Base de dados : MEDLINE
Pesquisa : D05.750.078.730.475.475.750 [Categoria DeCS]
Referências encontradas : 93 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 10 ir para página                        

  1 / 93 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27736981
[Au] Autor:Kammoun M; Pouletaut P; Canon F; Subramaniam M; Hawse JR; Vayssade M; Bensamoun SF
[Ad] Endereço:Biomechanics and Bioengineering Laboratory, UMR CNRS 7338, Sorbonne University, Université de Technologie de Compiègne, Compiègne, France.
[Ti] Título:Impact of TIEG1 Deletion on the Passive Mechanical Properties of Fast and Slow Twitch Skeletal Muscles in Female Mice.
[So] Source:PLoS One;11(10):e0164566, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:As transforming growth factor (TGF)-ß inducible early gene-1 is highly expressed in skeletal muscle, the effect of TIEG1 gene deletion on the passive mechanical properties of slow and fast twitch muscle fibers was analyzed. Twenty five muscle fibers were harvested from soleus (Sol) and extensor digitorum longus (EDL) muscles from TIEG1-/- (N = 5) and control (N = 5) mice. Mechanical tests were performed on fibers and the dynamic and static stresses were measured. A viscoelastic Hill model of 3rd order was used to fit the experimental relaxation test data. In parallel, immunohistochemical analyses were performed on three serial transverse sections to detect the myosin isoforms within the slow and fast muscles. The percentage and the mean cross sectional area of each fiber type were calculated. These tests revealed a significant increase in the mechanical stress properties for the TIEG1-/- Sol fibers while a significant decrease appeared for the TIEG1-/- EDL fibers. Hill model tracked the shape of the experimental relaxation curve for both genotypes and both fiber types. Immunohistochemical results showed hypertrophy of all fiber types for TIEG1-/- muscles with an increase in the percentage of glycolytic fibers (IIX, and IIB) and a decrease of oxidative fibers (I, and IIA). This study has provided new insights into the role of TIEG1, known as KLF10, in the functional (SoltypeI: more resistant, EDLtypeIIB: less resistant) and morphological (glycolytic hypertrophy) properties of fast and slow twitch skeletal muscles. Further investigation at the cellular level will better reveal the role of the TIEG1 gene in skeletal muscle tissue.
[Mh] Termos MeSH primário: Proteínas de Ligação a DNA/genética
Deleção de Genes
Fibras Musculares de Contração Rápida/patologia
Fibras Musculares de Contração Lenta/patologia
Músculo Esquelético/fisiopatologia
Miosinas de Músculo Esquelético/metabolismo
Fatores de Transcrição/genética
[Mh] Termos MeSH secundário: Animais
Fenômenos Biomecânicos
Feminino
Hipertrofia
Camundongos
Modelos Biológicos
Músculo Esquelético/patologia
Estresse Mecânico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (Tieg1 protein, mouse); 0 (Transcription Factors); EC 3.6.1.- (Skeletal Muscle Myosins)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170522
[Lr] Data última revisão:
170522
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161014
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0164566


  2 / 93 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27421960
[Au] Autor:Deguchi H; Sinha RK; Marchese P; Ruggeri ZM; Zilberman-Rudenko J; McCarty OJT; Cohen MJ; Griffin JH
[Ad] Endereço:Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA.
[Ti] Título:Prothrombotic skeletal muscle myosin directly enhances prothrombin activation by binding factors Xa and Va.
[So] Source:Blood;128(14):1870-1878, 2016 Oct 06.
