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1.
Georgian Med News ; (349): 154-160, 2024 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-38963220

RESUMO

Mitochondrial dysfunction in autism leads to impair the mitochondria's ability to synthesis adenosine triphosphate (ATP) by impairment citric acid cycle as well as increase anaerobic glycolysis. Aim - measuring and evaluating the levels of mitochondrial markers; including glutamate oxaloacetate transaminase (GOT), glutamate pyruvate transaminase (GPT), malate dehydrogenase, and pyruvate kinase) in the autistic group and knowing the possibility of using these markers to diagnose children with autism spectrum disorder. A case-control study was done in the Al-Zahraa Teaching Hospital (Kut City, Iraq) on 100 Iraqi children (male and female), between (April 2023 and January 2024). Their ages ranged between 3 and 9 years. Among them were 50 patients enrolled as autistic group and 50 healthy enrolled as control group. Blood samples were collected and bioassays for GOT, GPT, pyruvate kinase, and malate dehydrogenase were measured by ELISA technique. The autistic group showed that the urine GOT, urine GPT, serum malate, and serum pyruvate levels in the ASD group was significantly higher (P<0.001) than the control group. The ROC analysis showed that urine GOT, urine GOT, serum malate and serum pyruvate had an accuracy level of (81%,71%,77%, and 80 %) and the area under the curve (AUC) was > 0.7 (0.8),0.7, 0.7(0.76), and 0.7(0.8) thus urine GOT, urine GPT, serum, malate, and serum pyruvate are a valid diagnostic marker. There was a significant difference in the mean urine and serum concentrations of mitochondrial markers (GOT, GPT, malate dehydrogenase, and pyruvate kinase) between autistic children and the control group due to mitochondrial dysfunction.


Assuntos
Aspartato Aminotransferases , Transtorno do Espectro Autista , Biomarcadores , Malato Desidrogenase , Mitocôndrias , Piruvato Quinase , Humanos , Criança , Masculino , Feminino , Transtorno do Espectro Autista/sangue , Malato Desidrogenase/sangue , Pré-Escolar , Estudos de Casos e Controles , Piruvato Quinase/sangue , Biomarcadores/sangue , Biomarcadores/urina , Aspartato Aminotransferases/sangue , Mitocôndrias/metabolismo , Alanina Transaminase/sangue , Ácido Pirúvico/sangue , Malatos/sangue , Curva ROC
2.
Med Arch ; 74(3): 168-171, 2020 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-32801429

RESUMO

INTRODUCTION: Pre-diabetic precedes the development of full diabetes. Studying and identification changes in pre-diabetic conditions can give the possibility to decline the development of diabetes and treat conditions associated with diabetes such as cardiovascular diseases. AIM: The main objectives of the present study were to investigate the potential of using Urtica pilulifera in treating the pre-diabetic rat model and to investigate its anti-oxidant impact. METHODS: The pre-diabetic model was induced in rats through daily giving high sucrose diet (35%) for 30 days. The extraction of U. pilulifera leaves was made as described by previous studies. Thirty male Wistar rats were randomly divided into three groups, control group (n=10), pre-diabetic group (n=10), and treated group with the extract of U. pilulifera (n=10). Control group rats received standard diet; pre-diabetic group rats received standard diet and high sucrose (35%) in drinking water, treated group rats received the same conditions as a pre-diabetic group, with intra-peritoneal injection of U. pilulifera injection on daily basis. After one month experiment, blood samples were taken from all rats and tested for glucose, triglycerides, cholesterol, GSH, TAC, and MDA. RESULTS: Both glucose and triglycerides levels were significantly increased in pre-diabetic groups, and significantly reduced in the treated group by the extract of U.pilulifera. The cholesterol level was not significantly changed in all groups. The levels of GSH were significantly reduced in the pre-diabetic group compared with the control group. Treatment with the extract of U. pilulifera increased the levels of GSH significantly compared with the pre-diabetic group. The levels of TAC were not significantly changed between the control group and the pre-diabetic group, but significantly increased in the treated group compared with the pre-diabetic group. The levels of MDA significantly increased in the pre-diabetic group compared with the control group, and significantly reduced in the treated group compared with the control group. CONCLUSION: High sucrose pre-diabetic model is a good model to study diabetes at early stages, and the treatment using U. pilulifera has several benefits in reducing glucose and lipid profile lipids as well as combating oxidative stress.


Assuntos
Estresse Oxidativo/efeitos dos fármacos , Fitoterapia , Estado Pré-Diabético/sangue , Estado Pré-Diabético/tratamento farmacológico , Urticaceae , Animais , Antioxidantes/metabolismo , Glicemia/efeitos dos fármacos , Glicemia/metabolismo , Colesterol/sangue , Modelos Animais de Doenças , Glutationa/sangue , Injeções Intraperitoneais , Malato Desidrogenase/sangue , Masculino , Extratos Vegetais/uso terapêutico , Distribuição Aleatória , Ratos , Ratos Wistar , Triglicerídeos/sangue
3.
Skelet Muscle ; 10(1): 12, 2020 04 27.
Artigo em Inglês | MEDLINE | ID: mdl-32340625

