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1.
Article in Spanish | LILACS, CUMED | ID: biblio-1536306

ABSTRACT

Fundamento: La enzima lactoperoxidasa tiocianato es una proteína producida por células epiteliales en los acinos mamarios. Los carcinomas de la mama constituyen un tipo de cáncer que se origina por la transformación maligna de las células acinares de la mama y se caracterizan por el crecimiento y multiplicación descontrolado. Por tanto, podría existir una correlación entre el cáncer de mama y el aumento de la actividad sérica de la lactoperoxidasa. Objetivo: Determinar la asociación entre el diagnóstico de carcinoma mamario y la actividad aumentada de la enzima lactoperoxidasa sérica en muestras de pacientes que han sido atendidos en el Hospital Oncológico María Curie de Camagüey en el periodo de abril a agosto del 2022. Métodos: Se desarrolló un estudio correlacional en el Centro de Inmunología y Productos Biológicos de Camagüey, en el período de abril a agosto del 2022. Se empleó la citología por aspiración con aguja fina para el diagnóstico histopatológico del carcinoma mamario y se determinó la actividad de la enzima lactoperoxidasa sérica mediante el método del pirogalol salicilato. Se emplearon las pruebas t de student y chi-cuadrado para el análisis estadístico de los datos. Resultados: El carcinoma ductal infiltrante fue el subtipo de cáncer más frecuente con un 94,1 por ciento del total de las muestras. Se encontraron diferencias significativas entre los grupos de muestras analizadas p ( 0.000. De un total de 34 muestras positivas, 32 presentaron aumento de la actividad enzimática. Conclusiones: Hubo asociación entre el diagnóstico de carcinoma mamario y niveles aumentados de la enzima lactoperoxidasa sérica(AU)


Background: The enzyme lactoperoxidase thiocyanate is a protein produced by epithelial cells in the mammary acini. Breast carcinomas are a type of cancer that originates from the malignant transformation of the acinar cells of the breast and are characterized by uncontrolled growth and multiplication. Therefore, there could be a correlation between breast cancer and increased serum lactoperoxidase activity. Objective: To determine the association between the diagnosis of mammary carcinoma and the increased activity of the serum lactoperoxidase enzyme in samples of patients who have been treated at the Maria Curie Oncology Hospital in Camagüey from April to August 2022. Methods: A correlational study was developed at the Center for Immunology and Biological Products of Camagüey, from April to August 2022. Fine-needle aspiration cytology was used for the histopathological diagnosis of mammary carcinoma and the activity of serum lactoperoxidase enzyme by the pyrogallol salicylate method. Student's t and chi-square tests were used in the statistical analysis of the data. Results: Infiltrating ductal carcinoma was the most frequent subtype of cancer with 94,1 percent of the total samples. Significant differences were found between the groups of samples analyzed p ( 0,000. Of a total of 34 positive samples, 32 showed increased enzyme activity. Conclusions: There was an association between the diagnosis of mammary carcinoma and increased levels of the serum lactoperoxidase enzyme(AU)


Subject(s)
Humans , Female , Pyrogallol/antagonists & inhibitors , Breast Neoplasms/diagnosis , Carcinoma, Ductal, Breast/epidemiology , Biopsy, Fine-Needle/methods , Enzyme Inhibitors/analysis , Correlation of Data
2.
Chinese Journal of Natural Medicines (English Ed.) ; (6): 194-201, 2022.
Article in English | WPRIM | ID: wpr-929251

ABSTRACT

Harmaline and harmine are β-carboline alkaloids with effective pharmacological effects. Harmaline can be transformed into harmine after oral administration. However, enzymes involved in the metabolic pathway remain unclear. In this study, harmaline was incubated with rat liver microsomes (RLM), rat brain microsomes (RBM), blood, plasma, broken blood cells, and heme peroxidases including horseradish peroxidase (HRP), lactoperoxidase (LPO), and myeloperoxidase (MPO). The production of harmine was determined by a validated UPLC-ESI-MS/MS method. Results showed that heme peroxidases catalyzed the oxidative dehydrogenation of harmaline. All the reactions were in accordance with the Hill equation. The reaction was inhibited by ascorbic acid and excess H2O2. The transformation of harmaline to harmine was confirmed after incubation with blood, plasma, and broken blood cells, rather than RLM and RBM. Harmaline was incubated with blood, plasma, and broken cells liquid for 3 h, and the formation of harmine became stable. Results indicated an integrated metabolic pathway of harmaline, which will lay foundation for the oxidation reaction of dihydro-β-carboline. Moreover, the metabolic stability of harmaline in blood should not be ignored when the pharmacokinetics study of harmaline is carried out.