[Is] ISSN:1528-0020
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:To test the hypothesis that skeletal muscle myosins can directly influence blood coagulation and thrombosis, ex vivo studies of the effects of myosin on thrombogenesis in fresh human blood were conducted. Addition of myosin to blood augmented the thrombotic responses of human blood flowing over collagen-coated surfaces (300 s shear rate). Perfusion of human blood over myosin-coated surfaces also caused fibrin and platelet deposition, evidencing myosin's thrombogenicity. Myosin markedly enhanced thrombin generation in both platelet-rich plasma and platelet-poor plasma, indicating that myosin promoted thrombin generation in plasma primarily independent of platelets. In purified reaction mixtures composed only of factor Xa, factor Va, prothrombin, and calcium ions, myosin greatly enhanced prothrombinase activity. The Gla domain of factor Xa was not required for myosin's prothrombinase enhancement. When binding of purified clotting factors to immobilized myosin was monitored using biolayer interferometry, factors Xa and Va each showed favorable binding interactions. Factor Va reduced by 100-fold the apparent of myosin for factor Xa ( ∼0.48 nM), primarily by reducing k , indicating formation of a stable ternary complex of myosin:Xa:Va. In studies to assess possible clinical relevance for this discovery, we found that antimyosin antibodies inhibited thrombin generation in acute trauma patient plasmas more than in control plasmas ( = .0004), implying myosin might contribute to acute trauma coagulopathy. We posit that myosin enhancement of thrombin generation could contribute either to promote hemostasis or to augment thrombosis risk with consequent implications for myosin's possible contributions to pathophysiology in the setting of acute injuries.
[Mh] Termos MeSH primário: Fator Va/metabolismo
Fator Xa/metabolismo
Protrombina/metabolismo
Miosinas de Músculo Esquelético/farmacologia
Trombose/patologia
[Mh] Termos MeSH secundário: Doença Aguda
Animais
Circulação Sanguínea/efeitos dos fármacos
Estudos de Casos e Controles
Seres Humanos
Proteínas Imobilizadas/farmacologia
Interferometria
Modelos Biológicos
Plasma Rico em Plaquetas/metabolismo
Ligação Proteica/efeitos dos fármacos
Coelhos
Trombose/metabolismo
Ferimentos e Lesões/sangue
Ferimentos e Lesões/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Immobilized Proteins); 65522-14-7 (Factor Va); 9001-26-7 (Prothrombin); EC 3.4.21.6 (Factor Xa); EC 3.6.1.- (Skeletal Muscle Myosins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:160717
[St] Status:MEDLINE
[do] DOI:10.1182/blood-2016-03-707679


  3 / 93 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27022191
[Au] Autor:Li M; Andersson-Lendahl M; Sejersen T; Arner A
[Ad] Endereço:Department of Physiology and Pharmacology, Department of Cell and Molecular Biology, and Department of Women's and Children's Health, Karolinska Institutet, SE 171 77 Stockholm, Sweden.
[Ti] Título:Knockdown of fast skeletal myosin-binding protein C in zebrafish results in a severe skeletal myopathy.
[So] Source:J Gen Physiol;147(4):309-22, 2016 Apr.
[Is] ISSN:1540-7748
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Myosin-binding protein C (MyBPC) in the muscle sarcomere interacts with several contractile and structural proteins. Mutations in the cardiac isoform (MyBPC-3) in humans, or animal knockout, are associated with cardiomyopathy. Function of the fast skeletal isoform (MyBPC-2) in living muscles is less understood. This question was addressed using zebrafish models, combining gene expression data with functional analysis of contractility and small-angle x-ray diffraction measurements of filament structure. Fast skeletal MyBPC-2B, the major isoform, was knocked down by >50% using morpholino antisense nucleotides. These morphants exhibited a skeletal myopathy with elevated apoptosis and up-regulation of factors associated with muscle protein degradation. Morphant muscles had shorter sarcomeres with a broader length distribution, shorter actin filaments, and a wider interfilament spacing compared with controls, suggesting that fast skeletal MyBPC has a role in sarcomere assembly. Active force was reduced more than expected from the decrease in muscle size, suggesting that MyBPC-2 is required for optimal force generation at the cross-bridge level. The maximal shortening velocity was significantly increased in the MyBPC-2 morphants, but when related to the sarcomere length, the difference was smaller, reflecting that the decrease in MyBPC-2B content and the resulting myopathy were accompanied by only a minor influence on filament shortening kinetics. In the controls, equatorial patterns from small-angle x-ray scattering revealed that comparatively few cross-bridges are attached (as evaluated by the intensity ratio of the 11 and 10 equatorial reflections) during active contraction. X-ray scattering data from relaxed and contracting morphants were not significantly different from those in controls. However, the increase in the 11:10 intensity ratio in rigor was lower compared with that in controls, possibly reflecting effects of MyBPC on the cross-bridge interactions. In conclusion, lack of MyBPC-2 results in a severe skeletal myopathy with structural changes and muscle weakness.