RESUMO

BACKGROUND: Pulmonary hypertension leads to right ventricular heart failure and ultimately to cardiac cachexia. Cardiac cachexia induces skeletal muscles atrophy and contractile dysfunction. MAFbx and MuRF1 are two key proteins that have been implicated in chronic muscle atrophy of several wasting states. METHODS: Monocrotaline (MCT) was injected over eight weeks into mice to establish pulmonary hypertension as a murine model for cardiac cachexia. The effects on skeletal muscle atrophy, myofiber force, and selected muscle proteins were evaluated in wild-type (WT), MuRF1, and MuRF2-KO mice by determining muscle weights, in vitro muscle force and enzyme activities in soleus and tibialis anterior (TA) muscle. RESULTS: In WT, MCT treatment induced wasting of soleus and TA mass, loss of myofiber force, and depletion of citrate synthase (CS), creatine kinase (CK), and malate dehydrogenase (MDH) (all key metabolic enzymes). This suggests that the murine MCT model is useful to mimic peripheral myopathies as found in human cardiac cachexia. In MuRF1 and MuRF2-KO mice, soleus and TA muscles were protected from atrophy, contractile dysfunction, while metabolic enzymes were not lowered in MuRF1 or MuRF2-KO mice. Furthermore, MuRF2 expression was lower in MuRF1KO mice when compared to C57BL/6 mice. CONCLUSIONS: In addition to MuRF1, inactivation of MuRF2 also provides a potent protection from peripheral myopathy in cardiac cachexia. The protection of metabolic enzymes in both MuRF1KO and MuRF2KO mice as well as the dependence of MuRF2 expression on MuRF1 suggests intimate relationships between MuRF1 and MuRF2 during muscle atrophy signaling.


Assuntos
Hipertensão Pulmonar/metabolismo , Proteínas Musculares/genética , Músculo Esquelético/metabolismo , Atrofia Muscular/metabolismo , Proteínas com Motivo Tripartido/genética , Ubiquitina-Proteína Ligases/genética , Animais , Citrato (si)-Sintase/sangue , Creatina Quinase/sangue , Hipertensão Pulmonar/complicações , Hipertensão Pulmonar/patologia , Malato Desidrogenase/sangue , Camundongos , Camundongos Endogâmicos C57BL , Contração Muscular , Proteínas Musculares/metabolismo , Força Muscular , Músculo Esquelético/patologia , Músculo Esquelético/fisiopatologia , Atrofia Muscular/etiologia , Atrofia Muscular/patologia , Proteínas com Motivo Tripartido/metabolismo , Ubiquitina-Proteína Ligases/metabolismo
4.
J Cachexia Sarcopenia Muscle ; 11(2): 505-517, 2020 04.
Artigo em Inglês | MEDLINE | ID: mdl-31881125

RESUMO

BACKGROUND: Duchenne muscular dystrophy (DMD) is a fatal disease for which no cure is available. Clinical trials have shown to be largely underpowered due to inter-individual variability and noisy outcome measures. The availability of biomarkers able to anticipate clinical benefit is highly needed to improve clinical trial design and facilitate drug development. METHODS: In this study, we aimed to appraise the value of protein biomarkers to predict prognosis and monitor disease progression or treatment outcome in patients affected by DMD. We collected clinical data and 303 blood samples from 157 DMD patients in three clinical centres; 78 patients contributed multiple blood samples over time, with a median follow-up time of 2 years. We employed linear mixed models to identify biomarkers that are associated with disease progression, wheelchair dependency, and treatment with corticosteroids and performed survival analysis to find biomarkers whose levels are associated with time to loss of ambulation. RESULTS: Our analysis led to the identification of 21 proteins whose levels significantly decrease with age and nine proteins whose levels significantly increase. Seven of these proteins are also differentially expressed in non-ambulant patients, and three proteins are differentially expressed in patients treated with glucocorticosteroids. Treatment with corticosteroids was found to partly counteract the effect of disease progression on two biomarkers, namely, malate dehydrogenase 2 (MDH2, P = 0.0003) and ankyrin repeat domain 2 (P = 0.0005); however, patients treated with corticosteroids experienced a further reduction on collagen 1 serum levels (P = 0.0003), especially following administration of deflazacort. A time to event analysis allowed to further support the use of MDH2 as a prognostic biomarker as it was associated with an increased risk of wheelchair dependence (P = 0.0003). The obtained data support the prospective evaluation of the identified biomarkers in natural history and clinical trials as exploratory biomarkers. CONCLUSIONS: We identified a number of serum biomarkers associated with disease progression, loss of ambulation, and treatment with corticosteroids. The identified biomarkers are promising candidate prognostic and surrogate biomarkers, which may support drug developers if confirmed in prospective studies. The serum levels of MDH2 are of particular interest, as they correlate with disease stage and response to treatment with corticosteroids, and are also associated with the risk of wheelchair dependency and pulmonary function.


Assuntos
Biomarcadores/sangue , Detecção Precoce de Câncer/métodos , Malato Desidrogenase/sangue , Adolescente , Adulto , Criança , Pré-Escolar , Progressão da Doença , Feminino , Humanos , Estudos Longitudinais , Masculino , Distrofia Muscular de Duchenne , Prognóstico , Adulto Jovem
5.
Artigo em Inglês | MEDLINE | ID: mdl-28750864

RESUMO

Glanders is a disease of horses, donkeys and mules. The causative agent Burkholderia mallei, is a biorisk group 3 pathogen and is also a biothreat agent. Simple and rapid diagnostic tool is essential for control of glanders. Using a proteomic approach and immunoblotting with equine sera, we identified 12 protein antigens that may have diagnostic potential. Various immunoreactive proteins e.g. GroEL, translation elongation factor Tu, elongation factor Ts, arginine deiminase, malate dehydrogenase, DNA directed RNA polymerase subunit alpha were identified on 2-dimentional immunoblots. One of these proteins, GroEL, was cloned and expressed in E. coli and purified using Ni-NTA affinity chromatography. The recombinant GroEL protein was evaluated in ELISA format on a panel of glanders positive (n=49) and negative (n=79) equine serum samples to determine its diagnostic potential. The developed ELISA had a sensitivity and specificity of 96 and 98.7% respectively. The results of this study highlight the potential of GroEL in serodiagnosis of glanders.


