المؤلفون: Guan Shi, Li Bao, Hao Chen, Fei Feng, Hai Tang, Pu Jia

المصدر: Brazilian Journal of Medical and Biological Research, Volume: 52, Issue: 1, Article number: e7844, Published: 23 NOV 2018
Brazilian Journal of Medical and Biological Research v.52 n.1 2019
Brazilian Journal of Medical and Biological Research
Associação Brasileira de Divulgação Científica (ABDC)
instacron:ABDC
Brazilian Journal of Medical and Biological Research, Vol 52, Iss 1 (2018)

مصطلحات موضوعية: 0301 basic medicine, Programmed cell death, Indoles, Physiology, Cell Survival, Necroptosis, Immunology, Biophysics, Ocean Engineering, Caspase 3, Inhibitor of apoptosis, Caspase 8, Biochemistry, 03 medical and health sciences, Mice, Necrosis, 0302 clinical medicine, Animals, Viability assay, General Pharmacology, Toxicology and Pharmaceutics, Phosphorylation, lcsh:QH301-705.5, lcsh:R5-920, Osteoblasts, L-Lactate Dehydrogenase, Cell growth, Chemistry, Tumor Necrosis Factor-alpha, General Neuroscience, Imidazoles, Cell Biology, General Medicine, Molecular biology, Caspase Inhibitors, Mouse osteoblast, 030104 developmental biology, lcsh:Biology (General), Apoptosis, 030220 oncology & carcinogenesis, TNF-α, Necrostatin-1, lcsh:Medicine (General), Z-IETD-FMK, Oligopeptides, Research Article

الوصف: Necroptosis is a regulated cell death mechanism. However, it is unknown whether necroptosis is involved in the death of tumor necrosis factor-α (TNF-α)-treated osteoblasts. Therefore, we conducted the study with TNF-α, Nec-1 (a specific inhibitor of necroptosis), and Z-IETD-FMK (a specific inhibitor of apoptosis) to determine whether necroptosis plays a role in the death of TNF-α-treated osteoblast cell line MC3T3-E1. Cell viability, cell death, and lactate dehydrogenase (LDH) release were assayed to evaluate cytotoxicity. Specific marker proteins receptor interacting protein kinase (RIPK3) and phosphorylated mixed lineage kinase domain-like protein (p-MLKL) for necroptosis, and cleaved caspase 3 for apoptosis were detected by western blot, and mRNA was measured by quantitative real-time polymerase chain reaction (qRT-PCR). We found that TNF-α inhibited cell proliferation in a dose- and time-dependent manner. Nec-1 plus Z-IETD-FMK restored cell viability and significantly decreased LDH release. In addition, TNF-α alone increased the cell population of AV+PI-, while Z-IETD-FMK caused a shift in the cell population from AV+PI- to AV+PI+. Furthermore, TNF-α significantly increased protein cleaved caspase 3. TNF-α plus Z-IETD-FMK significantly increased the proteins RIPK3 and MLKL phosphorylation in MC3T3-E1 cells, while the changes in mRNA levels of RIPK3, MLKL, and caspase 3 were not consistent with the changes in the corresponding protein expression levels. In conclusion, TNF-α induced preferentially apoptosis in osteoblast cell line and necroptosis played a decisive role when TNF-α-induced death was inhibited by the inhibitor of apoptosis. Combined treatment with Nec-1 and Z-IETD-FMK protected mouse osteoblasts from death induced by TNF-α.

