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1.
Physiol Behav ; 270: 114320, 2023 10 15.
Artigo em Inglês | MEDLINE | ID: mdl-37558044

RESUMO

The effectiveness of exercise to reduce body mass is typically modest, partially due to energy compensation responses which may be linked to energy substrate availability around exercise. The present study aimed to investigate the effect of manipulating post-exercise energy substrate availability (high carbohydrate/low fat [HCLF] or low carbohydrate/high fat [LCHF] energy replacement) on energy balance components in the short-term (i.e., appetite, energy intake (EI) and energy expenditure (EE)). METHODS: Appetite, EI, activity- and total- EE were measured in twelve healthy, young (21.0 ± 2.3 years) physically active participants (10 men, 2 women) on two occasions across 4 days after a 75-min run and an isocaloric energy replacement drink (HCLF and LCHF). Appetite was measured daily by visual analogue scales, EI was calculated by subtracting the energy content of food leftovers from a provided food package, activity- and total- EE determined by heart-rate accelerometery. RESULTS: Composite appetite ratings between days were lower in HCLF (62.4 ± 12) compared to LCHF (68.3 ± 8.9 mm; p = 0.048). No differences between conditions were detected for EI. Cumulative activity-EE (HCLF=  20.9 ± 3.7, LCHF=  16.9 ± 3.1 MJ; p = 0.037), but not total-EE (HCLF=  44.6 ± 7.7, LCHF=  39.9 ± 4.7 MJ; p = 0.060), was higher for the HCLF condition than the LCHF across the measurement period. CONCLUSION: Compared with low carbohydrate/high fat, immediate post-exercise energy replacement with a high carbohydrate/low fat drink resulted in higher short-term activity energy expenditure and lower appetite ratings.


Assuntos
Apetite , Exercício Físico , Masculino , Humanos , Feminino , Apetite/fisiologia , Exercício Físico/fisiologia , Metabolismo Energético/fisiologia , Nutrientes , Ingestão de Energia/fisiologia , Carboidratos
2.
Cryo Letters ; 42(3): 154-158, 2021.
Artigo em Inglês | MEDLINE | ID: mdl-33970993

RESUMO

BACKGROUND: Cryolipolysis is a non-invasive method capable of reducing the thickness of the fat layer. OBJECTIVE: To evaluate the effects of cryolipolysis with the use of plate applicators in the treatment of abdominal fat in women. MATERIALS AND METHODS: The sample was composed of 15 participants, who were evaluated before and at the end of the intervention. Three applications of cryolipolysis were performed in the infraumbilical portion of the abdominal region. The volunteers were divided into three groups G-1 (temperature of -2°C), G-2 (temperature of -3°C) and G3 (temperature of -4°C). RESULTS: There was a reduction in plicometry measurements in groups G2 and G3, in the comparison between the initial and final moments (p <0.05), and a reduction in perimetry and ultrasound (p < 0.05) in all groups. It was found that the G3 group was subject to higher risk of first degree burns and redness when compared to the other groups. CONCLUSION: It is suggested that plate cryolipolysis is a possibly effective resource for reducing adiposity, as shown in the evaluation of perimetry, plicometry, and ultrasound results, and in the photographic analysis.


Assuntos
Gordura Abdominal , Adiposidade , Crioterapia , Lipólise , Feminino , Humanos , Sobrepeso/terapia , Resultado do Tratamento , Ultrassonografia
3.
Rev. méd. Chile ; 147(11): 1468-1486, nov. 2019. tab
Artigo em Espanhol | LILACS | ID: biblio-1094177

RESUMO

Physical exercise is useful in people who underwent bariatric surgery. However, the right dosage is still a topic for discussion. The aim of this article is to consolidate the prescription criteria for physical activity and exercise in bariatric patients. A panel of experts to whom the topics were previously assigned for review, met to reach a consensus. Each topic was presented and subjected to discussion and voting by the participants and attendants who were exercise professionals from different obesity treatment centers. We report the conclusions reached for aerobic exercise, strength training, protein supplementation and physical activity for weight maintenance in bariatric patients.