Assuntos
Anticorpos Antibacterianos/sangue , Antígenos de Bactérias/imunologia , Burkholderia mallei/imunologia , Chaperonina 60/imunologia , Mormo/diagnóstico , Doenças dos Cavalos/diagnóstico , Imunoproteínas/isolamento & purificação , Animais , Antígenos de Bactérias/sangue , Antígenos de Bactérias/isolamento & purificação , Burkholderia mallei/isolamento & purificação , Chaperonina 60/sangue , Chaperonina 60/genética , Ensaio de Imunoadsorção Enzimática/métodos , Escherichia coli/genética , Mormo/imunologia , Doenças dos Cavalos/imunologia , Doenças dos Cavalos/microbiologia , Cavalos , Hidrolases/sangue , Hidrolases/imunologia , Immunoblotting , Imunoproteínas/química , Malato Desidrogenase/sangue , Malato Desidrogenase/imunologia , Fator Tu de Elongação de Peptídeos/sangue , Fator Tu de Elongação de Peptídeos/imunologia , Fatores de Alongamento de Peptídeos/sangue , Fatores de Alongamento de Peptídeos/imunologia , Proteômica/métodos , Proteínas Recombinantes/imunologia , Proteínas Recombinantes/isolamento & purificação , Sensibilidade e Especificidade , Testes Sorológicos
6.
Oxid Med Cell Longev ; 2017: 1360565, 2017.
Artigo em Inglês | MEDLINE | ID: mdl-28337244

RESUMO

We have found selective elevation of serum enzyme activities in rats subjected to partial hepatectomy (PH), apparently controlled by hemodynamic flow-bearing physical forces. Here, we assess the involvement of stretch-sensitive calcium channels and calcium mobilization in isolated livers, after chemical modifications of the endothelial glycocalyx and changing perfusion directionality. Inhibiting in vivo protein synthesis, we found that liver enzyme release is influenced by de novo synthesis of endothelial glycocalyx components, and released enzymes are confined into a liver "pool." Moreover, liver enzyme release depended on extracellular calcium entry possibly mediated by stretch-sensitive calcium channels, and this endothelial-mediated mechanotransduction in liver enzyme release was also evidenced by modifying the glycocalyx carbohydrate components, directionality of perfusing flow rate, and the participation of nitric oxide (NO) and malondialdehyde (MDA), leading to modifications in the intracellular distribution of these enzymes mainly as nuclear enrichment of "mitochondrial" enzymes. In conclusion, the flow-induced shear stress may provide fine-tuned control of released hepatic enzymes through mediation by the endothelium glycocalyx, which provides evidence of a biological role of the enzyme release rather to be merely a biomarker for evaluating hepatotoxicity and liver damage, actually positively influencing progression of liver regeneration in mammals.


Assuntos
Endotélio Vascular/metabolismo , Glicocálix/metabolismo , Fígado/enzimologia , Fígado/cirurgia , Fluxo Sanguíneo Regional/fisiologia , Alanina Transaminase/sangue , Animais , Aspartato Aminotransferases/sangue , Cálcio/metabolismo , Bloqueadores dos Canais de Cálcio/farmacologia , Canais de Cálcio/química , Canais de Cálcio/metabolismo , Glutamato Desidrogenase/sangue , Fígado/efeitos dos fármacos , Fígado/lesões , Malato Desidrogenase/sangue , Masculino , Malondialdeído/sangue , Mecanotransdução Celular/efeitos dos fármacos , Óxido Nítrico/sangue , Ratos , Ratos Wistar , Fluxo Sanguíneo Regional/efeitos dos fármacos , Resistência ao Cisalhamento
7.
Toxicol Ind Health ; 31(12): 1318-24, 2015 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-23833244

RESUMO

The present study was undertaken to estimate the effect of occupational exposure to lead on the blood concentration of glucose and several enzymes involved in glycolysis, the citric acid cycle, and the pentose phosphate pathway. To estimate the degree of lipid peroxidation, the concentrations of conjugated dienes were determined. The examined group included 145 healthy male employees of lead-zinc works. Taking into account the mean blood lead levels, the examined group was divided into two subgroups. The control group was composed of 36 healthy male administrative workers. The markers of lead exposure were significantly elevated in both subgroups when compared with the controls. There were no significant changes in fasting glucose concentration and fructose-1,6-bisphosphate aldolase activity in the study population. The concentration of conjugated dienes was significantly higher in both subgroups, whereas the activity of malate dehydrogenase was significantly higher only in the group with higher exposure. The activities of lactate dehydrogenase and sorbitol dehydrogenase were significantly decreased in the examined subgroups. The activity of glucose-6-phosphate dehydrogenase decreased significantly in the group with higher exposure and could be the cause of the elevated concentrations of conjugated dienes. It is possible to conclude that lead interferes with carbohydrate metabolism, but compensatory mechanisms seem to be efficient, as glucose homeostasis in lead-exposed workers was not disturbed.


