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1.
Medicina (Kaunas) ; 57(8)2021 Aug 20.
Artigo em Inglês | MEDLINE | ID: mdl-34441051

RESUMO

Background and Objectives: Although the plank exercise is difficult to perform for untrained people, it does not require money, special equipment, or much space. However, it is not known how plank exercises affect physical fitness and immunocyte function. This study analyzed the changes in physical fitness and immune cells of a middle-aged man after performing 4 weeks of elbow plank exercise. Materials and Methods: Elbow plank exercise was performed for approximately 20 min (resting time, around 10 min) a day, 5 days a week for 4 weeks. The intensity was checked daily with ratings of perceived exertion (RPE). When the participant reached an intensity of RPE 15, RPE 16, and RPE 17 of the RPE 20 scale, 1 min of rest was given before repeating the process. Results: Compared with the pre-values, (1) all the physical fitness factors (muscle strength, muscle endurance, flexibility, and cardiopulmonary fitness) were increased after 4 weeks; (2) body weight, skeletal muscle mass, and the basal metabolic rate were increased, whereas body fat mass and fat percentage were decreased; and (3) although the variables of complete blood count were changed positively, some were not. Specifically, CD3, CD8, and CD56 were increased, whereas CD4, CD4/CD8, and cytotoxicity were decreased. These results show that elbow plank exercise can improve all factors of physical fitness and improve some of the immunocyte functions of a middle-aged man. Conclusions: This study confirmed that, although the elbow plank exercise of vigorous intensity for 4 weeks improved physical fitness, it was not effective in improving some immunocyte functions. Therefore, the exercise intensity of plank exercises for improving immunocyte functions should be reconsidered.


Assuntos
Exercício Físico , Aptidão Física , Terapia por Exercício , Humanos , Masculino , Pessoa de Meia-Idade , Força Muscular , Músculo Esquelético
2.
Prostate Int ; 10(3): 148-151, 2022 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-36225288

RESUMO

Background and objective: We aimed to evaluate the safety and efficacy of robot-assisted simple prostatectomy (RASP) after prostatic arterial embolization (PAE) in large benign prostatic hyperplasia (BPH). Material and methods: This retrospective study included 11 cases of PAE and subsequent RASP, performed on 11 patients with BPH from March 2018 to September 2020. Clinical information on the patients was collected before surgery and 3 months after surgery. For the quantification of lower urinary tract symptoms (LUTS), International Prostate Symptom Scores (IPSSs), prostate-specific antigen (PSA) levels, urinary peak flow rate (Qmax), voided volume (Vvol), and postvoid residual volume (PVR) were measured. Results: PAE and the subsequent RASP were successfully performed in all 11 patients. The mean total prostate volume was 129.7 ± 65.1 mL, and the transitional zone volume was 71.7 ± 5.9 mL. The mean resected prostate volume was 60.8 ± 26.1 mL. The mean hemoglobin level of the patients prior to PAE was 14.2 ± 2.3 g/dL, and one day after RASP, the hemoglobin level was 12.4 ± 1.9 g/dL. The outcome indicated that there was a considerable decline in IPSS and PVR after RASP was performed compared to before PAE (21.6 ± 9.4 vs. 10.6 ± 8.0 and 159.4 ± 145.8 mL vs. 43.9 ± 45.9 mL). Qmax and Vvol significantly improved after RASP was performed (7.6 ± 5.2 mL/s vs. 26.1 ± 12.6 mL/s; 114.2 ± 92.5 mL vs. 192.4 ± 91.8 mL, respectively). Conclusion: This research demonstrated that RASP could be performed safely and effectively after PAE in patients with large BPH.

3.
Diagnostics (Basel) ; 13(1)2022 Dec 28.
Artigo em Inglês | MEDLINE | ID: mdl-36611376

RESUMO

Although many studies on bladder cancer and the microbiome have been conducted so far, useful strains at the species level have not yet been identified. In addition, in the case of urine studies, methodological heterogeneity is too great, and in tissue studies, the species level through shotgun analysis has not been revealed, and studies using stool samples have provided only limited information. In this review, we will review all the microbiome studies related to bladder cancer so far through a systematic review.

