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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المؤلفون: L. S. Kattah, Marcelo M. Santoro, M.E. de Lima, Carlos R. Diniz

المصدر: Brazilian Journal of Medical and Biological Research, Vol 33, Iss 9, Pp 1093-1097 (2000)
Brazilian Journal of Medical and Biological Research, Volume: 33, Issue: 9, Pages: 1093-1097, Published: SEP 2000

مصطلحات موضوعية: guinea pig ileum, Physiology, Immunology, Biophysics, Venom, Phospholipase, Pharmacology, Biology, Neurotransmission, medicine.disease_cause, Biochemistry, chemistry.chemical_compound, Phospholipase A2, Lactate dehydrogenase, medicine, General Pharmacology, Toxicology and Pharmaceutics, Incubation, lcsh:QH301-705.5, Myenteric plexus, lcsh:R5-920, Toxin, General Neuroscience, crotoxin, Cell Biology, General Medicine, choline uptake, Crotalus durissus terrificus, chemistry, lcsh:Biology (General), biology.protein, phospholipase A2, lcsh:Medicine (General)

الوصف: We examined the effect of crotoxin, the neurotoxic complex from the venom of the South American rattlesnake Crotalus durissus terrificus, on the uptake of 3H-choline in minces of smooth muscle myenteric plexus from guinea pig ileum. In the concentration range used (0. 03-1 microM) and up to 10 min of treatment, crotoxin decreased 3H-choline uptake by 50-75% compared to control. This inhibition was time dependent and did not seem to be associated with the disruption of the neuronal membrane, because at least for the first 20 min of tissue exposure to the toxin (up to 1 microM) the levels of lactate dehydrogenase (LDH) released into the supernatant were similar to those of controls. Higher concentrations of crotoxin or more extensive incubation times with this toxin resulted in elevation of LDH activity detected in the assay supernatant. The inhibitory effect of crotoxin on 3H-choline uptake seems to be associated with its phospholipase activity since the equimolar substitution of Sr2+ for Ca2+ in the incubation medium or the modification of the toxin with p-bromophenacyl bromide substantially decreased this effect. Our results show that crotoxin inhibits 3H-choline uptake with high affinity (EC25 = 10 +/- 5 nM). We suggest that this inhibition could explain, at least in part, the blocking effect of crotoxin on neurotransmission.

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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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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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