Assuntos
Metabolismo dos Carboidratos/efeitos dos fármacos , Intoxicação por Chumbo/metabolismo , Chumbo/toxicidade , Peroxidação de Lipídeos/efeitos dos fármacos , Doenças Profissionais/induzido quimicamente , Exposição Ocupacional/efeitos adversos , Adulto , Ácido Aminolevulínico/urina , Biomarcadores/sangue , Biomarcadores/urina , Glicemia/análise , Frutose-Bifosfato Aldolase/sangue , Humanos , Chumbo/sangue , Intoxicação por Chumbo/sangue , Intoxicação por Chumbo/urina , Malato Desidrogenase/sangue , Masculino , Metalurgia , Pessoa de Meia-Idade , Doenças Profissionais/sangue , Doenças Profissionais/metabolismo , Doenças Profissionais/urina , Estresse Oxidativo/efeitos dos fármacos , Via de Pentose Fosfato/efeitos dos fármacos , Polônia , Protoporfirinas/sangue , Recursos Humanos
8.
Toxicol Sci ; 132(2): 276-83, 2013 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-23339181

RESUMO

Hepatotoxicity remains a major challenge in drug development. Although alanine aminotransferase (ALT) remains the gold standard biomarker of liver injury, alternative biomarker strategies to better predict the potential for severe drug-induced liver injury (DILI) are essential. In this study, we evaluated the utility of glutamate dehydrogenase (GLDH), purine nucleoside phosphorylase (PNP), malate dehydrogenase (MDH), and paraxonase 1 (PON1) as indicators of liver injury in cohorts of human subjects, including healthy subjects across age and gender, subjects with a variety of liver impairments, and several cases of acetaminophen poisoning. In the healthy subjects, levels of GLDH and MDH were not affected by age or gender. Reference ranges for GLDH and MDH in healthy subjects were 1-10 and 79-176U/L, respectively. In contrast, the levels of PON1 and PNP were not consistent across cohorts of healthy subjects. Furthermore, GLDH and MDH had a strong correlation with elevated ALT levels and possessed a high predictive power for liver injury, as determined by ROC analysis. In contrast, PON1 and PNP did not detect liver injury in our study. Finally, evaluation of patients with acetaminophen-induced liver injury provided evidence that both GLDH and MDH might have utility as biomarkers of DILI in humans. This study is the first to evaluate GLDH, MDH, PON1, and PNP in a large number of human subjects and, and it provides an impetus for prospective clinical studies to fully evaluate the diagnostic value of GLDH and MDH for detection of liver injury.


Assuntos
Biomarcadores/sangue , Doença Hepática Induzida por Substâncias e Drogas/sangue , Acetaminofen/toxicidade , Alanina Transaminase/sangue , Arildialquilfosfatase/sangue , Feminino , Glutamato Desidrogenase/sangue , Humanos , Malato Desidrogenase/sangue , Masculino , Purina-Núcleosídeo Fosforilase/sangue
9.
Vet Res Commun ; 36(2): 149-55, 2012 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-22297553

RESUMO

Continuous high intensity training may induce alterations to enzyme activities related to glucose and lipid metabolism in horses. In our study, five Thoroughbred race horses (3 male and 2 female, avg age=5 yrs old) were compared against five riding horses (1 male, 1 female, 3 gelding, avg age=13 yrs old) in terms of energy metabolism, by examining plasma malate (MDH) and lactate (LDH) dehydrogenase activities and M/L ratio. MDH is involved in NADH and ATP generation, whereas LDH can convert NADH back into NAD(+) for ATP generation. An increase in plasma M/L ratio can reflect heightened energy metabolism in the liver and skeletal muscle of horses adapted to continuous intensive exercise. Moreover, plasma lipid metabolism analytes (adiponectin, NEFA, total cholesterol (T-Cho), and triglycerides (TG)) can reflect changes to lipolysis rate, which can also indicate a change in energy metabolism. Overall, race horses demonstrated increased MDH and LDH activity in plasma (4x and 2x greater, respectively), in addition to a plasma M/L ratio twice as high as that of riding horses (2.0 vs 1.0). In addition, race horses also demonstrated significantly higher levels of plasma NEFA (50% greater), TG (2x greater), and T-Cho (20% greater) as compared to riding horses. Therefore, race horse muscles may have adapted to prolonged high intensity endurance exercise by gaining a higher oxidative capacity and an increased capacity for fat utilization as an energy source, resulting in heightened energy metabolism and increased rate of lipid mobilization.


Assuntos
Cavalos/sangue , Cavalos/fisiologia , L-Lactato Desidrogenase/sangue , Metabolismo dos Lipídeos/fisiologia , Malato Desidrogenase/sangue , Condicionamento Físico Animal/fisiologia , Animais , Metabolismo Energético/fisiologia , Ácidos Graxos não Esterificados/sangue , Feminino , L-Lactato Desidrogenase/metabolismo , Lipídeos/sangue , Malato Desidrogenase/metabolismo , Masculino , Fatores de Tempo
10.
Chem Res Toxicol ; 24(11): 1915-23, 2011 Nov 21.
Artigo em Inglês | MEDLINE | ID: mdl-21988407