Assuntos
Humanos , Adulto , Obesidade Mórbida/cirurgia , Tolerância ao Exercício , Cirurgia Bariátrica/reabilitação , Terapia por Exercício , Índice de Massa Corporal , Guias como Assunto , Consenso , Treinamento Resistido
4.
Rev Med Chil ; 147(11): 1468-1486, 2019 Nov.
Artigo em Espanhol | MEDLINE | ID: mdl-32186608

RESUMO

Physical exercise is useful in people who underwent bariatric surgery. However, the right dosage is still a topic for discussion. The aim of this article is to consolidate the prescription criteria for physical activity and exercise in bariatric patients. A panel of experts to whom the topics were previously assigned for review, met to reach a consensus. Each topic was presented and subjected to discussion and voting by the participants and attendants who were exercise professionals from different obesity treatment centers. We report the conclusions reached for aerobic exercise, strength training, protein supplementation and physical activity for weight maintenance in bariatric patients.


Assuntos
Cirurgia Bariátrica/reabilitação , Terapia por Exercício , Tolerância ao Exercício , Obesidade Mórbida/cirurgia , Adulto , Índice de Massa Corporal , Consenso , Guias como Assunto , Humanos , Treinamento Resistido
5.
Rev Argent Microbiol ; 35(2): 80-5, 2003.
Artigo em Espanhol | MEDLINE | ID: mdl-12920988

RESUMO

Fenton systems (H2O2/Fe(II) or H2O2/Cu(II)) inhibited Trypanosoma cruzi and Crithidia fasciculata topoisomerase I activity. About 61-71% inactivation was produced by 25 mM Fe(II) or Cu(II) with 3 mM H2O2. Thiol compounds and free radicals scavengers prevented the Fenton systems effects, depending on the topoisomerase assayed. With the T. cruzi enzyme, reduced glutathione, DL-dithiothreitol, cysteine and N-acetyl-L-cysteine entirely prevented the effect of the H2O2/Fe(II) system, mannitol protected 37%, whereas histidine and ethanol were ineffective. With C. fasciculata topoisomerase, reduced glutathione, DL-dithiothreitol and N-acetyl-L-cysteine protected 100%, cysteine, histidine and mannitol protected 28, 34 and 48% respectively, whereas ethanol was ineffective. With the H2O2/Cu(II) system and T. cruzi topoisomerase, DL-dithiothreitol and histidine protected 100% and 60%, respectively but the other assayed protectors were less effective. Similar results were obtained with the C. fasciculata enzyme. Topoisomerase inactivation by H2O2/Fe(II) or H2O2/Cu(II) systems was irreversible since they were not reverted by the more effective enzyme protectors. It is suggested that topoisomerases could act either as scavengers of "reactive oxygen species" (ROS) generated by Fenton systems or bind the corresponding metal ions, whose redox cycling would generate reactive oxygen species "in situ".


Assuntos
Crithidia fasciculata/enzimologia , Inibidores Enzimáticos/farmacologia , Peróxido de Hidrogênio/farmacologia , Ferro/farmacologia , Proteínas de Protozoários/antagonistas & inibidores , Inibidores da Topoisomerase I , Trypanosoma cruzi/enzimologia , Animais , Quelantes/farmacologia , Crithidia fasciculata/efeitos dos fármacos , Peróxido de Hidrogênio/antagonistas & inibidores , Ferro/antagonistas & inibidores , Oxirredução , Espécies Reativas de Oxigênio/metabolismo , Especificidade da Espécie , Reagentes de Sulfidrila/farmacologia , Trypanosoma cruzi/efeitos dos fármacos
6.
Rev. argent. microbiol ; 35(2): 80-85, abr.-jun. 2003.
Artigo em Espanhol | LILACS | ID: lil-356634

RESUMO

Los sistemas Fenton (H2O2/Fe o H2O2/Cu) fueron capaces de inhibir la actividad topoisomerasa I de extractos crudos de Trypanosoma cruzi y Crithidia fasciculata. El agregado de compuestos de tioles o complejantes de metales, modificó la inhibición y dicho efecto dependió del metal y del origen de la enzima. El glutation reducido, DL-ditiotreitol, y N-aceti-L-cisteína 1 mM fueron efectivos protectores frente a la inhibición, inducida por el sistema H2O2/Fe, de la actividad presente en T.cruzi, el manitol protegió 37 por ciento, mientras que la histidina y etanol fueron inefectivos. Con la topoisomerasa de C.fasciculata, glutatión reducido, DL-ditiotreitol y N-acetil L-cisteína protegieron 100 por ciento a la enzima de la acción deletérea del sistema Fenton (Fe), los compuestos manitol, histidina y cisteína 1 mM protegieron 48, 34 y 28 por ciento, respectivamente, mientras que el etanol 4 mM fue inefectivo. Con el sistema H2O2/Cu y la enzima de T.cruzi, el DL-ditiotreitol y la histidina 1mM protegieron 100 y 60 por ciento, respectivamente, los otros protectores ensayados fueron menos efectivos. Resultados semejantes se obtuvieron con la topoisomerasa de C.fasciculata. La disminución por sistemas Fenton de la actividad topoisomerasa I de los extractos resultó no ser revertida por posterior incubación con los compuestos que tuvieron efecto protector. Se sugiere que la estructura molecular de la proteína podría actuar como secuestrante de radicales libres generados por los sismtemas Fenton o mediante la unión de metales como el Cu o Fe, facilitando la generación de los mismos in situ. Ambos mecanismos conducirían a la inactivación de la misma.