[Mh] Termos MeSH primário: Doenças Musculares/genética
Sarcômeros/metabolismo
Miosinas de Músculo Esquelético/metabolismo
[Mh] Termos MeSH secundário: Actinas/metabolismo
Animais
Apoptose
Deleção de Genes
Doenças Musculares/metabolismo
Sarcômeros/patologia
Miosinas de Músculo Esquelético/genética
Peixe-Zebra
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Actins); EC 3.6.1.- (Skeletal Muscle Myosins)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160330
[St] Status:MEDLINE
[do] DOI:10.1085/jgp.201511452


  4 / 93 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26840730
[Au] Autor:Campbell KS
[Ad] Endereço:Division of Cardiovascular Medicine, Department of Physiology, University of Kentucky, Lexington, Kentucky. Electronic address: k.s.campbell@uky.edu.
[Ti] Título:Compliance Accelerates Relaxation in Muscle by Allowing Myosin Heads to Move Relative to Actin.
[So] Source:Biophys J;110(3):661-668, 2016 Feb 02.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The mechanisms that limit the speed at which striated muscles relax are poorly understood. This work presents, to our knowledge, novel simulations that show that the time course of relaxation is accelerated by interfilamentary movement resulting from series compliance; force drops faster when myosin heads move relative to actin during relaxation. This insight was obtained by using cross-bridge distribution techniques to simulate the mechanical behavior of half-sarcomeres that were connected in series with springs of varying stiffness. (The springs mimic the combined effects of half-sarcomere heterogeneity and muscle's series elastic component.) Half-sarcomeres that shortened by >∼10 nm when they were activated subsequently relaxed with a biphasic profile; force initially declined slowly and approximately linearly before collapsing with a fast exponential time course. Stretches imposed during the linear phase quickened relaxation, while shortening movements prolonged the time course. These predictions are consistent with data from experiments performed by many other groups using single muscle fibers and isolated myofibrils. When half-sarcomeres were linked to stiff springs (so that they did not shorten appreciably during the simulations), force relaxed with a slow exponential time course and did not show biphasic behavior. Together, these results suggest that fast relaxation of striated muscle is an emergent property that reflects multiscale interactions within the muscle architecture. The nonlinear behavior during relaxation reflects perturbations to the dynamic coupling of regulated binding sites and cycling myosin heads that are induced by interfilamentary movement.
[Mh] Termos MeSH primário: Actinas/metabolismo
Relaxamento Muscular
Miosinas de Músculo Esquelético/metabolismo
[Mh] Termos MeSH secundário: Aceleração
Actinas/química
Animais
Elasticidade
Seres Humanos
Modelos Teóricos
Sarcômeros/metabolismo
Miosinas de Músculo Esquelético/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Actins); EC 3.6.1.- (Skeletal Muscle Myosins)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170825
[Lr] Data última revisão:
170825
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160204
[St] Status:MEDLINE


  5 / 93 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:26586917
[Au] Autor:Bloemink MJ; Melkani GC; Bernstein SI; Geeves MA
[Ad] Endereço:From the School of Biosciences, University of Kent, CT2 7NJ Canterbury, United Kingdom and.
[Ti] Título:The Relay/Converter Interface Influences Hydrolysis of ATP by Skeletal Muscle Myosin II.
