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1.
Artigo em Inglês | MEDLINE | ID: mdl-26464877

RESUMO

The goal of this investigation was to determine if playing or training on third-generation artificial turf (AT) surfaces increases the incidence rate of injuries compared to natural grass (NG) surfaces. This was accomplished by a meta-analysis performed on previously published research. Eight studies met the criteria of competitive soccer players, participation on both surfaces, and presentation of both exposure time and injury occurrence. Exposure time and injury incidence values were used to generate injury rate ratios (IRRs, AT/NG) for all injuries as well as specific injuries. Subgroup analyses were also performed by condition (match or training), gender, and age (youth or adult). The overall IRR was 0.86 (P < 0.05) suggesting a lower injury risk on AT than NG. However, there was considerable heterogeneity between studies. Analyses of individual injuries and subgroups found that in many cases IRR values were significantly less than 1.0. In no case was the IRR significantly greater than 1.0. Based on this, it appears that the risk of sustaining an injury on AT under some conditions might be lowered compared to NG. However, until more is known about how issues such as altered playing styles affect injury incidence, it is difficult to make firm conclusions regarding the influence of AT on player safety.

2.
Anal Biochem ; 372(2): 135-9, 2008 Jan 15.
Artigo em Inglês | MEDLINE | ID: mdl-17967437

RESUMO

The goal of this investigation was to develop an assay whereby we could measure changes in ATP, ADP, and phosphocreatine (PCr) during stimulation of the sarcoplasmic reticulum (SR) Ca2+ ATPase. After stopping the enzyme reaction, compounds were extracted by perchloric acid and separated by reversed-phase high-performance liquid chromatography (HPLC). Absorbance of ATP and ADP was monitored at 260 nm, and detection of PCr was done at 205 nm. Chromatograms show that peaks associated with each compound are clearly separated and easily detected. The SR Ca2+ ATPase assay was run for various time periods and using varying free [Ca2+]. The changes in ATP and ADP contents were linear with increasing time and varied as expected with increasing free [Ca2+]. The ATPase activities determined using changes in ATP and ADP were nearly identical to those determined using previously established assays. When PCr was added to the assay, we were able to confirm that the Ca2+ ATPase uses ATP that is synthesized locally from PCr via creatine kinase (CK). The results indicate that this is a valid and reliable method for examining SR Ca2+ ATPase activity and for investigating its interaction with CK.


Assuntos
ATPases Transportadoras de Cálcio/metabolismo , Músculo Esquelético/enzimologia , Retículo Sarcoplasmático/enzimologia , Difosfato de Adenosina/metabolismo , Trifosfato de Adenosina/metabolismo , Animais , Cromatografia Líquida de Alta Pressão/métodos , Cinética , Fosfocreatina/metabolismo , Ratos
3.
BMC Cancer ; 7: 146, 2007 Aug 02.
Artigo em Inglês | MEDLINE | ID: mdl-17678552

RESUMO

BACKGROUND: Late stage cancer malignancies may result in severe skeletal muscle wasting, fatigue and reduced quality of life. Resistance training may attenuate these derangements in cancer patients, but how this hypertrophic response relates to normal muscle adaptations in healthy subjects is unknown. Here, we determined the effect of resistance training on muscle mass and myosin heavy chain (MHC) isoform composition in plantaris muscles from tumor-bearing (TB) rats. METHODS: Age- and gender-matched Buffalo rats were used for all studies (n = 6/group). Suspensions of Morris Hepatoma MH7777 cells or normal saline were injected subcutaneously into the dorsum. Six weeks after cell implantation, muscles from TB rats were harvested, weighed and processed for ATP-independent proteasome activity assays. Once tumor-induced atrophy had been established, subgroups of TB rats underwent unilateral, functional overload (FO). Healthy, sham-operated rats served as controls. After six weeks, the extent of plantaris hypertrophy was calculated and MHC isoform compositions were determined by gel electrophoresis. RESULTS: Six weeks of tumor growth reduced body mass and the relative masses of gastrocnemius, plantaris, tibialis anterior, extensor digitorum longus, and diaphragm muscles (p < or = 0.05). Percent reductions in body mass had a strong, negative correlation to final tumor size (r = -0.78). ATP-independent proteasome activity was increased in plantaris muscles from TB rats (p < or = 0.05). In healthy rats, functional overload (FO) increased plantaris mass ~44% compared to the contralateral control muscle, and increased the relative percentage of MHC type I and decreased the relative percentage of MHC type IIb compared to the sham-operated controls (p < or = 0.05). Importantly, plantaris mass was increased ~24% in TB-FO rats and adaptations to MHC isoform composition were consistent with normal, resistance-trained muscles. CONCLUSION: Despite significant skeletal muscle derangements due to cancer, muscle retains the capacity to respond normally to hypertrophic stimuli. Specifically, when challenged with functional overload, plantaris muscles from TB rats displayed greater relative mass, increased percentages of MHC type I and decreased percentages of MHC type IIb. Therefore, resistance training paradigms should provide relative morphological and functional benefits to cancer patients suffering from muscle wasting.