RESUMO

S-(1,2-Dichlorovinyl)-L-cysteine sulfoxide (DCVCS) is a reactive and potent nephrotoxic metabolite of the human trichloroethylene metabolite S-(1,2-dichlorovinyl)-L-cysteine (DCVC). Because DCVCS covalent binding to kidney proteins likely plays a role in its nephrotoxicity, in this study biotin-tagged DCVCS, N-biotinyl-DCVCS (NB-DCVCS), was synthesized, and its stability in buffer alone and in the presence of rat blood or plasma was characterized in vitro. In addition, reactivity toward GSH and covalent binding to selected model enzymes and isolated kidney proteins were characterized. The half-lives of NB-DCVCS (39.6 min) and the DCVCS (diastereomer 1, 14.4 min; diastereomer 2, 6 min) in the presence of GSH were comparable. Incubating the model enzymes glutathione reductase and malate dehydrogenase with 10 µM NB-DCVCS for 3 h at 37 °C followed by immunoblotting using antibiotin antibodies demonstrated that glutathione reductase and malate dehydrogenase were extensively modified by NB-DCVCS. When rat kidney cytosol (6 µg/µL) was incubated with NB-DCVCS (312.5 nM to 5 µM) for 3 h at 37 °C followed by immunoblotting, a concentration-dependent increase in signal with multiple proteins with different molecular weights was observed, suggesting that NB-DCVCS binds to multiple kidney proteins with different selectivity. Incubating rat kidney cytosol with DCVCS (10-100 µM) prior to the addition of NB-DCVCS (2.5 µM) reduced the immunoblotting signal, suggesting that NB-DCVCS and DCVCS compete for the same binding sites. A comparison of the stability of NB-DCVCS and DCVCS in rat blood and plasma was determined in vitro, and NB-DCVCS exhibited higher stability than DCVCS in both media. Collectively, these results suggest that NB-DCVCS shows sufficient stability, reactivity, and selectivity to warrant further investigations into its possible use as a tool for future characterization of the role of covalent modification of renal proteins by DCVCS in nephrotoxicity.


Assuntos
Biotina/metabolismo , Cisteína/análogos & derivados , Glutationa Redutase/sangue , Indicadores e Reagentes/análise , Neoplasias Renais/sangue , Rim/metabolismo , Malato Desidrogenase/sangue , Animais , Sítios de Ligação , Ligação Competitiva , Biotina/química , Biotinilação , Western Blotting , Cisteína/efeitos adversos , Cisteína/química , Cisteína/metabolismo , Cisteína/toxicidade , Relação Dose-Resposta a Droga , Estabilidade de Medicamentos , Eletroforese em Gel de Poliacrilamida , Glutationa Redutase/química , Meia-Vida , Humanos , Indicadores e Reagentes/química , Rim/efeitos dos fármacos , Rim/patologia , Neoplasias Renais/etiologia , Neoplasias Renais/patologia , Malato Desidrogenase/química , Ligação Proteica , Ratos Sprague-Dawley
11.
Acta Cir Bras ; 26 Suppl 1: 26-31, 2011.
Artigo em Inglês | MEDLINE | ID: mdl-21971653

RESUMO

PURPOSE: To determine the effects of oral L-glutamine (L-Gln) and the dipeptide L-alanyl-glutamine (L-Ala-Gln) upon the activity of the malate-aspartate shuttle in the rat distal small intestine following ischemia and reperfusion. METHODS: Seventy-two Wistar rats (350-400g), were randomized in 2 groups (n = 36): group S (Sham) and Group T (Treatment) and divided into 12 subgroups (n = 6): A-A6, and B1-B6. The subgroups A1-A3 were subjected to sham procedures at 30 and 60 minutes. Thirty minutes before the study, rats were treated with calcium caseinate, 0.5g/Kg (subgroups A1, A4, B1, B4), L-Gln, 0.5g / kg (subgroups A2, A5, B2 and B5) or L-Ala-Gln, 0.75g/Kg (subgroups A3, A6, B3, B6), administered by gavage. Ischemia was achieved by clamping the mesenteric vessels, delimiting a segment of bowel 5 cm long and 5 cm apart from the ileocecal valve. Samples were collected 30 and 60 minutes after start of the study for real-time PCR assay of malate dehydrogenases (MDH1-2) and aspartate-aminotransferases (GOT1-2) enzymes. RESULTS: Tissue MDH and GOT mRNA expression in intestinal samples from rats preconditioned with either L-Gln or L-Ala-Gln showed no significant differences both during ischemia and early reperfusion. CONCLUSION: Activation of the malate-aspartate shuttle system appears not to be the mechanism of glutamine-mediated elevation of glucose oxidation in rat intestine during ischemia/reperfusion injury.


Assuntos
Ácido Aspártico/metabolismo , Glutamina/farmacologia , Intestino Delgado/irrigação sanguínea , Malatos/metabolismo , RNA Mensageiro/sangue , Traumatismo por Reperfusão/prevenção & controle , Animais , Aspartato Aminotransferases/sangue , Aspartato Aminotransferases/genética , Dipeptídeos/farmacologia , Modelos Animais de Doenças , Intestino Delgado/enzimologia , Malato Desidrogenase/sangue , Malato Desidrogenase/genética , Distribuição Aleatória , Ratos , Ratos Wistar , Reação em Cadeia da Polimerase em Tempo Real , Traumatismo por Reperfusão/enzimologia , Fatores de Tempo
12.
Biochem Genet ; 49(7-8): 511-22, 2011 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-21394610

RESUMO

To determine the genetic structure and variation of Van cats and some other cats, seven enzyme loci were examined using horizontal starch gel electrophoresis. ME bands were observed for the first time in cats. For the enzyme loci CA ( 1 ), SOD, GPI, and GOT, neither the individual Van cats nor the specimens of other cat species exhibited any variation. These enzymes presented identical bands, all of which were homozygous. With respect to the PGD, ME, and ESD loci, however, genetic variation was observed in all of the cats. Hence, three of the seven gene-enzyme systems (43%) were polymorphic with two alleles, contributing to an estimate of average heterozygosity of 0.33-0.49 for the Van cats. PGD was the most discriminatory among the three polymorphic loci. The phylogenetic tree indicated that the Van, Persian, Turkish Angora, and Turkish Tekir cats are distinct from Siamese and Bombay cats.