[So] Source:J Biol Chem;291(4):1763-73, 2016 Jan 22.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The interface between relay and converter domain of muscle myosin is critical for optimal myosin performance. Using Drosophila melanogaster indirect flight muscle S1, we performed a kinetic analysis of the effect of mutations in the converter and relay domain. Introduction of a mutation (R759E) in the converter domain inhibits the steady-state ATPase of myosin S1, whereas an additional mutation in the relay domain (N509K) is able to restore the ATPase toward wild-type values. The R759E S1 construct showed little effect on most steps of the actomyosin ATPase cycle. The exception was a 25-30% reduction in the rate constant of the hydrolysis step, the step coupled to the cross-bridge recovery stroke that involves a change in conformation at the relay/converter domain interface. Significantly, the double mutant restored the hydrolysis step to values similar to the wild-type myosin. Modeling the relay/converter interface suggests a possible interaction between converter residue 759 and relay residue 509 in the actin-detached conformation, which is lost in R759E but is restored in N509K/R759E. This detailed kinetic analysis of Drosophila myosin carrying the R759E mutation shows that the interface between the relay loop and converter domain is important for fine-tuning myosin kinetics, in particular ATP binding and hydrolysis.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/metabolismo
Proteínas de Drosophila/metabolismo
Drosophila melanogaster/metabolismo
Miosinas de Músculo Esquelético/metabolismo
[Mh] Termos MeSH secundário: Actinas/metabolismo
Adenosina Trifosfatases/química
Adenosina Trifosfatases/genética
Adenosina Trifosfatases/metabolismo
Trifosfato de Adenosina/química
Animais
Proteínas de Drosophila/química
Proteínas de Drosophila/genética
Drosophila melanogaster/química
Drosophila melanogaster/genética
Hidrólise
Cinética
Mutação de Sentido Incorreto
Estrutura Terciária de Proteína
Miosinas de Músculo Esquelético/química
Miosinas de Músculo Esquelético/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Actins); 0 (Drosophila Proteins); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.1.- (Skeletal Muscle Myosins)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151121
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.688002


  6 / 93 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26579948
[Au] Autor:Russ DW; Acksel C; Boyd IM; Maynard J; McCorkle KW; Edens NK; Garvey SM
[Ad] Endereço:a Laboratory for Integrative Muscle Biology, Division of Physical Therapy, School of Rehabilitation and Communication Sciences, Ohio University, Athens, OH 45701, USA.
[Ti] Título:Dietary HMB and ß-alanine co-supplementation does not improve in situ muscle function in sedentary, aged male rats.
[So] Source:Appl Physiol Nutr Metab;40(12):1294-301, 2015 Dec.
[Is] ISSN:1715-5320
[Cp] País de publicação:Canada
[La] Idioma:eng
[Ab] Resumo:This study evaluated the effects of dietary ß-hydroxy-ß-methylbutyrate (HMB) combined with ß-alanine (ß-Ala) in sedentary, aged male rats. It has been suggested that dietary HMB or ß-Ala supplementation may mitigate age-related declines in muscle strength and fatigue resistance. A total of 20 aged Sprague-Dawley rats were studied. At age 20 months, 10 rats were administered a control, purified diet and 10 rats were administered a purified diet supplemented with both HMB and ß-Ala (HMB+ß-Ala) for 8 weeks (approximately equivalent to 3 and 2.4 g per day human dose). We measured medial gastrocnemius (MG) size, force, fatigability, and myosin composition. We also evaluated an array of protein markers related to muscle mitochondria, protein synthesis and breakdown, and autophagy. HMB+ß-Ala had no significant effects on body weight, MG mass, force or fatigability, myosin composition, or muscle quality. Compared with control rats, those fed HMB+ß-Ala exhibited a reduced (41%, P = 0.039) expression of muscle RING-finger protein 1 (MURF1), a common marker of protein degradation. Muscle from rats fed HMB+ß-Ala also exhibited a 45% reduction (P = 0.023) in p70s6K phosphorylation following fatiguing stimulation. These data suggest that HMB+ß-Ala at the dose studied may reduce muscle protein breakdown by reducing MURF1 expression, but has minimal effects on muscle function in this model of uncomplicated aging. They do not, however, rule out potential benefits of HMB+ß-Ala co-supplementation at other doses or durations of supplementation in combination with exercise or in situations where extreme muscle protein breakdown and loss of mass occur (e.g., bedrest, cachexia, failure-to-thrive).
