC material with a targeted high resolution single ion monitoring (tHR/SIM) LC-MS/MS approach for quantification of 197 peptide pairs, representing 51 drug metabolism enzymes (DME), in mouse liver. However, as important enzymes (for example, cytochromes P450 (Cyp) of the 1a and 2b subfamilies) are maintained at low or undetectable levels in the liver of unstimulated metabolically labeled mice, quantification of these proteins was unreliable. In the present study, we induced DME expression in labeled mice through synchronous ligand-mediated activation of multiple upstream nuclear receptors, thereby enhancing signals for proteins including Cyps 1a, 2a, 2b, 2c, and 3a. With this enhancement, 115 unique, lysine-containing, Cyp-derived peptides were detected in the liver of a single animal, as opposed to 56 in a pooled sample from three uninduced animals. A total of 386 peptide pairs were quantified by tHR/SIM, representing 68 Phase I, 30 Phase II, and eight control proteins. This method was employed to quantify changes in DME expression in the hepatic cytochrome P450 reductase null (HRN) mouse. We observed compensatory induction of several enzymes, including Cyps 2b10, 2c29, 2c37, 2c54, 2c55, 2e1, 3a11, and 3a13, carboxylesterase (Ces) 2a, and glutathione S-transferases (Gst) m2 and m3, along with down-regulation of hydroxysteroid dehydrogenases (Hsd) 11b1 and 17b6. Using DME-enhanced in vivo SILAC material with tHR/SIM, therefore, permits the robust analysis of multiple DME of importance to xenobiotic metabolism, with improved utility for the study of drug pharmacokinetics, pharmacodynamics, and of chemically treated and genetically modified mouse models.
[Mh] Termos MeSH primário: Aminoácidos/metabolismo
Enzimas/isolamento & purificação
Marcação por Isótopo/métodos
Fígado/enzimologia
Modelos Biológicos
[Mh] Termos MeSH secundário: Animais
Técnicas de Cultura de Células
Cromatografia Líquida
Grupo dos Citocromos a/isolamento & purificação
Masculino
Camundongos
Camundongos Endogâmicos C57BL
NADPH-Ferri-Hemoproteína Redutase/genética
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amino Acids); 0 (Cytochrome a Group); 0 (Enzymes); EC 1.6.2.4 (NADPH-Ferrihemoprotein Reductase)
[Em] Mês de entrada:1512
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150107
[St] Status:MEDLINE
[do] DOI:10.1074/mcp.M114.043661


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[PMID]:25482539
[Au] Autor:Bhowmick A; Head-Gordon T
[Ad] Endereço:Department of Chemical and Biomolecular Engineering, University of California, Berkeley, Berkeley, CA 94720, USA.
[Ti] Título:A monte carlo method for generating side chain structural ensembles.
[So] Source:Structure;23(1):44-55, 2015 Jan 06.
[Is] ISSN:1878-4186
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We report a Monte Carlo side chain entropy (MC-SCE) method that uses a physical energy function inclusive of long-range electrostatics and hydrophobic potential of mean force, coupled with both backbone variations and a backbone dependent side chain rotamer library, to describe protein conformational ensembles. Using the MC-SCE method in conjunction with backbone variability, we can reliably determine the side chain rotamer populations derived from both room temperature and cryogenically cooled X-ray crystallographic structures for CypA and H-Ras and NMR J-coupling constants for CypA, Eglin-C, and the DHFR product binary complexes E:THF and E:FOL. Furthermore, we obtain near perfect discrimination between a protein's native state ensemble and ensembles of misfolded structures for 55 different proteins, thereby generating far more competitive side chain packings for all of these proteins and their misfolded states.