Subject(s)
Animals , Rats , Harmaline/metabolism , Harmine/metabolism , Heme , Hydrogen Peroxide , Tandem Mass Spectrometry
3.
Arch. méd. Camaguey ; 26: e8376, 2022. tab, graf
Article in Spanish | LILACS-Express | LILACS | ID: biblio-1403273

ABSTRACT

RESUMEN Introducción: La enzima lactoperoxidasa tiocianato se produce por células epiteliales de las glándulas salivales y desempeña funciones defensivas contra microorganismos patógenos de la cavidad oral, por tanto, identificar su presencia por métodos cualitativos podría ser de utilidad para investigar una de las causas de infecciones orales recurrentes como la periodontitis, gingivitis y caries dental, donde se ha reportado una relación con los niveles bajos de esta enzima en diferentes estudios. Objetivo: Demostrar la utilidad del método pirogalol salicilato en la identificación de la enzima lactoperoxidasa tiocianato salival. Métodos: Se desarrolló un estudio piloto, descriptivo, observacional y transversal, en el Centro de Inmunología y Productos Biológicos de la provincia Camagüey, en el período de junio a octubre de 2020 mediante el empleo del método del pirogalol salicilato para identificar la presencia de la enzima lactoperoxidasa tiocianato en saliva humana. Se utilizaron 14 muestras de saliva que se analizaron después de la transformación enzimática del sustrato a 405 nm. Los datos obtenidos fueron procesados mediante estadística descriptiva. Resultados: La enzima lactoperoxidasa tiocianato se encontró en todas las muestras salivales estudiadas. La absorbancia de las muestras se halló entre 0,406 y 0,939 unidades. Conclusiones: El método del pirogalol salicilato resulta útil en la identificación de la enzima lactoperoxidasa tiocianato salival lo cual puede ser favorable en el estudio de infecciones bucales.


ABSTRACT Introduction: The enzyme lactoperoxidase thiocyanate is produced by epithelial cells of the salivary glands and performs defensive functions against pathogenic microorganisms of the oral cavity, therefore, identifying its presence by qualitative methods could be useful when investigating the causes of recurrent oral infections such as periodontitis, gingivitis and dental caries, in which a relationship with low levels of this enzyme has been reported in different studies. Objective: To demonstrate the usefulness of the pyrogallol salicylate method in the identification of the salivary enzyme lactoperoxidase thiocyanate. Methods: An observational and cross-sectional pilot study was carried out at the Center of Immunology and Biological Products of Camagüey, from June to October 2020, using the pyrogallol salicylate method to identify the lactoperoxidase thiocyanate enzyme in human saliva. Fourteen saliva samples were analyzed by observation and spectrophotometry at a wavelength of 405 nm. Descriptive statistical methods were applied to process data. Results: The enzyme lactoperoxidase thiocyanate was found in all the salivary samples studied. The absorbance of the samples ranged between 0,406 and 0,939. Conclusions: The pyrogallol salicylate method is useful in identifying the salivary lactoperoxidase enzyme, which may be favorable in the study of oral infections.

4.
Rev. Inst. Adolfo Lutz (Online) ; 78: 1-7, dez. 2019. tab
Article in Portuguese | LILACS, CONASS, ColecionaSUS, SES-SP, SESSP-ACVSES, SESSP-IALPROD, SES-SP, SESSP-IALACERVO | ID: biblio-1147467

ABSTRACT

O presente estudo analisou um binômio de tempo-temperatura alternativo para ser utilizado na pasteurização lenta sobre a inativação da fosfatase alcalina no leite caprino. Sua eficiência foi demonstrada pela contagem padrão em placas, e foi feita a comparação no processamento de leite refrigerado e congelado. Foram utilizados 18 tratamentos em leite caprino cru (nove em leite refrigerado e nove em leite congelado). Estes foram acondicionados em frascos de 300 mL, pasteurizados a 60, 63 e 65°C durante 10-20-30 minutos, e testadas às enzimas fosfatase alcalina e peroxidase. A contagem padrão em placas (CPP) e coliformes a 35 e 45°C foi feita nas amostras cruas e em cada tratamento, em duplicata. Após a pasteurização, todos os tratamentos apresentaram: não crescimento de microrganismos mesófilos, coliformes com <0,3 NMP/mL, prova de fosfatase negativa e peroxidase positiva. A pasteurização foi eficiente para melhorar a qualidade microbiológica do leite tanto refrigerado quanto congelado. Todos os binômios avaliados apresentaram resultados satisfatórios para alcançar os parâmetros preconizados em legislação, sugerindo-se o menor binômio (60°C por 10 min). Não houve diferença entre as formas de armazenamento das amostras: refrigerada ou congelada. (AU)


The objective of this study was to investigate an alternative time-temperature binomial to be used in the slow pasteurization on the alkaline phosphatase inactivation in the goat milk. Its efficiency was demonstrated with the standard counting in plates, and also refrigerated and the frozen milks processing were compared. Eighteen treatments were used in the raw goat milk (nine refrigerated milk and nine frozen milk). They were packed in 300 mL-flasks, pasteurized at 60-63-65°C for 10, 20, 30 minutes, and then tested for alkaline phosphatase and peroxidase enzymes. The standard counts in plates (CPP) and coliforms at 35°C and 45°C were performed in the raw samples and in the every treatment, in duplicate. After the pasteurization process, all of the treatments showed: no growth of mesophilic microorganisms, coliforms with <0.3 MPN / mL, negative phosphatase and positive peroxidase tests. The pasteurization was efficient to improve the microbiological quality of the milk either refrigerated or frozen. All of the evaluated binomials presented satisfactory results to reach the recommended parameters preconized in the legislation, suggesting the smaller binomial (60°C for 10 min). There was no difference between the samples storage form, either refrigerated or frozen. (AU)


Subject(s)
Goats , Milk , Alkaline Phosphatase , Coliforms , Pasteurization , Lactoperoxidase
5.
Rev. Inst. Adolfo Lutz ; 78: e1769, dez. 2019. tab
Article in Portuguese | LILACS, VETINDEX | ID: biblio-1489595

ABSTRACT

O presente estudo analisou um binômio de tempo-temperatura alternativo para ser utilizado na pasteurização lenta sobre a inativação da fosfatase alcalina no leite caprino. Sua eficiência foi demonstrada pela contagem padrão em placas, e foi feita a comparação no processamento de leite refrigerado e congelado. Foram utilizados 18 tratamentos em leite caprino cru (nove em leite refrigerado e nove em leite congelado). Estes foram acondicionados em frascos de 300 mL, pasteurizados a 60, 63 e 65°C durante 10-20-30 minutos, e testadas às enzimas fosfatase alcalina e peroxidase. A contagem padrão em placas (CPP) e coliformes a 35 e 45°C foi feita nas amostras cruas e em cada tratamento, em duplicata. Após a pasteurização, todos os tratamentos apresentaram: não crescimento de microrganismos mesófilos, coliformes com <0,3 NMP/mL, prova de fosfatase negativa e peroxidase positiva. A pasteurização foi eficiente para melhorar a qualidade microbiológica do leite tanto refrigerado quanto congelado. Todos os binômios avaliados apresentaram resultados satisfatórios para alcançar os parâmetros preconizados em legislação, sugerindo-se o menor binômio (60°C por 10 min). Não houve diferença entre as formas de armazenamento das amostras: refrigerada ou congelada.


The objective of this study was to investigate an alternative time-temperature binomial to be used in the slow pasteurization on the alkaline phosphatase inactivation in the goat milk. Its efficiency was demonstrated with the standard counting in plates, and also refrigerated and the frozen milks processing were compared. Eighteen treatments were used in the raw goat milk (nine refrigerated milk and nine frozen milk). They were packed in 300 mL-flasks, pasteurized at 60-63-65°C for 10, 20, 30 minutes, and then tested for alkaline phosphatase and peroxidase enzymes. The standard counts in plates (CPP) and coliforms at 35°C and 45°C were performed in the raw samples and in the every treatment, in duplicate. After the pasteurization process, all of the treatments showed: no growth of mesophilic microorganisms, coliforms with <0.3 MPN / mL, negative phosphatase and positive peroxidase tests. The pasteurization was efficient to improve the microbiological quality of the milk either refrigerated or frozen. All of the evaluated binomials presented satisfactory results to reach the recommended parameters preconized in the legislation, suggesting the smaller binomial (60°C for 10 min). There was no difference between the samples storage form, either refrigerated or frozen.


Subject(s)
Alkaline Phosphatase , Lactoperoxidase , Milk/chemistry , Pasteurization/methods , Goats , Coliforms , Mesophyll Cells
6.
Acta cir. bras ; 33(5): 462-471, May 2018. tab, graf
Article in English | LILACS | ID: biblio-949341

ABSTRACT

Abstract Purpose: To evaluate the effect of hyperbaric oxygenation (HBO) on the expression of the genes antioxidant glutathione peroxidase 4 (Gpx4) and lactoperoxidase (Lpo) in the lung of mice subjected to intestinal ischemia and reperfusion (IIR). Methods: Control group (CG) in which were subjected to anesthesia, laparotomy and observation for 120 minutes; an ischemia and reperfusion group (IRG) subjected to anesthesia, laparotomy, small bowel ischemia for 60 minutes and reperfusion for 60 minutes; and three groups treated with HBO during ischemia (HBOG + I), during reperfusion (HBOG + R) and during ischemia and reperfusion (HBOG + IR). Studied 84 genes of oxidative stress by the method (RT-qPCR). Genes with expression levels three times below or above the threshold cycle were considered significantly hypoexpressed or hyperexpressed, respectively (Student's t-test p<0.05). Results: Gpx4 and Lpo were hiperexpressed on IRG, showing a correlation with these genes with lung oxidative stress. Treated with HBO, there was a significant reduction on genic expression on HBOG+I. Conclusion: Hyperbaric oxygenation showed to be associated with decreased expression of these antioxidant genes, suggesting a beneficial effect on the mechanism of pulmonary oxidative stress whenever applied during the ischemia.


Subject(s)
Animals , Rats , Reperfusion Injury/metabolism , Oxidative Stress/genetics , Glutathione Peroxidase/metabolism , Hyperbaric Oxygenation/methods , Lactoperoxidase/genetics , Lung/metabolism , Oxidative Stress/drug effects , Disease Models, Animal , Intestines/blood supply , Ischemia/metabolism , Antioxidants/metabolism , Antioxidants/pharmacology
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