Assuntos
Músculo Esquelético/fisiologia , Atrofia Muscular/prevenção & controle , Atrofia Muscular/fisiopatologia , Ensaios Antitumorais Modelo de Xenoenxerto , Animais , Linhagem Celular Tumoral , Feminino , Técnicas In Vitro , Músculo Esquelético/patologia , Atrofia Muscular/etiologia , Ratos , Ratos Endogâmicos BUF
4.
Am J Physiol Cell Physiol ; 286(1): C97-104, 2004 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-12967914

RESUMO

The purpose of this investigation was to determine whether there is a link between sarcoplasmic reticulum (SR) glycogen status and SR Ca2+ handling. In this investigation, skeletal muscle SR was purified from female Sprague-Dawley rats (200-250 g). Glycogen was extracted from the SR purified from one hindlimb, whereas the SR purified from the contralateral limb served as control. Before removal of the tissue, the animals were anesthetized with an intraperitoneal injection of ketamine (80 mg/kg) and xylazine (10 mg/kg). Both alpha-amylase treatment (AM) and removal of EDTA from the homogenization and storage buffers reduced the amount of glycogen associated with the SR (P < 0.05). AM treatment reduced the glycogen phosphorylase content of SR (P < 0.05). In contrast, creatine kinase (CK) and pyruvate kinase (PK) contents were increased after both glycogen extraction protocols (P < 0.05). Under exogenous ATP conditions, both AM and EDTA-free (EF) treatments resulted in an increase in Ca2+-stimulated ATPase activity when normalized to sarco(endo)plasmic reticulum calcium-ATPase (SERCA) content (P < 0.05). CK and PK-supported SR Ca2+ uptake was decreased (P < 0.05) in the AM group when normalized to SERCA and CK or SERCA and PK content, respectively. AM was more effective than the EF for extracting glycogen associated with purified SR. Glycogen extraction alters the yield of purified SR proteins and must be taken into account when investigating SR calcium handling. Removal of glycogen from purified SR causes a change in Ca2+-handling properties as measured by ATPase and uptake activities.


Assuntos
Trifosfato de Adenosina/fisiologia , Cálcio/metabolismo , Glicogênio/metabolismo , Músculo Esquelético/metabolismo , Retículo Sarcoplasmático/metabolismo , Trifosfato de Adenosina/farmacologia , Animais , ATPases Transportadoras de Cálcio/metabolismo , Creatina Quinase/metabolismo , Feminino , Fluoresceína-5-Isotiocianato , Corantes Fluorescentes , Glicogênio/análise , Glicogênio Fosforilase/metabolismo , Proteínas Musculares/metabolismo , Músculo Esquelético/química , Piruvato Quinase/metabolismo , Ratos , Ratos Sprague-Dawley , Retículo Sarcoplasmático/química
5.
Eur J Appl Physiol ; 89(1): 63-8, 2003 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-12627306

RESUMO

The effects of a single bout of prolonged treadmill exercise [mean=81 (13) min] on sarcoplasmic reticulum (SR) Ca(2+) release, uptake and ATPase activity were determined in the costal region of rat diaphragm (D) and red gastrocnemius (RG). Glycogen depletion measurements made immediately following exercise suggested that treadmill running substantially recruited the fibers throughout both muscles. SR Ca(2+) ATPase activity, measured in isolated SR vesicles, decreased in the RG by 33% but remained unchanged in D in response to the exercise bout. This effect in RG was matched by a 37% decline in Ca(2+) uptake and a 28% depression in Ca(2+) release when measured in muscle homogenates. Conversely, Ca(2+) uptake increased between 157% and 263% in the D in the absence of any change in Ca(2+) release. These data show that the attenuation of SR function that has been consistently observed in limb muscle over the last several decades is absent in diaphragm despite the fact that its fibers appear to experience sufficient activity to deplete their glycogen. In fact, the large increase in Ca(2+) uptake in D shows that prolonged activity actually potentiates the ability of SR vesicles to sequester Ca(2+) in the absence of any increase in energy cost. Thus, it appears necessary to re-evaluate the role of exercise in regulating Ca(2+) sequestration by the SR as different muscles may respond in ways that are dictated by their function.