[Mh] Termos MeSH primário: Modelos Moleculares
Método de Monte Carlo
Dobramento de Proteína
Estrutura Terciária de Proteína
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Cristalografia por Raios X
Grupo dos Citocromos a/química
Grupo dos Citocromos a/genética
Entropia
Seres Humanos
Ressonância Magnética Nuclear Biomolecular
Proteínas/química
Proteínas/genética
Proteínas Proto-Oncogênicas p21(ras)/química
Proteínas Proto-Oncogênicas p21(ras)/genética
Tetra-Hidrofolato Desidrogenase/química
Tetra-Hidrofolato Desidrogenase/genética
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Cytochrome a Group); 0 (Proteins); 0 (eglin proteinase inhibitors); EC 1.5.1.3 (Tetrahydrofolate Dehydrogenase); EC 3.6.5.2 (HRAS protein, human); EC 3.6.5.2 (Proto-Oncogene Proteins p21(ras))
[Em] Mês de entrada:1510
[Cu] Atualização por classe:150108
[Lr] Data última revisão:
150108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141209
[St] Status:MEDLINE


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[PMID]:23227713
[Au] Autor:Marchenko MM; Voloshchuk ON
[Ti] Título:[The state of the cytochrome part of respiratory chain in tumor carrier rats' liver in the conditions of preliminary low-level irradiation].
[So] Source:Radiats Biol Radioecol;52(5):496-502, 2012 Sep-Oct.
[Is] ISSN:0869-8031
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:The effect of low-level irradiation on the structural and functional organization of the cytochrome part of the respiratory chain in tumor carrier rats' liver is studied. The preliminary low-level irradiation leading to the mitochondrial cytochrome a, b and c content reduction at the latent stage of Guerin's carcinoma is shown. At the same time, the maximal reduction of the content of all liver cytochromes is observed at the terminal stages of oncogenesis. The content of cytochome c undergoes the most significant changes in the liver mitochondrial fracture. The possible mechanism of mitochondrial haem-containing cytochromes content reduction may be associated with the disorder of their formation caused by the heam synthesis inhibition found in our study. Simultaneously, the cytochrome oxydase (key enzyme of the cytochrome part) activity inhibition is observed to be caused by preliminary low-level irradiation at the latent growth stage of Guerin's carcinoma. The determined differences between irradiated and non-irradiated tumor carrier groups allow us to come to the conclusion that low-level irradiation has an impact only at the initial stages of the aftereffect. At the following stages, the state of the cytochrome part of the respiratory chain is defined by growth conditions of tumor.
[Mh] Termos MeSH primário: Grupo dos Citocromos a/metabolismo
Grupo dos Citocromos b/metabolismo
Grupo dos Citocromos c/metabolismo
Transporte de Elétrons/efeitos da radiação
[Mh] Termos MeSH secundário: Animais
Complexo IV da Cadeia de Transporte de Elétrons/metabolismo
Neoplasias Hepáticas/radioterapia
Mitocôndrias Hepáticas/metabolismo
Mitocôndrias Hepáticas/efeitos da radiação
Neoplasias Experimentais/radioterapia
Dose de Radiação
Ratos
Raios X
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytochrome a Group); 0 (Cytochrome b Group); 0 (Cytochrome c Group); EC 1.9.3.1 (Electron Transport Complex IV)
[Em] Mês de entrada:1302
[Cu] Atualização por classe:161020
[Lr] Data última revisão:
161020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121212
[St] Status:MEDLINE


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[PMID]:15231238
[Au] Autor:Atamna H
[Ad] Endereço:Children's Hospital Oakland Research Institute, 5700 Martin Luther King Jr. Way, Oakland, CA 94609-1673, USA. hatamna@chori.org
[Ti] Título:Heme, iron, and the mitochondrial decay of ageing.
[So] Source:Ageing Res Rev;3(3):303-18, 2004 Jul.