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http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2019000100603&lng=en&tlng=enTest

المؤلفون: X.N. Chen, A.X. Zhu, Yong Zhou, Ting Wang

المصدر: Brazilian Journal of Medical and Biological Research v.47 n.9 2014
Brazilian Journal of Medical and Biological Research
Associação Brasileira de Divulgação Científica (ABDC)
instacron:ABDC
Brazilian Journal of Medical and Biological Research, Volume: 47, Issue: 9, Pages: 738-745, Published: 25 JUL 2014
Brazilian Journal of Medical and Biological Research, Vol 47, Iss 9, Pp 738-745 (2014)

مصطلحات موضوعية: Male, Pathology, Time Factors, Physiology, Hindlimb, Biochemistry, Random Allocation, chemistry.chemical_compound, General Pharmacology, Toxicology and Pharmaceutics, Creatine Kinase, lcsh:QH301-705.5, lcsh:R5-920, biology, General Neuroscience, Interleukin, General Medicine, Immunohistochemistry, Interleukin-10, Up-Regulation, medicine.anatomical_structure, Reperfusion Injury, lcsh:Medicine (General), Perfusion, Skeletal muscle ischemia, medicine.medical_specialty, Blotting, Western, Immunology, Biophysics, Ischemia, Ocean Engineering, Internal medicine, Lactate dehydrogenase, medicine, Animals, Rats, Wistar, Muscle, Skeletal, Ischemic postconditioning, L-Lactate Dehydrogenase, Interleukin-6, Tumor Necrosis Factor-alpha, business.industry, Hypoxia-inducible factor-1α, Biomedical Sciences, Endothelial Cells, Skeletal muscle, Extremities, Cell Biology, Hypoxia-Inducible Factor 1, alpha Subunit, medicine.disease, Disease Models, Animal, Endocrinology, lcsh:Biology (General), chemistry, Hypoxia-inducible factor-1?, biology.protein, Creatine kinase, business, Reperfusion injury

الوصف: Hypoxia-inducible factor-1α (HIF-1α) is one of the most potent angiogenic growth factors. It improves angiogenesis and tissue perfusion in ischemic skeletal muscle. In the present study, we tested the hypothesis that ischemic postconditioning is effective for salvaging ischemic skeletal muscle resulting from limb ischemia-reperfusion injury, and that the mechanism involves expression of HIF-1α. Wistar rats were randomly divided into three groups (n=36 each): sham-operated (group S), hindlimb ischemia-reperfusion (group IR), and ischemic postconditioning (group IPO). Each group was divided into subgroups (n=6) according to reperfusion time: immediate (0 h, T0), 1 h (T1), 3 h (T3), 6 h (T6), 12 h (T12), and 24 h (T24). In the IPO group, three cycles of 30-s reperfusion and 30-s femoral aortic reocclusion were carried out before reperfusion. At all reperfusion times (T0-T24), serum creatine kinase (CK) and lactate dehydrogenase (LDH) activities, as well as interleukin (IL)-6, IL-10, and tumor necrosis factor-α (TNF-α) concentrations, were measured in rats after they were killed. Histological and immunohistochemical methods were used to assess the skeletal muscle damage and HIF-1α expression in skeletal muscle ischemia. In groups IR and IPO, serum LDH and CK activities and TNF-α, IL-6, and IL-10 concentrations were all significantly increased compared to group S, and HIF-1α expression was up-regulated (P

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المؤلفون: Haiquan Qiao, Xueying Sun, F. Meng, Bo Tang

المصدر: Brazilian Journal of Medical and Biological Research, Vol 40, Iss 12, Pp 1637-1646 (2007)
Brazilian Journal of Medical and Biological Research, Volume: 40, Issue: 12, Pages: 1637-1646, Published: 29 OCT 2007
Brazilian Journal of Medical and Biological Research v.40 n.12 2007
Brazilian Journal of Medical and Biological Research
Associação Brasileira de Divulgação Científica (ABDC)
instacron:ABDC

مصطلحات موضوعية: Lipopolysaccharides, Male, Lipopolysaccharide, Physiology, medicine.medical_treatment, Anti-Inflammatory Agents, Apoptosis, Pharmacology, Biochemistry, Severity of Illness Index, chemistry.chemical_compound, Glycyrrhizin, General Pharmacology, Toxicology and Pharmaceutics, Saline, lcsh:QH301-705.5, lcsh:R5-920, biology, General Neuroscience, Cytochrome c, Liver Diseases, Alanine Transaminase, General Medicine, Immunohistochemistry, Acute Disease, Tumor necrosis factor alpha, Chemical and Drug Induced Liver Injury, lcsh:Medicine (General), Inflammatory cytokine, Immunology, Biophysics, Ocean Engineering, Proliferating Cell Nuclear Antigen, medicine, Animals, Hepatectomy, Aspartate Aminotransferases, Rats, Wistar, L-Lactate Dehydrogenase, business.industry, Tumor Necrosis Factor-alpha, Cell Biology, Glycyrrhizic Acid, Endotoxemia, Proliferating cell nuclear antigen, Rats, chemistry, lcsh:Biology (General), biology.protein, business

الوصف: Massive hepatectomy associated with infection induces liver dysfunction, or even multiple organ failure and death. Glycyrrhizin has been shown to exhibit anti-oxidant and anti-inflammatory activities. The aim of the present study was to investigate whether glycyrrhizin could attenuate endotoxin-induced acute liver injury after partial hepatectomy. Male Wistar rats (6 to 8 weeks old, weighing 200-250 g) were randomly assigned to three groups of 24 rats each: sham, saline and glycyrrhizin. Rats were injected intravenously with lipopolysaccharide (LPS) 24 h after 70% hepatectomy. Glycyrrhizin, pre-administered three times with 24 h intervals 48 h before hepatectomy, prolonged the survival of rats submitted to partial hepatectomy and LPS injection, compared with saline controls. Glycyrrhizin was shown to attenuate histological hepatic changes and significantly reduced serum levels of aspartate aminotransferase, alanine aminotransferase, and lactic dehydrogenase, at all the indicated times (6 rats from each were sacrificed 1, 3, 6, and 9 h after LPS injection), compared with saline controls. Glycyrrhizin also significantly inhibited hepatocyte apoptosis by down-regulating the expression of caspase-3 and inhibiting the release of cytochrome C from mitochondria into the cytoplasm. The anti-inflammatory activity of glycyrrhizin may rely on the inhibition of release of tumor necrosis factor-a, myeloperoxidase activity, and translocation of nuclear factor-kappa B into the nuclei. Glycyrrhizin also up-regulated the expression of proliferating cell nuclear antigen, implying that it might be able to promote regeneration of livers harmed by LPS. In summary, glycyrrhizin may represent a potent drug protecting the liver against endotoxin-induced injury, especially after massive hepatectomy.

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http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2007001200007Test

المؤلفون: Marilia Seelaender, Waldecir Paula Lima, Robson Eder, Nelo Eidy Zanchi, Humberto Nicastro, Daniela Caetano Gonçalves, Fábio Santos Lira, Jean Marc Lavoie, Luiz Carlos Carnevali

المصدر: Brazilian Journal of Medical and Biological Research, Volume: 45, Issue: 8, Pages: 777-783, Published: AUG 2012
Brazilian Journal of Medical and Biological Research, Vol 45, Iss 8, Pp 777-783 (2012)
Brazilian Journal of Medical and Biological Research
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
Brazilian Journal of Medical and Biological Research v.45 n.8 2012
Associação Brasileira de Divulgação Científica (ABDC)
instacron:ABDC

مصطلحات موضوعية: Male, Physiology, Biochemistry, chemistry.chemical_compound, Random Allocation, Citrate synthase, General Pharmacology, Toxicology and Pharmaceutics, lcsh:QH301-705.5, computer.programming_language, Lipoprotein lipase, lcsh:R5-920, biology, sed, Reverse Transcriptase Polymerase Chain Reaction, General Neuroscience, General Medicine, Adaptation, Physiological, High-intensity intermittent training, Carnitine palmitoyl transferase, lcsh:Medicine (General), Oxidation-Reduction, medicine.drug, medicine.medical_specialty, Short Communication, Immunology, Biophysics, Real-Time Polymerase Chain Reaction, Gastrocnemius muscle, Internal medicine, Lactate dehydrogenase, Physical Conditioning, Animal, medicine, Animals, Carnitine O-palmitoyltransferase, Carnitine, Rats, Wistar, Muscle, Skeletal, Carnitine O-Palmitoyltransferase, Lipid metabolism, Cell Biology, HISTOLOGIA, Rats, Lipoprotein Lipase, Endocrinology, chemistry, lcsh:Biology (General), biology.protein, computer