Assuntos
Articulação do Tornozelo/fisiologia , Cálcio/metabolismo , Diafragma/fisiologia , Fadiga Muscular/fisiologia , Condicionamento Físico Animal/fisiologia , Músculos Respiratórios/fisiologia , Retículo Sarcoplasmático/fisiologia , Adenosina Trifosfatases/metabolismo , Animais , Articulação do Tornozelo/metabolismo , Diafragma/metabolismo , Feminino , Glicogênio/metabolismo , Resistência Física/fisiologia , Esforço Físico , Ratos , Ratos Sprague-Dawley , Músculos Respiratórios/metabolismo , Retículo Sarcoplasmático/metabolismo
6.
Eur J Appl Physiol ; 87(2): 182-6, 2002 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-12070630

RESUMO

Recent investigations have suggested that changes in contractile protein expression contribute to reductions in skeletal muscle function during congestive heart failure (CHF). Myosin heavy chain (MHC), a major contractile protein, has been shown to undergo alterations in protein isoform expression during CHF. The purpose of this investigation was twofold: (1) to determine whether muscles of the same functional group undergo similar changes in MHC expression, and (2) determine whether the magnitude of alterations in MHC is related to the severity of CHF. Using the rat coronary ligation model, mild and severe forms of CHF were produced and muscles of the plantar flexor group were analyzed. Whole-muscle MHC isoform proportions were not altered in the soleus and white gastrocnemius muscle, however significant increases in the percentage of fast MHC isoforms (7-9% increases in MHC IIx and IIb expression) were found in the red gastrocnemius muscle. In addition, there were significant proportional increases (8%) in MHC type IIb at the expense of MHC type IIx in the plantaris muscle. Many of the changes in the proportions of MHC isoforms were significantly correlated with indices of CHF severity. This indicates that changes in skeletal muscle MHC isoform expression are related to the severity of CHF and suggests that some peripheral skeletal muscles are more susceptible to shifts in MHC expression due to CHF. These changes in MHC isoform expression may contribute to alterations in the physiological performance of skeletal muscle and exercise capacity during CHF.


Assuntos
Insuficiência Cardíaca/fisiopatologia , Fibras Musculares de Contração Rápida/química , Fibras Musculares de Contração Lenta/química , Músculo Esquelético/química , Cadeias Pesadas de Miosina/análise , Animais , Tornozelo/fisiopatologia , Insuficiência Cardíaca/etiologia , Músculo Esquelético/fisiopatologia , Infarto do Miocárdio/complicações , Isoformas de Proteínas , Ratos , Valores de Referência , Reprodutibilidade dos Testes , Sensibilidade e Especificidade , Índice de Gravidade de Doença
7.
J Appl Physiol (1985) ; 92(1): 18-24, 2002 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-11744638

RESUMO

It is thought that changes in sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA) of skeletal muscle contribute to alterations in skeletal muscle function during congestive heart failure (CHF). It is well established that exercise training can improve muscle function. However, it is unclear whether similar adaptations will result from exercise training in a CHF patient. Therefore, the purpose of this study was to determine whether skeletal muscle during moderate CHF adapts to increased activity, utilizing the functional overload (FO) model. Significant increases in plantaris mass of the CHF-FO and sham-FO groups compared with the CHF and control (sham) groups were observed. Ca(2+) uptake rates were significantly elevated in the CHF group compared with all other groups. No differences were detected in Ca(2+) uptake rates between the CHF-FO, sham, and sham-FO groups. Increases in Ca(2+) uptake rates in moderate-CHF rats were not due to changes in SERCA isoform proportions; however, FO may have attenuated the CHF-induced increases through alterations in SERCA isoform expression. Therefore, changes in skeletal muscle Ca(2+) handling during moderate CHF may be due to alterations in regulatory mechanisms, which exercise may override, by possibly altering SERCA isoform expression.


Assuntos
Insuficiência Cardíaca/fisiopatologia , Músculo Esquelético/fisiologia , Animais , Western Blotting , Cálcio/metabolismo , ATPases Transportadoras de Cálcio/biossíntese , Feminino , Insuficiência Cardíaca/metabolismo , Ventrículos do Coração/patologia , Músculo Esquelético/metabolismo , Infarto do Miocárdio/patologia , Infarto do Miocárdio/fisiopatologia , Miocárdio/patologia , Tamanho do Órgão/fisiologia , Ratos , Ratos Sprague-Dawley , Retículo Sarcoplasmático/metabolismo , Retículo Sarcoplasmático/fisiologia , ATPases Transportadoras de Cálcio do Retículo Sarcoplasmático
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