[Is] ISSN:1568-1637
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Heme, the major functional form of iron, is synthesized in the mitochondria. Although disturbed heme metabolism causes mitochondrial decay, oxidative stress, and iron accumulation, all of which are hallmarks of ageing, heme has been little studied in nutritional deficiency, in ageing, or age-related disorders such as Alzheimer's disease (AD). Biosynthesis of heme requires Vitamin B(6), riboflavin, biotin, pantothenic acid, and lipoic acid and the minerals zinc, iron, and copper, micronutrients are essential for the production of succinyl-CoA, the precursor for porphyrins, by the TCA (Krebs) cycle. Only a small fraction of the porphyrins synthesized from succinyl-CoA are converted to heme, the rest are excreted out of the body together with the degradation products of heme (e.g. bilirubin). Therefore, the heme biosynthetic pathway causes a net loss of succinyl-CoA from the TCA cycle. The mitochondrial pool of succinyl-CoA may limit heme biosynthesis in deficiencies for micronutrients (e.g. iron or biotin deficiency). Ageing and AD are also associated with hypometabolism, increase in heme oxygenase-1, loss of complex IV, and iron accumulation. Heme is a common denominator for all these changes, suggesting that heme metabolism maybe altered in age-related disorders. Heme can also be a prooxidant: it converts less reactive oxidants to highly reactive free radicals. Free heme has high affinity for different cell structures (protein, membranes, and DNA), triggering site-directed oxidative damage. This review discusses heme metabolism as related to metabolic changes seen in ageing and age-related disorders and highlights the possible role in iron deficiency.
[Mh] Termos MeSH primário: Envelhecimento
Heme/análogos & derivados
Heme/metabolismo
Ferro/metabolismo
Mitocôndrias/metabolismo
[Mh] Termos MeSH secundário: Aconitato Hidratase/metabolismo
Acil Coenzima A/metabolismo
Doença de Alzheimer/metabolismo
Peptídeos beta-Amiloides/metabolismo
Precursor de Proteína beta-Amiloide/metabolismo
Animais
Química Encefálica
Grupo dos Citocromos a
Complexo IV da Cadeia de Transporte de Elétrons/metabolismo
Ferroquelatase/metabolismo
Heme/análise
Heme Oxigenase (Desciclizante)/metabolismo
Seres Humanos
Micronutrientes/metabolismo
Neurônios/metabolismo
Porfirinas/biossíntese
Receptores Muscarínicos/metabolismo
Succinato-CoA Ligases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, P.H.S.; REVIEW
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Amyloid beta-Peptides); 0 (Amyloid beta-Protein Precursor); 0 (Cytochrome a Group); 0 (Micronutrients); 0 (Porphyrins); 0 (Receptors, Muscarinic); 18535-39-2 (heme a); 42VZT0U6YR (Heme); 604-98-8 (succinyl-coenzyme A); E1UOL152H7 (Iron); EC 1.14.14.18 (Heme Oxygenase (Decyclizing)); EC 1.9.3.1 (Electron Transport Complex IV); EC 4.2.1.3 (Aconitate Hydratase); EC 4.99.1.1 (Ferrochelatase); EC 6.2.1.- (Succinate-CoA Ligases)
[Em] Mês de entrada:0503
[Cu] Atualização por classe:161124
[Lr] Data última revisão:
161124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:040703
[St] Status:MEDLINE


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[PMID]:14635652
[Au] Autor:Huckstorf C; Streller T; Acker H
[Ad] Endereço:Institute of Physiology, University of Rostock, Gertrudenstr. 9, D-18057 Rostock, Germany.
[Ti] Título:An unusual cytochrome a592 with low PO2 affinity correlates with afferent discharge in the carotid body.
[So] Source:Adv Exp Med Biol;536:75-83, 2003.