Assuntos
Gatos/genética , Enzimas/genética , Variação Genética , Animais , Anidrase Carbônica I/sangue , Anidrase Carbônica I/genética , Enzimas/sangue , Cor de Olho/genética , Feminino , Glucose-6-Fosfato Isomerase/sangue , Glucose-6-Fosfato Isomerase/genética , Heterozigoto , Malato Desidrogenase/sangue , Malato Desidrogenase/genética , Masculino , Filogenia , Polimorfismo Genético , Superóxido Dismutase/sangue , Superóxido Dismutase/genética , Tioléster Hidrolases/sangue , Tioléster Hidrolases/genética , Turquia
13.
Mol Cell Biochem ; 350(1-2): 163-8, 2011 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-21188623

RESUMO

Coronary artery disease is a multifunctional disease and represents one of the leading causes of death worldwide. Oxidative stress appears as an etiological factor for myocardial damage during acute myocardial infarction. Some data suggest that acute coronary syndromes may also be influenced by matrix metalloproteinases through degradation of the fibrous cap of vulnerable atherosclerotic lesions. It has been indicated that gelatinases A and B play a key role in acute myocardial infarction and deoxyribonuclease I has been postulated to be a novel early phase marker of disease. The aim was to study activity of gelatinases A and B in acute myocardial infarction and its association with some membrane damage markers. Seventy-five patients with disease and seventy-five healthy controls were enrolled. Activities of lactate dehydrogenase, malate dehydrogenase, and deoxyribonuclease I were estimated using standard spectrophotometric assay and isoforms of lactate and malate dehydrogenases were determined using direct zymography. Activity of dehydrogenases was significantly higher in patients, while deoxyribonuclease I was lower. Isoform 2 of lactate dehydrogenase was significantly higher in the patient group. Gelatinases A and B were detected only in patients group. The results suggest determination of serum malate dehydrogenase activity to be used as an additional parameter for acute myocardial infarction diagnosis. Those findings suggest important role of gelatinases A and B as biomarkers of early stage of acute myocardial infarction together with membrane damage parameters.


Assuntos
Biomarcadores/sangue , Membrana Celular/patologia , Metaloproteinases da Matriz/fisiologia , Infarto do Miocárdio/sangue , Infarto do Miocárdio/diagnóstico , Idoso , Biomarcadores/metabolismo , Estudos de Casos e Controles , Membrana Celular/metabolismo , Desoxirribonuclease I/sangue , Desoxirribonuclease I/metabolismo , Feminino , Humanos , Isoenzimas/sangue , Isoenzimas/metabolismo , L-Lactato Desidrogenase/sangue , L-Lactato Desidrogenase/metabolismo , Malato Desidrogenase/sangue , Malato Desidrogenase/metabolismo , Masculino , Metaloproteinases da Matriz/metabolismo , Pessoa de Meia-Idade , Índice de Gravidade de Doença
14.
Acta cir. bras ; 26(supl.1): 26-31, 2011. ilus, graf
Artigo em Inglês | LILACS | ID: lil-600653

RESUMO

PURPOSE: To determine the effects of oral L-glutamine (L-Gln) and the dipeptide l-alanyl-glutamine (L-Ala-Gln) upon the activity of the malate-aspartate shuttle in the rat distal small intestine following ischemia and reperfusion. METHODS: Seventy-two Wistar rats (350-400g), were randomized in 2 groups (n = 36): group S (Sham) and Group T (Treatment) and divided into 12 subgroups (n = 6): A-A6, and B1-B6. The subgroups A1-A3 were subjected to sham procedures at 30 and 60 minutes. Thirty minutes before the study, rats were treated with calcium caseinate, 0.5g/Kg (subgroups A1, A4, B1, B4), L-Gln, 0.5g / kg (subgroups A2, A5, B2 and B5) or L-Ala-Gln, 0.75g/Kg (subgroups A3, A6, B3, B6), administered by gavage. Ischemia was achieved by clamping the mesenteric vessels, delimiting a segment of bowel 5 cm long and 5 cm apart from the ileocecal valve. Samples were collected 30 and 60 minutes after start of the study for real-time PCR assay of malate dehydrogenases (MDH1-2) and aspartate-aminotransferases (GOT1-2) enzymes. RESULTS: Tissue MDH and GOT mRNA expression in intestinal samples from rats preconditioned with either L-Gln or L-Ala-Gln showed no significant differences both during ischemia and early reperfusion. CONCLUSION: Activation of the malate-aspartate shuttle system appears not to be the mechanism of glutamine-mediated elevation of glucose oxidation in rat intestine during ischemia/reperfusion injury.


OBJETIVO: Determinar os efeitos da administração oral de L-glutamina (L-Gln) e do dipeptídeo L-alanil-glutamina (L-Ala-Gln) sobre a atividade do ciclo malato-aspartato no intestino delgado distal de ratos após isquemia/reperfusão. MÉTODOS: Setenta e dois ratos Wistar (350-400g) foram randomizados em 2 grupos (n = 36): T grupo S (Sham) e grupo (Tratamento) e distribuídos em 12 subgrupos (n = 6): A-A6, e B1-B6. Os subgrupos A1-A3 foram submetidos a procedimentos "sham" aos 30 e 60 minutos. Trinta minutos antes do estudo, os ratos foram tratados com caseinato de cálcio, 0,5 g/kg (subgrupos A1, A4, B1 e B4), L-Gln, 0,5 g/kg (subgrupos A2, A5, B2 e B5) ou L-Ala -Gln, 0,75g/kg (subgrupos A3, A6, B3, B6), administrado por gavagem. A isquemia foi obtida por pinçamento dos vasos mesentéricos, delimitando um segmento do intestino cinco centímetros de comprimento e 5 cm da válvula ileocecal. Amostras foram coletadas aos 30-60 minutos para ensaio de PCR em tempo real das enzimas malato desidrogenases (MDH1-2), aspartato-aminotransferase (GOT1-2). RESULTADOS: A expressão de MDH e GOT mRNA nas amostras provenientes do intestino delgado de ratos pré-condicionados com L-Gln ou L-Ala-Gln não apresentou diferenças significativas, tanto durante a isquemia como na fase inicial de reperfusão. CONCLUSÃO: Ativação do ciclo malato-aspartato não parece ser o mecanismo de elevação glutamina-mediada da oxidação da glicose no intestino de ratos durante a isquemia / reperfusão.


Assuntos
Animais , Ratos , Ácido Aspártico/metabolismo , Glutamina/farmacologia , Intestino Delgado/irrigação sanguínea , Malatos/metabolismo , RNA Mensageiro/sangue , Traumatismo por Reperfusão/prevenção & controle , Aspartato Aminotransferases/sangue , Aspartato Aminotransferases/genética , Modelos Animais de Doenças , Dipeptídeos/farmacologia , Intestino Delgado/enzimologia , Malato Desidrogenase/sangue , Malato Desidrogenase/genética , Distribuição Aleatória , Ratos Wistar , Reação em Cadeia da Polimerase em Tempo Real , Traumatismo por Reperfusão/enzimologia , Fatores de Tempo
15.
J Vet Med A Physiol Pathol Clin Med ; 54(7): 342-5, 2007 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-17718805

RESUMO

Concentrations of metabolites and immunoreactive insulin (IRI) and activities of enzymes related to energy metabolism were measured in plasma of Korean and Japanese beef cattle, which were raised by the indoor feeding system programmed to feed larger amount of roughage in their growing periods and larger amount of concentrate diet in their finishing periods (Japanese feeding system), and grazing New Zealand beef cattle. By the Japanese beef grading system, Korean and Japanese beef cattle showed high beef quality score, average grade 3.3 and 3.6, respectively. The plasma free fatty acid and lactate concentrations and lactate dehydrogenase (LDH), malate dehydrogenase (MDH) and aspartate aminotransferase (AST) activities in Korean beef cattle were significantly higher than those in Japanese beef cattle. The plasma lactate concentration in Korean beef cattle was 8.40 mmol/l, which was similar to the values observed in lactic acidosis. The higher activities of plasma LDH, MDH and AST may indicate slight liver damage by slightly acidotic conditions in Korean beef cattle. New Zealand beef cattle fed on pasture which they harvest by grazing showed significantly lower plasma glucose, cholesterol, lactate and IRI concentrations and enzyme activities than those in Korean and Japanese beef cattle fed on larger amount of concentrate diets. Plasma metabolite concentrations and energy metabolism-related enzyme activities may be good indicators for evaluating metabolic conditions of beef cattle raised by different feeding systems.


Assuntos
Ração Animal , Fenômenos Fisiológicos da Nutrição Animal/fisiologia , Bovinos/sangue , Metabolismo Energético/fisiologia , Carne/normas , Animais , Aspartato Aminotransferases/sangue , Aspartato Aminotransferases/metabolismo , Bovinos/metabolismo , Insulina/sangue , Japão , Coreia (Geográfico) , L-Lactato Desidrogenase/sangue , L-Lactato Desidrogenase/metabolismo , Malato Desidrogenase/sangue , Malato Desidrogenase/metabolismo , Masculino , Nova Zelândia
16.
Toxicology ; 234(1-2): 21-33, 2007 May 05.
Artigo em Inglês | MEDLINE | ID: mdl-17368689

RESUMO

Decreases in serum total thyroxine (TT4) and free thyroxine (FT4) without a compensatory rise in thyroid stimulating hormone (thyrotropin or TSH) or histological changes of the thyroid have been observed in studies with perfluorooctanesulfonate (PFOS) treatments in rats. Prior observations do not fit the clinical profile of a hypothyroid state. PFOS is known to compete with fatty acids for albumin binding, and serum free fatty acids (FFA) are known to interfere with FT4 measurement using analog methods due to competition for protein binding. Therefore, we hypothesized that measured decreases in serum FT4 by analog methods in the presence of PFOS were due to carrier protein binding interference. We compared FT4 analog assay methods with a reference method using equilibrium dialysis (ED-RIA) for FT4 measurement in rat sera in vitro and in vivo. We also measured hepatic malic enzyme mRNA transcripts and activity as a marker for hepatic thyroid hormone response. PFOS did not reduce serum TT4 and FT4 in vitro at concentrations up to 200 microM. After three daily 5mg/kg oral doses of potassium PFOS to female rats, serum TSH and FT4 by ED-RIA were unchanged (although FT4 determined by two common analog methods was decreased), and malic enzyme was not suppressed. These data suggest that prior reports of reduced free thyroid hormone in the presence of PFOS were due to negative bias in analog methods and that short-term PFOS treatment does not suppress the physiological thyroid status in rats. A reference method such as ED-RIA should be used for determination of serum FT4 in the presence of PFOS.


Assuntos
Ácidos Alcanossulfônicos/sangue , Fluorocarbonos/sangue , Tiroxina/sangue , Administração Oral , Ácidos Alcanossulfônicos/administração & dosagem , Animais , Técnicas de Laboratório Clínico/normas , Relação Dose-Resposta a Droga , Feminino , Fluorocarbonos/administração & dosagem , Soluções para Hemodiálise/química , Fígado/efeitos dos fármacos , Fígado/enzimologia , Medições Luminescentes/métodos , Malato Desidrogenase/sangue , Malato Desidrogenase/efeitos dos fármacos , Malato Desidrogenase/genética , Ácido Oleico/farmacologia , RNA/genética , RNA/metabolismo , Radioimunoensaio/métodos , Ratos , Ratos Sprague-Dawley , Reprodutibilidade dos Testes , Reação em Cadeia da Polimerase Via Transcriptase Reversa , Espectrometria de Massas em Tandem/métodos , Tireotropina/sangue , Tireotropina/imunologia
18.
Urologiia ; (6): 31-6, 2007.
Artigo em Russo | MEDLINE | ID: mdl-18649657

RESUMO

The activity of lactate dehydrogenase (LDG), malate dehydrogenase (MDG), concentrations of lactic acid and lipid peroxidation (LPO) products in the blood serum and urine were estimated in 119 patients with acute pyelonephritis (70 cases of serous and 49 cases of purulent). The results of the study showed that acute pyelonephritis patients have activated anaerobic glycolysis. Ischemia leads to accumulation of lactic acid, activation of LPO. Significant differences between the groups of patients reflect strong influence of renaltissue ischemia on activity of systemic metabolic processes and metabolism in renal parenchyma. Standard infusion therapy was given to 30 patients with acute purulent pyelonephritis. 19 patients received solution of succinic acid reamberin. On day 4 of reamberin therapy plasma and urine activity of LDG and MDG attenuated, lactic acid concentration decreased, content of dienic conjugates was close to normal. Patients on reamberin treatment exhibited earlier relief of endogenic intoxication and improvement of blood count. Thus, succinic acid drugs reduce renal ischemia, improve a course of postoperative period in patients with acute purulent pyelonephritis.


Assuntos
Isquemia/tratamento farmacológico , Rim , Pielonefrite , Ácido Succínico/administração & dosagem , Doença Aguda , Adolescente , Adulto , Idoso , Idoso de 80 Anos ou mais , Feminino , Glicólise/efeitos dos fármacos , Humanos , Infusões Intraósseas , Isquemia/sangue , Isquemia/complicações , Isquemia/urina , Rim/irrigação sanguínea , L-Lactato Desidrogenase/sangue , L-Lactato Desidrogenase/urina , Ácido Láctico/sangue , Ácido Láctico/urina , Peroxidação de Lipídeos/efeitos dos fármacos , Malato Desidrogenase/sangue , Malato Desidrogenase/urina , Masculino , Pessoa de Meia-Idade , Pielonefrite/sangue , Pielonefrite/complicações , Pielonefrite/cirurgia , Pielonefrite/urina , Estudos Retrospectivos , Fatores de Tempo
19.
Vet Res Commun ; 30(1): 29-38, 2006 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-16362608

RESUMO

Activities of enzymes related to energy metabolism and isoenzyme patterns of lactate dehydrogenase (LDH) were determined in peripheral leukocytes and livers of Holstein dairy cows and Institute of Cancer Research (ICR) mice. In dairy cow liver, activities of enzymes in glycolysis, malate-aspartate shuttle and lipogenesis were lower, but activities of glucose-6-phosphatase in gluconeogenesis were higher than those in mouse liver. Glucokinase activities were below detection limit in leukocytes and liver of the cows. Dairy cow leukocytes and liver showed the isoenzyme patterns with dominance of LDH-1, -2 and-3, whereas mouse leukocytes and liver showed that LDH-5 was dominant. The LDH isoenzyme patterns were very similar between leukocytes and liver in each animal species. Some enzymes in leukocytes may reflect those enzymes activities in liver and be a useful indicator for energy metabolism in animals.


Assuntos
Bovinos/metabolismo , Metabolismo Energético/fisiologia , L-Lactato Desidrogenase/metabolismo , Leucócitos Mononucleares/enzimologia , Fígado/enzimologia , Animais , Glicemia/metabolismo , Bovinos/sangue , Eletroforese em Gel de Poliacrilamida/veterinária , Ácidos Graxos não Esterificados/sangue , Feminino , Isoenzimas/sangue , Isoenzimas/metabolismo , L-Lactato Desidrogenase/sangue , Malato Desidrogenase/sangue , Camundongos , Camundongos Endogâmicos ICR , Triglicerídeos/sangue
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