Assuntos
Crithidia fasciculata , DNA Topoisomerases Tipo I , Trypanosoma cruzi , Argentina
7.
Rev. argent. microbiol ; 35(2): 80-85, abr.-jun. 2003.
Artigo em Espanhol | BINACIS | ID: bin-4853

RESUMO

Los sistemas Fenton (H2O2/Fe o H2O2/Cu) fueron capaces de inhibir la actividad topoisomerasa I de extractos crudos de Trypanosoma cruzi y Crithidia fasciculata. El agregado de compuestos de tioles o complejantes de metales, modificó la inhibición y dicho efecto dependió del metal y del origen de la enzima. El glutation reducido, DL-ditiotreitol, y N-aceti-L-cisteína 1 mM fueron efectivos protectores frente a la inhibición, inducida por el sistema H2O2/Fe, de la actividad presente en T.cruzi, el manitol protegió 37 por ciento, mientras que la histidina y etanol fueron inefectivos. Con la topoisomerasa de C.fasciculata, glutatión reducido, DL-ditiotreitol y N-acetil L-cisteína protegieron 100 por ciento a la enzima de la acción deletérea del sistema Fenton (Fe), los compuestos manitol, histidina y cisteína 1 mM protegieron 48, 34 y 28 por ciento, respectivamente, mientras que el etanol 4 mM fue inefectivo. Con el sistema H2O2/Cu y la enzima de T.cruzi, el DL-ditiotreitol y la histidina 1mM protegieron 100 y 60 por ciento, respectivamente, los otros protectores ensayados fueron menos efectivos. Resultados semejantes se obtuvieron con la topoisomerasa de C.fasciculata. La disminución por sistemas Fenton de la actividad topoisomerasa I de los extractos resultó no ser revertida por posterior incubación con los compuestos que tuvieron efecto protector. Se sugiere que la estructura molecular de la proteína podría actuar como secuestrante de radicales libres generados por los sismtemas Fenton o mediante la unión de metales como el Cu o Fe, facilitando la generación de los mismos in situ. Ambos mecanismos conducirían a la inactivación de la misma. (AU)


Assuntos
Trypanosoma cruzi , Crithidia fasciculata , Argentina
8.
Rev. argent. microbiol ; 35(2): 80-5, 2003 Apr-Jun.
Artigo em Espanhol | BINACIS | ID: bin-38909

RESUMO

Fenton systems (H2O2/Fe(II) or H2O2/Cu(II)) inhibited Trypanosoma cruzi and Crithidia fasciculata topoisomerase I activity. About 61-71


inactivation was produced by 25 mM Fe(II) or Cu(II) with 3 mM H2O2. Thiol compounds and free radicals scavengers prevented the Fenton systems effects, depending on the topoisomerase assayed. With the T. cruzi enzyme, reduced glutathione, DL-dithiothreitol, cysteine and N-acetyl-L-cysteine entirely prevented the effect of the H2O2/Fe(II) system, mannitol protected 37


, whereas histidine and ethanol were ineffective. With C. fasciculata topoisomerase, reduced glutathione, DL-dithiothreitol and N-acetyl-L-cysteine protected 100


, cysteine, histidine and mannitol protected 28, 34 and 48


respectively, whereas ethanol was ineffective. With the H2O2/Cu(II) system and T. cruzi topoisomerase, DL-dithiothreitol and histidine protected 100


and 60


, respectively but the other assayed protectors were less effective. Similar results were obtained with the C. fasciculata enzyme. Topoisomerase inactivation by H2O2/Fe(II) or H2O2/Cu(II) systems was irreversible since they were not reverted by the more effective enzyme protectors. It is suggested that topoisomerases could act either as scavengers of [quot ]reactive oxygen species[quot ] (ROS) generated by Fenton systems or bind the corresponding metal ions, whose redox cycling would generate reactive oxygen species [quot ]in situ[quot ].

9.
Mol Biochem Parasitol ; 115(2): 249-56, 2001 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-11420111

RESUMO

Crithidia fasciculata poly(ADP-ribose)polymerase (PARP) has been isolated and partially purified. This is the first PARP isolated from trypanosomatids; it requires DNA and histone for activity, using NAD(+) as substrate. Thiol compounds specially dithiothreitol essentially contributed to PARP stability during purification and to PARP activity during assays. Nicotinamide, 3-aminobenzamide, theophylline, histamine, histidine, N-ethylmaleimide, p-chloromercuribenzoic acid, p-chloromercuriphenylsulfonic acid and o-iodosobenzoate inhibited PARP, thus confirming enzyme identity. PARP was also inhibited by the Fe(II)/H(2)O(2) Fenton system. beta-Lapachone inhibited PARP, apparently by direct interaction with the enzyme.


Assuntos
Antiprotozoários/farmacologia , Crithidia fasciculata/enzimologia , Naftoquinonas/farmacologia , Poli(ADP-Ribose) Polimerases/isolamento & purificação , Poli(ADP-Ribose) Polimerases/metabolismo , Animais , Eletroforese em Gel de Poliacrilamida , Peróxido de Hidrogênio/farmacologia , Ferro/farmacologia , Inibidores de Poli(ADP-Ribose) Polimerases
10.
Eur Biophys J ; 23(1): 51-8, 1994.
Artigo em Inglês | MEDLINE | ID: mdl-8206006

RESUMO

We have studied the mechanism of Ca current inactivation in the beta-cell line HIT-T15 by conventional and perforated patch recording techniques, using two pulse voltage protocols and a combination of current and tail current measurements. In 5 mM Ca, from a holding potential of -80 mV, the maximum current showed a complex time course of inactivation: a relatively fast, double exponential inactivation (tau h1 approximately 12 ms and tau h2 approximately 60 ms) and a very slowly inactivating component (tau > 1 s). The faster component (tau h1) was due to the voltage-dependent inactivation of a low-threshold-activated (LVA), T-type current, which deactivates more slowly (tau approximately 3-5 ms) than the other components (tau approximately 0.2-0.3 ms). The intermediate component (tau h2) was due to the Ca-dependent inactivation of a portion of the high-threshold-activated (HVA) current. A saturating dose of the dihydropyridine (DHP) nifedipine (10 microM) did not affect the LVA current, but inhibited by 68 +/- 5% the transient, Ca-sensitive portion of the HVA current and by 33 +/- 12% the long lasting component. We suggest that three components of the calcium current can be resolved in HIT cells and the main target of DHPs is a HVA current, which inactivates faster than the DHP-resistant HVA component and does so primarily through calcium influx.


Assuntos
Bloqueadores dos Canais de Cálcio/farmacologia , Canais de Cálcio/efeitos dos fármacos , Insulinoma/metabolismo , Neoplasias Pancreáticas/metabolismo , Animais , Canais de Cálcio/metabolismo , Cloreto de Cálcio/farmacologia , Cricetinae , Meios de Cultura , Eletrofisiologia , Mesocricetus , Nifedipino/farmacologia , Nistatina/farmacologia , Sódio/fisiologia , Células Tumorais Cultivadas
11.
In. Congresso Internacional de Leprologia, 8. Congresso Internacional de Leprologia, 8/Anais. Rio de Janeiro, Serviço Nacional de Lepra, 1963. p.321-3.
Não convencional em Espanhol | LILACS-Express | Sec. Est. Saúde SP, HANSEN, Hanseníase, SESSP-ILSLACERVO, Sec. Est. Saúde SP | ID: biblio-1244445
12.
In. Congresso Internacional de Leprologia, 8. Congresso Internacional de Leprologia, 8/Anais. Rio de Janeiro, Serviço Nacional de Lepra, 1963. p.324-5.
Não convencional em Espanhol | LILACS-Express | Sec. Est. Saúde SP, HANSEN, Hanseníase, SESSP-ILSLACERVO, Sec. Est. Saúde SP | ID: biblio-1244446
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