الوصف: We examined the capacity of high-intensity intermittent training (HI-IT) to facilitate the delivery of lipids to enzymes responsible for oxidation, a task performed by the carnitine palmitoyl transferase (CPT) system in the rat gastrocnemius muscle. Male adult Wistar rats (160-250 g) were randomly distributed into 3 groups: sedentary (Sed, N = 5), HI-IT (N = 10), and moderate-intensity continuous training (MI-CT, N = 10). The trained groups were exercised for 8 weeks with a 10% (HI-IT) and a 5% (MI-CT) overload. The HI-IT group presented 11.8% decreased weight gain compared to the Sed group. The maximal activities of CPT-I, CPT-II, and citrate synthase were all increased in the HI-IT group compared to the Sed group (P < 0.01), as also was gene expression, measured by RT-PCR, of fatty acid binding protein (FABP; P < 0.01) and lipoprotein lipase (LPL; P < 0.05). Lactate dehydrogenase also presented a higher maximal activity (nmol·min -1 ·mg protein ) in HI-IT (around 83%). We suggest that 8 weeks of HI-IT enhance mitochondrial lipid transport capacity thus facilitating the oxidation process in the gastrocnemius muscle. This adaptation may also be associated with the decrease in weight gain observed in the animals and was concomitant to a higher gene expression of both FABP and LPL in HI-IT, suggesting that intermittent exercise is a “time-efficient” strategy inducing metabolic adaptation. Key words: High-intensity intermittent training; Lipid metabolism; Carnitine palmitoyl transferase

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المؤلفون: M.A. dos-Santos, R. Curi, D.H.G.P Barbieri, R. Rosa

المصدر: Brazilian Journal of Medical and Biological Research, Vol 30, Iss 6, p 719 (1997)

مصطلحات موضوعية: Male, Physiology, Glutamine, Phosphofructokinase-1, Biochemistry, Glutaminase activity, chemistry.chemical_compound, thymus, lymph nodes, Fructose-Bisphosphate Aldolase, Hexokinase, glutamine metabolism, Mesenteric lymph nodes, Glycolysis, General Pharmacology, Toxicology and Pharmaceutics, lcsh:QH301-705.5, lcsh:R5-920, Glutaminase, General Neuroscience, General Medicine, protein malnutrition, medicine.anatomical_structure, Lymph, Dietary Proteins, lcsh:Medicine (General), Phosphofructokinase, medicine.medical_specialty, glucose metabolism, Immunology, Pyruvate Kinase, Biophysics, Thymus Gland, Biology, Protein-Energy Malnutrition, Internal medicine, Lactate dehydrogenase, medicine, Animals, Rats, Wistar, L-Lactate Dehydrogenase, Glucose-6-Phosphate Isomerase, Cell Biology, Rats, Endocrinology, Glucose, chemistry, lcsh:Biology (General), Pyruvate kinase

الوصف: The activity of important glycolytic enzymes (hexokinase, phosphofructokinase, aldolase, phosphohexoseisomerase, pyruvate kinase and lactate dehydrogenase) and glutaminolytic enzymes (phosphate-dependent glutaminase) was determined in the thymus and mesenteric lymph nodes of Wistar rats submitted to protein malnutrition (6% protein in the diet rather than 20%) from conception to 12 weeks after birth. The wet weight (g) of the thymus and mesenteric lymph nodes decreased due to protein malnutrition by 87% (from 0.30 +/- 0.05 to 0.04 +/- 0.01) and 75% (0.40 +/- 0.04 to 0.10 +/- 0.02), respectively. The protein content was reduced only in the thymus from 102.3 +/- 4.4 (control rats) to 72.6 +/- 6.6 (malnourished rats). The glycolytic enzymes were not affected by protein malnutrition, but the glutaminase activity of the thymus and lymph nodes was reduced by half in protein-malnourished rats as compared to controls. This fact may lead to a decrease in the cellularity of the organ and thus in its size, weight and protein content.