[Mh] Termos MeSH primário: Envelhecimento
Suplementos Nutricionais
Contração Muscular/efeitos dos fármacos
Força Muscular/efeitos dos fármacos
Músculo Esquelético/efeitos dos fármacos
Sarcopenia/prevenção & controle
Estilo de Vida Sedentário
Valeratos/farmacologia
beta-Alanina/farmacologia
[Mh] Termos MeSH secundário: Fatores Etários
Animais
Autofagia
Biomarcadores/metabolismo
Modelos Animais de Doenças
Masculino
Fadiga Muscular
Proteínas Musculares/metabolismo
Músculo Esquelético/metabolismo
Músculo Esquelético/patologia
Músculo Esquelético/fisiopatologia
Fosforilação
Proteólise
Ratos Sprague-Dawley
Proteínas Quinases S6 Ribossômicas 70-kDa/metabolismo
Sarcopenia/etiologia
Sarcopenia/metabolismo
Sarcopenia/patologia
Sarcopenia/fisiopatologia
Miosinas de Músculo Esquelético/metabolismo
Fatores de Tempo
Proteínas com Motivo Tripartido
Ubiquitina-Proteína Ligases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Muscle Proteins); 0 (Tripartite Motif Proteins); 0 (Valerates); 11P2JDE17B (beta-Alanine); 3F752311CD (beta-hydroxyisovaleric acid); EC 2.3.2.27 (Trim63 protein, rat); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 2.7.11.1 (Ribosomal Protein S6 Kinases, 70-kDa); EC 3.6.1.- (Skeletal Muscle Myosins)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151119
[St] Status:MEDLINE
[do] DOI:10.1139/apnm-2015-0391


  7 / 93 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:26289121
[Au] Autor:Wiedemar N; Riedi AK; Jagannathan V; Drögemüller C; Meylan M
[Ad] Endereço:Institute of Genetics, Vetsuisse Faculty, University of Berne, Berne, Switzerland.
[Ti] Título:Genetic Abnormalities in a Calf with Congenital Increased Muscular Tonus.
[So] Source:J Vet Intern Med;29(5):1418-21, 2015 Sep-Oct.
[Is] ISSN:1939-1676
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Doenças dos Bovinos/congênito
Hipertonia Muscular/veterinária
[Mh] Termos MeSH secundário: Animais
Bovinos
Doenças dos Bovinos/genética
Doenças dos Bovinos/patologia
Doenças dos Bovinos/fisiopatologia
Feminino
Hipertonia Muscular/congênito
Hipertonia Muscular/genética
Hipertonia Muscular/patologia
Hipertonia Muscular/fisiopatologia
Músculo Esquelético/patologia
Músculo Esquelético/fisiopatologia
Mutação de Sentido Incorreto
Miosinas de Músculo Esquelético/genética
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.6.1.- (Skeletal Muscle Myosins)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150821
[St] Status:MEDLINE
[do] DOI:10.1111/jvim.13599


  8 / 93 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:26222548
[Au] Autor:Mizunoya W; Miyahara H; Okamoto S; Akahoshi M; Suzuki T; Do MK; Ohtsubo H; Komiya Y; Lan M; Waga T; Iwata A; Nakazato K; Ikeuchi Y; Anderson JE; Tatsumi R
[Ad] Endereço:Department of Animal and Marine Bioresource Sciences, Graduate School of Agriculture, Kyushu University, Hakozaki, Fukuoka, Japan.