4.
Medicine (Baltimore) ; 101(43): e31295, 2022 Oct 28.
Artigo em Inglês | MEDLINE | ID: mdl-36316868

RESUMO

PURPOSE: To evaluate the pathophysiology of nocturia based on the frequency volume chart, and determine the risk factors for nocturia occurring ≥2 times per night. MATERIALS AND METHODS: In this retrospective study, we reviewed 311 patients with complaints of nocturia from January 2017 to February 2019 at our institution. Nocturnal polyuria (NP) and global polyuria (GP) were defined as NP index >0.35 regardless of age and 24 h urine volume >2.5 L/day, respectively. Decreased bladder capacity (dBC) was when the maximal voided volume was <325 mL. Decreased nocturnal bladder capacity (dNBC) was defined as nocturnal bladder capacity index >0. RESULTS: In total, 273 patients were included in the primary analyses. Of 802 days from 273 frequency volume charts, the median number of nocturia was 1 episode per day. Further, NP (odds ratios [OR] 7.01), GP (OR 4.25), dBC (OR 3.00), dNBC (OR 10.12), and age (OR 1.04) had the association with nocturia ≥2 times per night. There was a significant stepwise increase in NP, dNBC, dBC, and GP with the number of nocturia episodes. As patient age increased, the likelihood of NP (P < 0.001) and dBC (P < 0.001) being the cause for nocturia tended to increase, but that of dNBC (P = 0.022) and nocturia without cause (P = 0.007) tended to decrease. Moreover, dBC was more likely to cause nocturia in female patients than in male patients (P < 0.001). CONCLUSION: NP, dBC, dNBC, and GP are important factors involved in the pathophysiology of nocturia occurring ≥2 times per night.


Assuntos
Noctúria , Humanos , Masculino , Feminino , Adulto Jovem , Adulto , Noctúria/epidemiologia , Noctúria/etiologia , Poliúria/epidemiologia , Poliúria/complicações , Estudos Retrospectivos , Micção , Razão de Chances , Estudos Observacionais como Assunto
5.
J Am Chem Soc ; 133(9): 3139-43, 2011 Mar 09.
Artigo em Inglês | MEDLINE | ID: mdl-21291261

RESUMO

In this paper we report the study of a high capacity Sn-C nanostructured anode and of a high rate, high voltage Li[Ni(0.45)Co(0.1)Mn(1.45)]O(4) spinel cathode. We have combined these anode and cathode materials in an advanced lithium ion battery that, by exploiting this new chemistry, offers excellent performances in terms of cycling life, i.e., ca. 100 high rate cycles, of rate capability, operating at 5C and still keeping more than 85% of the initial capacity, and of energy density, expected to be of the order of 170 Wh kg(-1). These unique features make the battery a very promising energy storage for powering low or zero emission HEV or EV vehicles.

6.
J Cell Physiol ; 222(2): 313-9, 2010 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-19847807

RESUMO

Hibernators like bats show only marginal muscle atrophy during prolonged hibernation. The current study was designed to test the hypothesis that hibernators use periodic arousal to increase protein anabolism that compensates for the continuous muscle proteolysis during disuse. To test this hypothesis, we investigated the effects of 3-month hibernation (HB) and 7-day post-arousal torpor (TP) followed by re-arousal (RA) on signaling activities in the pectoral muscles of summer-active (SA) and dormant Murina leucogaster bats. The bats did not lose muscle mass relative to body mass during the HB or TP-to-RA period. For the first 30-min following arousal, the peak amplitude and frequency of electromyographic spikes increased 3.1- and 1.4-fold, respectively, indicating massive myofiber recruitment and elevated motor signaling during shivering. Immunoblot analyses of whole-tissue lysates revealed several principal outcomes: (1) for the 3-month HB, the phosphorylation levels of Akt1 (p-Akt1) and p-mTOR decreased significantly compared to SA bats, but p-FoxO1 levels remained unaltered; (2) for the TP-to-RA period, p-Akt1 and p-FoxO1 varied little, while p-mTOR showed biphasic oscillation; (3) proteolytic signals (i.e., atrogin-1, MuRF1, Skp2 and calpain-1) remained constant during the HB and TP-to-RA period. These results suggest that the resistive properties of torpid bat muscle against atrophy might be attained primarily by relatively constant proteolysis in combination with oscillatory anabolic activity (e.g., p-mTOR) corresponding to the frequency of arousals occurring throughout hibernation.


Assuntos
Nível de Alerta , Quirópteros/metabolismo , Hibernação , Proteínas Musculares/metabolismo , Atrofia Muscular/prevenção & controle , Músculos Peitorais/metabolismo , Periodicidade , Estremecimento , Animais , Western Blotting , Temperatura Corporal , Calpaína/metabolismo , Eletromiografia , Fatores de Transcrição Forkhead/metabolismo , Proteínas I-kappa B/metabolismo , Masculino , Contração Muscular , Atrofia Muscular/metabolismo , Atrofia Muscular/patologia , Tamanho do Órgão , Músculos Peitorais/patologia , Fosforilação , Proteínas Quinases/metabolismo , Proteínas Proto-Oncogênicas c-akt/metabolismo , Estações do Ano , Transdução de Sinais , Serina-Treonina Quinases TOR , Ubiquitina-Proteína Ligases/metabolismo
7.
Cell Physiol Biochem ; 24(5-6): 537-46, 2009.
Artigo em Inglês | MEDLINE | ID: mdl-19910694

RESUMO

At times, exercise accompanied by its anabolic effects is not a tractable countermeasure to muscle atrophy. Instead, training is often attempted after the affected muscle has atrophied greatly as a result of unloading. This study was designed to elucidate stress and signaling mechanisms underlying a process of muscle catch-up growth as a result of transitory exercise during unloading. Rats were exercised daily with a routine of 20- or 40-minute treadmill running (at 60% of maximum oxygen uptake) during the second week of a two-week hindlimb suspension. We examined the expression and activation of heat shock proteins and anabolic and proteolytic markers in the rat soleus muscle. Muscle mass relative to body mass decreased 2.4-fold in the unloaded group (HU) with respect to controls but decreased only 1.7-fold in the 40-min trained group (HT40) (P < 0.05) - equivalent to a 1.4-fold increase in the relative muscle mass over HU. Immunoblotting analyses on whole-tissue lysates demonstrated the following: (1) HSP72 and alphaB-crystallin were upregulated 7- and 2.5-fold, respectively, in HT40 versus HU; (2) phosphorylation of Akt1 and p70/S6K decreased only slightly in HU; (3) when compared to HU, HT40 phosphorylation of Akt1, S6K, and FoxO1 increased 1.4- to 3.0-fold while phosphorylation of FoxO3 was unchanged; and (4) activities of the ubiquitin E3 ligases, calpain 1 and caspase-3 increased 2- to 4-fold in the unloaded groups regardless of exercise duration. These results suggest that the significant upregulation of chaperones and anabolic markers (e.g., HSP72, p-Akt1, p-S6K) in HT40, along with the lack of the training effect on proteolytic activity, is likely crucial for muscle mass catch-up in the unloaded muscle.


Assuntos
Músculo Esquelético/fisiologia , Atrofia Muscular/metabolismo , Condicionamento Físico Animal , Estresse Fisiológico , Animais , Calpaína/metabolismo , Caspase 3/metabolismo , Fatores de Transcrição Forkhead/metabolismo , Proteínas de Choque Térmico/metabolismo , Elevação dos Membros Posteriores , Proteínas do Tecido Nervoso/metabolismo , Fosforilação , Proteínas Proto-Oncogênicas c-akt/metabolismo , Ratos , Ratos Sprague-Dawley , Proteínas Quinases S6 Ribossômicas , Transdução de Sinais , Ubiquitina-Proteína Ligases/metabolismo
8.
J Cell Biochem ; 104(2): 642-56, 2008 May 15.
Artigo em Inglês | MEDLINE | ID: mdl-18181155

RESUMO

Prolonged disuse of skeletal muscle causes significant loss of myofibrillar contents, muscle tension, and locomotory capacity. However, hibernating mammals like bats appear to deviate from this trend. Although low functional demands during winter dormancy has been implicated as a factor contributing to reduced muscle loss, the precise mechanism that actively prevents muscle atrophy remains unclear. We explored proteomic and molecular assessments of bat muscle to test a hypothesis that expression levels of major myofibrillar proteins are retained during hibernation, with periodic arousals utilized as a potential mechanism to prevent disuse atrophy. We examined changes in myofibrillar contents and contractile properties of the pectoral or biceps brachii muscles of the bat Murina leucogaster in summer active (SA), hibernation (HB) and early phase of arousal (AR) states. We found the bat muscles did not show any sign of atrophy or tension reduction over the 3-month winter dormancy. Levels of most sarcomeric and metabolic proteins examined were maintained through hibernation, with some proteins (e.g., actin and voltage dependent anion channel 1) 1.6- to 1.8-fold upregulated in HB and AR compared to SA. Moreover, expression levels of six heat shock proteins (HSPs) including glucose-regulated protein 75 precursor were similar among groups, while the level of HSP70 was even 1.7-fold higher in HB and AR than in SA. Thus, considering the nature of arousal with strenuous muscle shivering and heat stress, upregulation or at least balanced regulation of the chaperones (HSPs) would contribute to retaining muscle properties during prolonged disuse of the bat.


Assuntos
Hibernação , Proteínas dos Microfilamentos/análise , Atrofia Muscular , Proteômica , Animais , Nível de Alerta , Quirópteros , Proteínas de Choque Térmico HSP70 , Proteínas de Choque Térmico , Mamíferos , Tono Muscular , Miofibrilas/química , Estações do Ano , Regulação para Cima
9.
J Biochem ; 139(1): 71-80, 2006 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-16428321

RESUMO

Unloading of skeletal muscle causes atrophy and altered contractility. To identify major muscle proteins responding significantly to the altered loading and to elucidate how the contractile alterations reflect potential proteomic modifications, we examined protein expression in the rat soleus muscle during 3-week hindlimb suspension and 2-week reloading. Compared with unsuspended controls, experimental animals had a 0.5- to 0.6-fold decrease in tension during unloading and early reloading, comparable to 0.2- to 0.6-fold decreases in the protein levels of myosin light chain 1 (MLC1), alpha-actin, tropomyosin beta-chain, and troponins T1 and T2. The observed 1.4- to 1.6-fold increase in shortening velocity appears to reflect 1.2- to 9.0-fold increases in the protein levels of fast-type MLC2, glycolytic enzymes, and creatine kinase, and 0.2- to 0.3-fold decreases in slow-type troponins T1 and T2. The levels of three heat shock proteins (p20, alpha crystallin B chain, and HSP90) decreased during unloading but returned to control levels during reloading. These results imply that proteomic responses to unloading change overall myofibrillar integrity and metabolic regulation, resulting in altered contractility.


Assuntos
Elevação dos Membros Posteriores , Contração Muscular , Músculo Esquelético/metabolismo , Proteômica , Animais , Proteínas Sanguíneas/metabolismo , Proteínas de Choque Térmico/metabolismo , Músculo Esquelético/fisiologia , Atrofia Muscular , Ratos , Ratos Sprague-Dawley
10.
Mol Cells ; 22(3): 275-84, 2006 Dec 31.
Artigo em Inglês | MEDLINE | ID: mdl-17202855

RESUMO

The molecular components that generate and maintain circadian rhythms of physiology and behavior in mammals are present both in the brain (suprachiasmatic nucleus; SCN) and in peripheral tissues. Examination of mice with targeted disruptions of either mPer1 or mPer2 has shown that these two genes have key roles in the SCN circadian clock. Here we show that loss of the clock gene mPer2 affects forced locomotor performance in mice without altering muscle contractility. A proteomic analysis revealed that the anterior tibialis muscles of the mPer2 knockout mice had higher levels of glycolytic enzymes such as triose phosphate isomerase and enolase than those of either the wild type or mPer1 knockout mice. In addition, the level of expression of HSP90 in the mPer2 mutant mice was also significantly higher than in wildtype mice. These results suggest that the reduced locomotor endurance of the mPer2 knockout mice reflects a greater dependence on anaerobic metabolism under stress conditions, and that the two canonical clock genes, mPer1 and mPer2, play distinct roles in the physiology of skeletal muscle.


Assuntos
Relógios Biológicos , Proteínas de Ciclo Celular/genética , Músculo Esquelético/fisiologia , Proteínas Nucleares/genética , Proteômica , Fatores de Transcrição/genética , Animais , Proteínas Sanguíneas/metabolismo , Ritmo Circadiano , Proteínas Contráteis/metabolismo , Eletroforese em Gel Bidimensional , Proteínas de Choque Térmico/metabolismo , Immunoblotting , Camundongos , Camundongos Endogâmicos , Camundongos Knockout , Atividade Motora , Contração Muscular , Proteínas Musculares/metabolismo , Músculo Esquelético/anatomia & histologia , Músculo Esquelético/química , Proteínas Circadianas Period
11.
Yonsei Med J ; 45(4): 690-702, 2004 Aug 31.
Artigo em Inglês | MEDLINE | ID: mdl-15344212

RESUMO

In order to elucidate muscle functional changes by acute reloading, contractile and fatigue properties of the rat soleus muscle were investigated at three weeks of hindlimb suspension and the following 1 hr, 5 hr, 1 d, and 2 weeks of reloading. Compared to age-matched controls, three weeks of unloading caused significant changes in myofibrillar alignments, muscle mass relative to body mass (-43%), normalized tension (-35%), shortening velocity (+143%), and response times. Further significant changes were not observed during early reloading, because the transitional reverse process was gradual rather than abrupt. Although most of the muscle properties returned to the control level after two weeks of reloading, full recovery of the tissue would require more than the two-week period. Delayed recovery due to factors such as myofibrillar arrangement and fatigue resistance was apparent, which should be considered for rehabilitation after a long-term spaceflight or bed-rest.


Assuntos
Contração Muscular/fisiologia , Fadiga Muscular/fisiologia , Músculo Esquelético/fisiologia , Animais , Elevação dos Membros Posteriores , Ácido Láctico/metabolismo , Microscopia Eletrônica , Músculo Esquelético/citologia , Miofibrilas/ultraestrutura , Ratos , Ratos Sprague-Dawley , Suporte de Carga/fisiologia
12.
Korean J Orthod ; 42(4): 169-81, 2012 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-23112948

RESUMO

OBJECTIVE: The purpose of this study was to develop superimposition method on the lower arch using 3-dimensional (3D) cone beam computed tomography (CBCT) images and orthodontic 3D digital modeling. METHODS: Integrated 3D CBCT images were acquired by substituting the dental portion of 3D CBCT images with precise dental images of an orthodontic 3D digital model. Images were acquired before and after treatment. For the superimposition, 2 superimposition methods were designed. Surface superimposition was based on the basal bone structure of the mandible by surface-to-surface matching (best-fit method). Plane superimposition was based on anatomical structures (mental and lingual foramen). For the evaluation, 10 landmarks including teeth and anatomic structures were assigned, and 30 times of superimpositions and measurements were performed to determine the more reproducible and reliable method. RESULTS: All landmarks demonstrated that the surface superimposition method produced relatively more consistent coordinate values. The mean distances of measured landmarks values from the means were statistically significantly lower with the surface superimpositions method. CONCLUSIONS: Between the 2 superimposition methods designed for the evaluation of 3D changes in the lower arch, surface superimposition was the simpler, more reproducible, reliable method.

13.
Korean J Orthod ; 42(1): 1-2, 2012 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-23112923
14.
J Cell Biochem ; 96(6): 1231-43, 2005 Dec 15.
Artigo em Inglês | MEDLINE | ID: mdl-16149053

RESUMO

Skeletal muscle undergoes a significant reduction in tension upon unloading. To explore intracellular signalling mechanisms underlying this phenomenon, we investigated twitch tension, the ratio of actin/myosin filaments, and activities of key signalling molecules in rat soleus muscle during a 3-week hindlimb suspension and 2-week reloading. Twitch tension and myofilament ratio (actin/myosin) gradually decreased during unloading but progressively recovered to initial levels during reloading. To study the involvement of stress-responsive signalling proteins during these changes, the activities of protein kinase C alpha (PKCalpha) and three mitogen-activated protein kinases (MAPKs)--c-Jun NH2-terminal kinase (JNK), extracellular signal-regulated protein kinase (ERK), and p38 MAPK--were examined using immunoblotting and immune complex kinase assays. PKCalpha phosphorylation correlated positively with the tension (Pearson's r = 0.97, P < 0.001) and the myofilament ratio (r = 0.83, P < 0.01) over the entire unloading and reloading period. Treatment of the soleus muscle with a PKC activator resulted in a similar paralleled increment in both PKCalpha phosphorylation and the alpha-sarcomeric actin expression. The three MAPKs differed in the pattern of activation in that JNK activity peaked only for the first hours of reloading, whereas ERK and p38 MAPK activities remained elevated during reloading. These results suggest that PKCalpha may play a pivotal role in converting loading stress to intracellular changes in contractile proteins that determine muscle tension. Differential activation of MAPKs may also help alleviate muscle damage, modulate energy transport and/or regulate the expression of contractile proteins upon altered loading.


Assuntos
Proteínas de Choque Térmico/metabolismo , Músculo Esquelético/metabolismo , Transdução de Sinais/fisiologia , Actinas/metabolismo , Animais , Peso Corporal/fisiologia , MAP Quinases Reguladas por Sinal Extracelular/metabolismo , Proteínas Quinases JNK Ativadas por Mitógeno/metabolismo , Microscopia Eletrônica , Proteínas Quinases Ativadas por Mitógeno/metabolismo , Contração Muscular/fisiologia , Músculo Esquelético/citologia , Miofibrilas/metabolismo , Miosinas/metabolismo , Fosforilação , Isoformas de Proteínas/metabolismo , Proteína Quinase C/metabolismo , Ratos , Ratos Sprague-Dawley , Proteínas Quinases p38 Ativadas por Mitógeno/metabolismo
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