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http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1997000600003Test

المؤلفون: A.V. Spichenkov, Volodymyr I. Lushchak, T.V. Bahnjukova

المصدر: Brazilian Journal of Medical and Biological Research, Vol 30, Iss 3, p 381 (1997)
Brazilian Journal of Medical and Biological Research, Vol 30, Iss 3, Pp 381-385 (1997)

مصطلحات موضوعية: Pyruvate dehydrogenase kinase, Physiology, muscle, Immunology, Biophysics, Biochemistry, Cofactor, pyruvate kinase, chemistry.chemical_compound, Lactate dehydrogenase, Animals, Seawater, General Pharmacology, Toxicology and Pharmaceutics, lcsh:QH301-705.5, chemistry.chemical_classification, lcsh:R5-920, L-Lactate Dehydrogenase, biology, Muscles, General Neuroscience, anaerobiosis, lactate dehydrogenase, Cell Biology, General Medicine, Mussel, biology.organism_classification, Enzyme assay, Mytilus, Bivalvia, Enzyme, chemistry, Mytilus galloprovincialis, lcsh:Biology (General), biology.protein, property modification, lcsh:Medicine (General), Pyruvate kinase

الوصف: The modification of pyruvate kinase (PK) and lactate dehydrogenase (LDH) activity in foot muscle of the mussel Mytilus galloprovincialis during exposure to air and recovery in water was investigated. In the course of exposure to air, the activity of these enzymes measured at high and low substrate concentrations showed successive increases and decreases. Returning the mussels to water after exposure to air affected enzyme activity in a manner similar to anaerobiosis. When measuring at saturated concentrations of substrates and substrate and coenzyme for PK and LDH, respectively, the maximum activation of PK (37%) was observed at 4 h of animal exposure to air, and for LDH (67%) at 6 h exposure to air. During 24 h of exposure of animals to air, PK activity practically reached the stock level, while LDH was still activated (148%). The change in lactate dehydrogenase activity in mussel muscle during anoxia and recovery is described here for the first time. Variation in pyruvate kinase activity during exposure to air and recovery is linked to the alteration of half-maximal saturation constants and maximal velocity for both substrates. The possible role of reversible phosphorylation in the regulation of pyruvate kinase and lactate dehydrogenase properties is discussed.

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http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1997000300012Test

المؤلفون: Reginaldo Ceneviva, Fernanda Viaro, Paulo Roberto Barbosa Evora, L.C. Miranda

المصدر: Brazilian Journal of Medical and Biological Research v.40 n.6 2007
Brazilian Journal of Medical and Biological Research
Associação Brasileira de Divulgação Científica (ABDC)
instacron:ABDC
Brazilian Journal of Medical and Biological Research, Volume: 40, Issue: 6, Pages: 857-865, Published: JUN 2007
Brazilian Journal of Medical and Biological Research, Vol 40, Iss 6, Pp 857-865 (2007)

مصطلحات موضوعية: Male, medicine.medical_specialty, Endothelium, Physiology, Immunology, Biophysics, Ischemia, Vasodilation, Ischemia/reperfusion injury, Biochemistry, Nitric oxide, Random Allocation, chemistry.chemical_compound, Dogs, Internal medicine, medicine, Animals, Aspartate Aminotransferases, General Pharmacology, Toxicology and Pharmaceutics, lcsh:QH301-705.5, lcsh:R5-920, L-Lactate Dehydrogenase, business.industry, General Neuroscience, Alanine Transaminase, Hepatic artery, Cell Biology, General Medicine, medicine.disease, Malondialdehyde, Endocrinology, medicine.anatomical_structure, lcsh:Biology (General), chemistry, Liver, Reperfusion Injury, Anesthesia, Female, Artery Endothelium, Endothelium, Vascular, Lipid Peroxidation, Sodium nitroprusside, lcsh:Medicine (General), business, Reperfusion injury, medicine.drug