[Is] ISSN:0065-2598
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Corpo Carotídeo/metabolismo
Grupo dos Citocromos a/metabolismo
[Mh] Termos MeSH secundário: Animais
Monóxido de Carbono/farmacologia
Corpo Carotídeo/efeitos dos fármacos
Células Quimiorreceptoras/metabolismo
Cianetos/farmacologia
Complexo IV da Cadeia de Transporte de Elétrons/metabolismo
Hipóxia/metabolismo
Técnicas In Vitro
Modelos Neurológicos
Neurônios Aferentes/metabolismo
Oxirredução
Oxigênio/metabolismo
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cyanides); 0 (Cytochrome a Group); 7U1EE4V452 (Carbon Monoxide); EC 1.9.3.1 (Electron Transport Complex IV); S88TT14065 (Oxygen)
[Em] Mês de entrada:0408
[Cu] Atualização por classe:161124
[Lr] Data última revisão:
161124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:031126
[St] Status:MEDLINE


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[PMID]:12505305
[Au] Autor:Puga A; Marlowe J; Barnes S; Chang CY; Maier A; Tan Z; Kerzee JK; Chang X; Strobeck M; Knudsen ES
[Ad] Endereço:Department of Environmental Health, University of Cincinnati Medical Center, P.O. Box 670056, 123 E. Shields Street, Cincinnati, OH 45267-0056, USA. alvaro.puga@uc.edu
[Ti] Título:Role of the aryl hydrocarbon receptor in cell cycle regulation.
[So] Source:Toxicology;181-182:171-7, 2002 Dec 27.
[Is] ISSN:0300-483X
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:One of the most puzzling aspects of the biological impact of polycyclic aromatic hydrocarbon compounds is that they elicit an apparently unrelated variety of toxic, teratogenic, and carcinogenic responses in exposed animals and in humans. At the cellular level, these environmental toxicants affect cell cycle regulatory mechanisms and signal transduction pathways in ways that are equally diverse and often contradictory. For example, depending on the particular cell lines studied, exposure to these compounds may lead to cell proliferation, to terminal differentiation, or to apoptosis. These effects are mediated by the aryl hydrocarbon receptor, a ligand-activated transcription factor well known for its regulatory activity on the expression of several phase I detoxification cytochrome P450 genes. Research into the molecular mechanisms of aryl hydrocarbon receptor function has uncovered a novel role for this protein during cell cycle progression. The activated receptor acts as an environmental sensor and cell cycle checkpoint that commits cells exposed to adverse environmental stimuli to arrest before the onset of DNA replication.
[Mh] Termos MeSH primário: Ciclo Celular/fisiologia
Receptores de Hidrocarboneto Arílico/fisiologia
[Mh] Termos MeSH secundário: Animais
Apoptose/efeitos dos fármacos
Ciclo Celular/genética
Grupo dos Citocromos a/metabolismo
Replicação do DNA/efeitos dos fármacos
Poluentes Ambientais/toxicidade
Seres Humanos
Ligantes
Plasmídeos/genética
Hidrocarbonetos Aromáticos Policíclicos/toxicidade
Receptores de Hidrocarboneto Arílico/genética
Proteína do Retinoblastoma/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, P.H.S.; REVIEW
[Nm] Nome de substância:
0 (Cytochrome a Group); 0 (Environmental Pollutants); 0 (Ligands); 0 (Polycyclic Aromatic Hydrocarbons); 0 (Receptors, Aryl Hydrocarbon); 0 (Retinoblastoma Protein)
[Em] Mês de entrada:0302
[Cu] Atualização por classe:161124
[Lr] Data última revisão:
161124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:021231
[St] Status:MEDLINE


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[PMID]:12153998
[Au] Autor:Streller T; Huckstorf C; Pfeiffer C; Acker H
[Ad] Endereço:Institut für Physiologie der Universität Rostock,18057 Rostock, Germany. tino.streller@medizin.uni-rostock.de
[Ti] Título:Unusual cytochrome a592 with low PO2 affinity correlates as putative oxygen sensor with rat carotid body chemoreceptor discharge.
[So] Source:FASEB J;16(10):1277-9, 2002 Aug.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Light-absorption spectra and afferent chemoreceptor discharge were simultaneously recorded on superfused rat carotid bodies (CBs) under the influence of cytochrome a3-CuB ligands (O2, CN-, CO) in order to identify the primary mitochondrial cytochrome c oxidase (CCO) oxygen sensor. Spectra could be described on the basis of weighted light-absorption spectra of cytochrome b558 of the NAD(P)H oxidase and mitochondrial cytochromes b and c, CCO, cytochrome a3, and an unusual cytochrome a peaking at 592 nm. Discharge signals were deconvoluted into phasic and tonic activity for comparing different CB responses. The spectral weight of cytochrome a592 decreased significantly starting at high PO2 (100 mm Hg) and low sodium cyanide (CN-, 10 mM) accompanied by increasing phasic peak discharge. Combined CO-hypoxia or CO-CN- application inhibited photolysis of CO-stimulated chemoreceptor discharge, revealing photometrically cytochrome a592 as central in oxygen sensing. Control spectra in tissue from sympathetic and nodose ganglia did not show any cytochrome a592 contribution. According to these results, cytochrome a592 is assumed as a unique component of CB CCO, revealing in contrast to other cytochromes an apparent low PO2 and high CN- affinity, probably due to a shortcut of electron flow within CCO between CuA and cytochrome a3-CuB.
[Mh] Termos MeSH primário: Corpo Carotídeo/fisiologia
Grupo dos Citocromos a/metabolismo
Grupo dos Citocromos a/fisiologia
Oxigênio/metabolismo
[Mh] Termos MeSH secundário: Animais
Corpo Carotídeo/efeitos dos fármacos
Hipóxia Celular
Células Cultivadas
Técnicas de Cultura
Cianetos/farmacologia
Transporte de Elétrons
Complexo IV da Cadeia de Transporte de Elétrons/metabolismo
Cinética
Ligantes
Mitocôndrias/enzimologia
Modelos Biológicos
Gânglio Nodoso/metabolismo
Oxirredução
Pressão Parcial
Ratos
Análise Espectral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cyanides); 0 (Cytochrome a Group); 0 (Ligands); EC 1.9.3.1 (Electron Transport Complex IV); S88TT14065 (Oxygen)
[Em] Mês de entrada:0209
[Cu] Atualização por classe:141120
[Lr] Data última revisão:
141120
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:020803
[St] Status:MEDLINE


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[PMID]:11214473
[Au] Autor:Dzhagarov BM; Belyanovich LM; Konstantinov AA; Rudenok AN; Tikhomirov SA
[Ad] Endereço:Institute of Molecular and Atomic Physics, National Academy of Sciences of Belarus, pr. Frantsiska Skoriny 70, Minsk, 220072 Belarus.
[Ti] Título:Picosecond absorption spectroscopy of cytochrome c oxidase: excited states and relaxation processes in heme groups of cytochromes a and a3.
[So] Source:Dokl Biophys;373-375:53-5, 2000 Jul-Dec.
[Is] ISSN:0012-4974
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Grupo dos Citocromos a/química
Complexo IV da Cadeia de Transporte de Elétrons/química
Heme/química
[Mh] Termos MeSH secundário: Animais
Bovinos
Cinética
Miocárdio/enzimologia
Espectrofotometria
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cytochrome a Group); 42VZT0U6YR (Heme); EC 1.9.3.1 (Electron Transport Complex IV)
[Em] Mês de entrada:0104
[Cu] Atualização por classe:161021
[Lr] Data última revisão:
161021
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:010224
[St] Status:MEDLINE


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[PMID]:11132641
[Au] Autor:Tanimura Y; Fukumori Y
[Ad] Endereço:Department of Biology, Faculty of Science, Kanazawa University, Japan.
[Ti] Título:Heme-copper oxidase family structure of Magnetospirillum magnetotacticum 'cytochrome a1'-like hemoprotein without cytochrome c oxidase activity.
[So] Source:J Inorg Biochem;82(1-4):73-8, 2000 Nov.
[Is] ISSN:0162-0134
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The genes encoding 'cytochrome a1'-like hemoprotein of Magnetospirillum magnetotacticum were identified and sequenced. Three ORFs, mcalI, mcaI and hosA, were included in the sequenced region. The six histidine residues which were predicted to associate with the prosthetic cofactors of heme-copper oxidase superfamily were conserved in the hemoprotein. However, none of the amino acid residues which were proposed to participate in the oxygen-reducing and the coupled proton pumping reactions in cytochrome c oxidase were at all conserved in the hemoprotein.
[Mh] Termos MeSH primário: Grupo dos Citocromos a/genética
Oxirredutases/genética
Rhodospirillaceae/enzimologia
Rhodospirillaceae/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Aminoácidos/análise
Sequência de Bases
Grupo dos Citocromos a/química
Grupo dos Citocromos a/metabolismo
Citocromos a1
Dados de Sequência Molecular
Oxirredução
Oxirredutases/química
Oxirredutases/metabolismo
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amino Acids); 0 (Cytochrome a Group); 9035-35-2 (Cytochromes a1); EC 1.- (Oxidoreductases); EC 1.16.- (copper oxidase)
[Em] Mês de entrada:0103
[Cu] Atualização por classe:061115
[Lr] Data última revisão:
061115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:010102
[St] Status:MEDLINE


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[PMID]:10667518
[Au] Autor:Schenkman KA; Yan S
[Ad] Endereço:Department of Pediatrics, University of Wisconsin, Madison, USA. kschen@chmc.org
[Ti] Título:Propofol impairment of mitochondrial respiration in isolated perfused guinea pig hearts determined by reflectance spectroscopy.
[So] Source:Crit Care Med;28(1):172-7, 2000 Jan.
[Is] ISSN:0090-3493
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: To simultaneously determine the effect of propofol on myocardial oxygenation, mitochondrial function, and whole organ function in an isolated heart model, using optical reflectance spectroscopy. DESIGN: Controlled laboratory investigation. SETTING: Research laboratory. SUBJECTS: Twenty adult guinea pigs. INTERVENTIONS: Isolated hearts were perfused alternately with a modified oxygenated Krebs-Henseleit buffer and with buffer containing varied concentrations of propofol. Ninety seconds of ischemia were produced during perfusion with each solution studied. MEASUREMENTS AND MAIN RESULTS: Myoglobin oxygen saturation, cytochrome c and cytochrome a/a3 redox state, and ventricular pressure were continuously measured from isolated guinea pig hearts during a 2-hr period. Myoglobin oxygen saturation increased and both cytochromes became more oxidized in the presence of propofol. During ischemia, myoglobin desaturation and cytochrome reduction were delayed and less complete in the presence of propofol. The mean ischemic time to 50% myoglobin desaturation was, on average, 14.3 secs with buffer perfusion, and increased to 24.5, 27.9, and 41.8 secs, with 50, 100, and 200 microM propofol perfusion, respectively. Ventricular function decreased linearly with increasing propofol concentration. From baseline buffer perfusion, maximal dP/dt per cardiac cycle decreased on average by 30.4%, 40.9%, and 69.4%, with 50, 100, and 200 microM propofol perfusion, respectively. CONCLUSIONS: Propofol impairs either oxygen utilization or inhibits electron flow along the mitochondrial electron transport chain in the guinea pig cardiomyocyte. Propofol also significantly decreases ventricular performance in the isolated perfused heart. These effects are linearly correlated with propofol concentration in the range studied.
[Mh] Termos MeSH primário: Anestésicos Intravenosos/farmacologia
Coração/efeitos dos fármacos
Isquemia/fisiopatologia
Mitocôndrias Cardíacas/efeitos dos fármacos
Oxigênio/metabolismo
Propofol/farmacologia
[Mh] Termos MeSH secundário: Animais
Grupo dos Citocromos a/metabolismo
Grupo dos Citocromos c/metabolismo
Relação Dose-Resposta a Droga
Feminino
Cobaias
Coração/fisiologia
Masculino
Mitocôndrias Cardíacas/fisiologia
Mioglobina/metabolismo
Função Ventricular Esquerda/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anesthetics, Intravenous); 0 (Cytochrome a Group); 0 (Cytochrome c Group); 0 (Myoglobin); S88TT14065 (Oxygen); YI7VU623SF (Propofol)
[Em] Mês de entrada:0002
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:000210
[St] Status:MEDLINE



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