[Ti] Título:Improvement of Endurance Based on Muscle Fiber-Type Composition by Treatment with Dietary Apple Polyphenols in Rats.
[So] Source:PLoS One;10(7):e0134303, 2015.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A recent study demonstrated a positive effect of apple polyphenol (APP) intake on muscle endurance of young-adult animals. While an enhancement of lipid metabolism may be responsible, in part, for the improvement, the contributing mechanisms still need clarification. Here we show that an 8-week intake of 5% (w/w) APP in the diet, up-regulates two features related to fiber type: the ratio of myosin heavy chain (MyHC) type IIx/IIb and myoglobin protein expression in plantaris muscle of 9-week-old male Fischer F344 rats compared to pair-fed controls (P < 0.05). Results were demonstrated by our SDS-PAGE system specialized for MyHC isoform separation and western blotting of whole muscles. Animal-growth profiles (food intake, body-weight gain, and internal-organ weights) did not differ between the control and 5% APP-fed animals (n = 9/group). Findings may account for the increase in fatigue resistance of lower hind limb muscles, as evidenced by a slower decline in the maximum isometric planter-flexion torque generated by a 100-s train of electrical stimulation of the tibial nerve. Additionally, the fatigue resistance was lower after 8 weeks of a 0.5% APP diet than after 5% APP, supporting an APP-dose dependency of the shift in fiber-type composition. Therefore, the present study highlights a promising contribution of dietary APP intake to increasing endurance based on fiber-type composition in rat muscle. Results may help in developing a novel strategy for application in animal sciences, and human sports and age-related health sciences.
[Mh] Termos MeSH primário: Malus
Fibras Musculares Esqueléticas/fisiologia
Resistência Física/fisiologia
Compostos Fitoquímicos/administração & dosagem
Polifenóis/administração & dosagem
[Mh] Termos MeSH secundário: Animais
Estimulação Elétrica
Seres Humanos
Contração Isométrica/fisiologia
Masculino
Músculo Esquelético/fisiologia
Mioglobina/metabolismo
Cadeias Pesadas de Miosina/metabolismo
Isoformas de Proteínas/fisiologia
Ratos
Ratos Endogâmicos F344
Miosinas de Músculo Esquelético/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Myoglobin); 0 (Phytochemicals); 0 (Polyphenols); 0 (Protein Isoforms); EC 3.6.1.- (Skeletal Muscle Myosins); EC 3.6.4.1 (Myosin Heavy Chains)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150730
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0134303


  9 / 93 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:25848839
[Au] Autor:Carmona G; Roca E; Guerrero M; Cussó R; Irurtia A; Nescolarde L; Brotons D; Bedini JL; Cadefau JA
[Ad] Endereço:National Inst of Physical Education of Catalonia, Barcelona, Spain.
[Ti] Título:Sarcomere Disruptions of Slow Fiber Resulting From Mountain Ultramarathon.
[So] Source:Int J Sports Physiol Perform;10(8):1041-7, 2015 Nov.
[Is] ISSN:1555-0273
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: To investigate changes after a mountain ultramarathon (MUM) in the serum concentration of fast (FM) and slow (SM) myosin isoforms, which are fiber-type-specific sarcomere proteins. The changes were compared against creatine kinase (CK), a widely used fiber-sarcolemma-damage biomarker, and cardiac troponin I (cTnI), a widely used cardiac biomarker. METHODS: Observational comparison of response in a single group of 8 endurance-trained amateur athletes. Time-related changes in serum levels of CK, cTnI, SM, and FM from competitors were analyzed before, 1 h after the MUM, and 24 and 48 h after the start of the MUM by 1-way ANOVA for repeated measures or Friedman and Wilcoxon tests. Pearson correlation coefficient was employed to examine associations between variables. RESULTS: While SM was significantly (P = .009) increased in serum 24 h after the beginning of the MUM, FM and cTnI did not change significantly. Serum CK activity peak was observed 1 h after the MUM (P = .002). Moreover, serum peaks of CK and SM were highly correlated (r = .884, P = .004). CONCLUSIONS: Since there is evidence of muscle damage after prolonged mountain running, the increase in SM serum concentration after a MUM could be indirect evidence of slow- (type I) fiber-specific sarcomere disruptions.