الوصف: We investigated whether hepatic artery endothelium may be the earliest site of injury consequent to liver ischemia and reperfusion. Twenty-four heartworm-free mongrel dogs of either sex exposed to liver ischemia/reperfusion in vivo were randomized into four experimental groups (N = 6): a) control, sham-operated dogs, b) dogs subjected to 60 min of ischemia, c) dogs subjected to 30 min of ischemia and 60 min of reperfusion, and d) animals subjected to 45 min of ischemia and 120 min of reperfusion. The nitric oxide endothelium-dependent relaxation of hepatic artery rings contracted with prostaglandin F2a and exposed to increasing concentrations of acetylcholine, calcium ionophore A23187, sodium fluoride, phospholipase-C, poly-L-arginine, isoproterenol, and sodium nitroprusside was evaluated in organ-chamber experiments. Lipid peroxidation was estimated by malondialdehyde activity in liver tissue samples and by blood lactic dehydrogenase (LDH), serum aspartate aminotransferase (AST) and serum alanine aminotransferase (ALT) activities. No changes were observed in hepatic artery relaxation for any agonist tested. The group subjected to 45 min of ischemia and 120 min of reperfusion presented marked increases of serum aminotransferases (ALT = 2989 ± 1056 U/L and AST = 1268 ± 371 U/L; P < 0.01), LDH = 2887 ± 1213 IU/L; P < 0.01) and malondialdehyde in liver samples (0.360 ± 0.020 nmol/mgPT; P < 0.05). Under the experimental conditions utilized, no abnormal changes in hepatic arterial vasoreactivity were observed: endothelium-dependent and independent hepatic artery vasodilation were not impaired in this canine model of ischemia/reperfusion injury. In contrast to other vital organs and in the ischemia/reperfusion injury environment, dysfunction of the main artery endothelium is not the first site of reperfusion injury.

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http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2007000600016Test

المؤلفون: H.M. Molina, Adagmar Andriolo, Durval Rosa Borges, D.T. Ito

المساهمون: Universidade Federal de São Paulo (UNIFESP)

المصدر: Repositório Institucional da UNIFESP
Universidade Federal de São Paulo (UNIFESP)
instacron:UNIFESP
Brazilian Journal of Medical and Biological Research, Vol 40, Iss 3, Pp 343-348 (2007)
Brazilian Journal of Medical and Biological Research v.40 n.3 2007
Brazilian Journal of Medical and Biological Research
Associação Brasileira de Divulgação Científica (ABDC)
instacron:ABDC
Brazilian Journal of Medical and Biological Research, Volume: 40, Issue: 3, Pages: 343-348, Published: MAR 2007

مصطلحات موضوعية: Male, Physiology, Atorvastatin, Alcohol, Pharmacology, Liver injury, Biochemistry, Sulfobromophthalein, chemistry.chemical_compound, Liver Function Tests, General Pharmacology, Toxicology and Pharmaceutics, lcsh:QH301-705.5, media_common, lcsh:R5-920, General Neuroscience, Alanine Transaminase, Drug Synergism, General Medicine, Perfusion, Liver, Animal studies, lcsh:Medicine (General), Hepatotoxic, medicine.drug, Drug, medicine.medical_specialty, media_common.quotation_subject, Immunology, Biophysics, Oxygen Consumption, medicine, Animals, Pyrroles, Aspartate Aminotransferases, Rats, Wistar, Ethanol, L-Lactate Dehydrogenase, business.industry, Cell Biology, medicine.disease, Surgery, Rats, chemistry, lcsh:Biology (General), Heptanoic Acids, Liver function, business, Biomarkers

الوصف: Animal studies and premarketing clinical trials have revealed hepatotoxicity of statins, primarily minor elevations in serum alanine aminotransferase levels. The combined chronic use of medicines and eventual ethanol abuse are common and may present a synergistic action regarding liver injury. Our objective was to study the effect of the chronic use of atorvastatin associated with acute ethanol administration on the liver in a rat model. One group of rats was treated daily for 5 days a week for 2 months with 0.8 mg/kg atorvastatin by gavage. At the end of the treatment the livers were perfused with 72 mM ethanol for 60 min. Control groups (at least 4 animals in each group) consisted of a group of 2-month-old male Wistar EPM-1 rats exposed to 10% ethanol (v/v) ad libitum replacing water for 2 months, followed by perfusion of the liver with 61 nM atorvastatin for 60 min, and a group of animals without chronic ethanol treatment whose livers were perfused with atorvastatin and/or ethanol. The combination of atorvastatin with ethanol did not increase the release of injury marker enzymes (alanine aminotransferase, aspartate aminotransferase, and lactic dehydrogenase) from the liver and no change in liver function markers (bromosulfophthalein clearance, and oxygen consumption) was observed. Our results suggest that the combination of atorvastatin with ethanol is not more hepatotoxic than the separate use of each substance. Universidade Federal de São Paulo (UNIFESP) Escola Paulista de Medicina Departamento de Bioquímica Universidade Federal de São Paulo (UNIFESP) Escola Paulista de Medicina Departamento de Medicina UNIFESP, EPM, Depto. de Bioquímica UNIFESP, EPM, Depto. de Medicina SciELO

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المؤلفون: Kenneth B. Storey, Tetyana V. Bagnyukova, Janet M. Storey, Volodymyr I. Lushchak

المصدر: Brazilian Journal of Medical and Biological Research, Volume: 34, Issue: 8, Pages: 1055-1064, Published: AUG 2001
Scopus-Elsevier
Brazilian Journal of Medical and Biological Research, Vol 34, Iss 8, Pp 1055-1064 (2001)
Brazilian Journal of Medical and Biological Research v.34 n.8 2001
Brazilian Journal of Medical and Biological Research
Associação Brasileira de Divulgação Científica (ABDC)
instacron:ABDC

مصطلحات موضوعية: medicine.medical_specialty, swimming exercise, Physiology, Phosphofructokinase-1, Immunology, Biophysics, Trachurus mediterraneus, Biology, Biochemistry, chemistry.chemical_compound, Internal medicine, Lactate dehydrogenase, Physical Conditioning, Animal, medicine, Animals, Glycolysis, subcellular enzyme binding, General Pharmacology, Toxicology and Pharmaceutics, Muscle, Skeletal, lcsh:QH301-705.5, Swimming, chemistry.chemical_classification, lcsh:R5-920, Hexokinase, General Neuroscience, Aldolase A, Fishes, Brain, Cell Biology, General Medicine, glycolysis, Enzymes, Fructose-Bisphosphatase, Enzyme, Endocrinology, lcsh:Biology (General), chemistry, Liver, Phosphoglucomutase, biology.protein, lcsh:Medicine (General), Pyruvate kinase, Phosphofructokinase

الوصف: The effects of short-term burst (5 min at 1.8 m/s) swimming and long-term cruiser (60 min at 1.2 m/s) swimming on maximal enzyme activities and enzyme distribution between free and bound states were assessed for nine glycolytic and associated enzymes in tissues of horse mackerel, Trachurus mediterraneus ponticus. The effects of exercise were greatest in white muscle. The activities of phosphofructokinase (PFK), pyruvate kinase (PK), fructose-1,6-bisphosphatase (FBPase), and phosphoglucomutase (PGM) all decreased to 47, 37, 37 and 67%, respectively, during 60-min exercise and all enzymes except phosphoglucoisomerase (PGI) and PGM showed a change in the extent of binding to subcellular particulate fractions during exercise. In red muscle, exercise affected the activities of PGI, FBPase, PFK, and lactate dehydrogenase (LDH) and altered percent binding of only PK and LDH. In liver, exercise increased the PK activity 2.3-fold and reduced PGI 1.7-fold only after 5 min of exercise but altered the percent binding of seven enzymes. Fewer effects were seen in brain, with changes in the activities of aldolase and PGM and in percent binding of hexokinase, PFK and PK. Changes in enzyme activities and in binding interactions with subcellular particulate matter appear to support the altered demands of tissue energy metabolism during exercise.

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http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2001000800013&lng=en&tlng=enTest