[Mh] Termos MeSH primário: Fibras Musculares de Contração Lenta/metabolismo
Músculo Esquelético/lesões
Miosina Tipo I/sangue
Resistência Física/fisiologia
Corrida/fisiologia
Sarcômeros/metabolismo
Miosinas de Músculo Esquelético/sangue
[Mh] Termos MeSH secundário: Adulto
Biomarcadores/sangue
Creatina Quinase/sangue
Feminino
Seres Humanos
Masculino
Troponina I/sangue
[Pt] Tipo de publicação:JOURNAL ARTICLE; OBSERVATIONAL STUDY; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Biomarkers); 0 (Troponin I); EC 2.7.3.2 (Creatine Kinase); EC 3.6.1.- (Myosin Type I); EC 3.6.1.- (Skeletal Muscle Myosins)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:151105
[Lr] Data última revisão:
151105
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150408
[St] Status:MEDLINE
[do] DOI:10.1123/ijspp.2014-0267


  10 / 93 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:25775934
[Au] Autor:Kengyel A; Bécsi B; Kónya Z; Sellers JR; Erdodi F; Nyitrai M
[Ad] Endereço:Department of Biophysics, University of Pécs Medical School, Szigeti Str. 12, Pécs, H-7624, Hungary.
[Ti] Título:Ankyrin domain of myosin 16 influences motor function and decreases protein phosphatase catalytic activity.
[So] Source:Eur Biophys J;44(4):207-18, 2015 May.
[Is] ISSN:1432-1017
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The unconventional myosin 16 (Myo16), which may have a role in regulation of cell cycle and cell proliferation, can be found in both the nucleus and the cytoplasm. It has a unique, eight ankyrin repeat containing pre-motor domain, the so-called ankyrin domain (My16Ank). Ankyrin repeats are present in several other proteins, e.g., in the regulatory subunit (MYPT1) of the myosin phosphatase holoenzyme, which binds to the protein phosphatase-1 catalytic subunit (PP1c). My16Ank shows sequence similarity to MYPT1. In this work, the interactions of recombinant and isolated My16Ank were examined in vitro. To test the effects of My16Ank on myosin motor function, we used skeletal muscle myosin or nonmuscle myosin 2B. The results showed that My16Ank bound to skeletal muscle myosin (K D ≈ 2.4 µM) and the actin-activated ATPase activity of heavy meromyosin (HMM) was increased in the presence of My16Ank, suggesting that the ankyrin domain can modulate myosin motor activity. My16Ank showed no direct interaction with either globular or filamentous actin. We found, using a surface plasmon resonance-based binding technique, that My16Ank bound to PP1cα (K D ≈ 540 nM) and also to PP1cδ (K D ≈ 600 nM) and decreased its phosphatase activity towards the phosphorylated myosin regulatory light chain. Our results suggest that one function of the ankyrin domain is probably to regulate the function of Myo16. It may influence the motor activity, and in complex with the PP1c isoforms, it can play an important role in the targeted dephosphorylation of certain, as yet unidentified, intracellular proteins.
[Mh] Termos MeSH primário: Repetição de Anquirina
Proteína Fosfatase 1/metabolismo
Miosinas de Músculo Esquelético/química
[Mh] Termos MeSH secundário: Actinas/metabolismo
Animais
Ligação Proteica
Ratos
Miosinas de Músculo Esquelético/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Actins); EC 3.1.3.16 (Protein Phosphatase 1); EC 3.6.1.- (Skeletal Muscle Myosins)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150318
[St] Status:MEDLINE
[do] DOI:10.1007/s00249-015-1015-z



página 1 de 10 ir para página                        
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde