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Pesquisa : A10.690.552.500.500.700 [Categoria DeCS]
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[PMID]:28738414
[Au] Autor:Tjust AE; Danielsson A; Andersen PM; Brännström T; Pedrosa Domellöf F
[Ad] Endereço:Department of Integrative Medical Biology, Umeå University, Umeå, Sweden 2Department of Clinical Science, Ophthalmology, Umeå University, Umeå, Sweden.
[Ti] Título:Impact of Amyotrophic Lateral Sclerosis on Slow Tonic Myofiber Composition in Human Extraocular Muscles.
[So] Source:Invest Ophthalmol Vis Sci;58(9):3708-3715, 2017 Jul 01.
[Is] ISSN:1552-5783
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Purpose: To analyze the proportion and cross-sectional area of myofibers containing myosin heavy chain slow-twitch (MyHCI) and myosin heavy chain slow tonic (MyHCsto) in extraocular muscles of autopsied amyotrophic lateral sclerosis (ALS) patients with either spinal or bulbar site of disease onset. Methods: Whole-muscle cross sections from the middle portion of the medial rectus were labeled with antibodies against MyHCI or MyHCsto and laminin. Myofibers labeled with the MyHC antibodies (MyHCI+sto) and the total number of myofibers were quantified in the orbital and global layer of 6 control individuals and 18 ALS patients. The cross-sectional area of myofibers labeled for either MyHC was quantified in 130 to 472 fibers/individual in the orbital and in 180 to 573 fibers/individual in the global layer of each specimen. Results: The proportion of MyHCI+sto myofibers was significantly smaller in the orbital and global layer of ALS compared to control individuals. MyHCI+sto myofibers were significantly smaller in the global layer than in the orbital layer of ALS, whereas they were of similar size in control subjects. The decreased proportion of MyHCI+sto fibers correlated significantly with the age of death, but not disease duration, in patients who had the bulbar-onset variant of ALS but not in patients with spinal variant. Conclusions: ALS, regardless of site of onset, involves a loss of myofibers containing MyHCI+sto. Only in bulbar-onset cases did aging seem to play a role in the pathophysiological processes underlying the loss of MyHCI+sto fibers.
[Mh] Termos MeSH primário: Esclerose Amiotrófica Lateral/patologia
Fibras Musculares de Contração Lenta/patologia
Miofibrilas/patologia
Cadeias Pesadas de Miosina/metabolismo
Músculos Oculomotores/patologia
[Mh] Termos MeSH secundário: Adulto
Idoso
Idoso de 80 Anos ou mais
Miosinas Cardíacas/metabolismo
Feminino
Técnica Indireta de Fluorescência para Anticorpo
Seres Humanos
Masculino
Meia-Idade
Miofibrilas/metabolismo
Músculos Oculomotores/metabolismo
Isoformas de Proteínas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MYH7 protein, human); 0 (Protein Isoforms); EC 3.6.1.- (Cardiac Myosins); EC 3.6.4.1 (Myosin Heavy Chains)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170728
[Lr] Data última revisão:
170728
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170725
[St] Status:MEDLINE
[do] DOI:10.1167/iovs.17-22098


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[PMID]:28712031
[Au] Autor:Koskinen SOA; Kyröläinen H; Flink R; Selänne HP; Gagnon SS; Ahtiainen JP; Nindl BC; Lehti M
[Ad] Endereço:LIKES Research Centre for Physical Activity and Health, Rautpohjankatu 8, 40700, Jyväskylä, Finland. satuosmianneli@hotmail.com.
[Ti] Título:Human skeletal muscle type 1 fibre distribution and response of stress-sensing proteins along the titin molecule after submaximal exhaustive exercise.
[So] Source:Histochem Cell Biol;148(5):545-555, 2017 Nov.
[Is] ISSN:1432-119X
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Early responses of stress-sensing proteins, muscle LIM protein (MLP), ankyrin repeat proteins (Ankrd1/CARP and Ankrd2/Arpp) and muscle-specific RING finger proteins (MuRF1 and MuRF2), along the titin molecule were investigated in the present experiment after submaximal exhaustive exercise. Ten healthy men performed continuous drop jumping unilaterally on a sledge apparatus with a submaximal height until complete exhaustion. Five stress-sensing proteins were analysed by mRNA measurements from biopsies obtained immediately and 3 h after the exercise from exercised vastus lateralis muscle while control biopsies were obtained from non-exercised legs before the exercise. Decreased maximal jump height and increased serum creatine kinase activities as indirect markers for muscle damage and HSP27 immunostainings on muscle biopsies as a direct marker for muscle damage indicated that the current exercised protocol caused muscle damage. mRNA levels for four (MLP, Ankrd1/CARP, MuRF1 and MuRF2) out of the five studied stress sensors significantly (p < 0.05) increased 3 h after fatiguing exercise. The magnitude of MLP and Ankrd2 responses was related to the proportion of type 1 myofibres. Our data showed that the submaximal exhaustive exercise with subject's own physical fitness level activates titin-based stretch-sensing proteins. These results suggest that both degenerative and regenerative pathways are activated in very early phase after the exercise or probably already during the exercise. Activation of these proteins represents an initial step forward adaptive remodelling of the exercised muscle and may also be involved in the initiation of myofibre repair.
[Mh] Termos MeSH primário: Conectina/metabolismo
Exercício
Fibras Musculares de Contração Lenta/metabolismo
Proteínas Musculares/metabolismo
Esforço Físico
[Mh] Termos MeSH secundário: Adolescente
Adulto
Seres Humanos
Masculino
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Connectin); 0 (Muscle Proteins); 0 (TTN protein, human)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171108
[Lr] Data última revisão:
171108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170717
[St] Status:MEDLINE
[do] DOI:10.1007/s00418-017-1595-z


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[PMID]:28654264
[Au] Autor:Yang K; Wang L; Zhou G; Lin X; Peng J; Wang L; Luo L; Wang J; Shu G; Wang S; Gao P; Zhu X; Xi Q; Zhang Y; Jiang Q
[Ad] Endereço:College of Animal Science and National Engineering Research Center for Breeding Swine Industry, South China Agricultural University , Guangzhou, Guangdong 510640, People's Republic of China.
[Ti] Título:Phytol Promotes the Formation of Slow-Twitch Muscle Fibers through PGC-1α/miRNA but Not Mitochondria Oxidation.
[So] Source:J Agric Food Chem;65(29):5916-5925, 2017 Jul 26.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Phytol is a side chain of chlorophyll belonging to the side-chain double terpenoid. When animals consume food rich in chlorophyll, phytol can be broken down to phytanic acid after digestion. It was reported that feeding animals with different varieties and levels of forage could significant improve pH and marbling score of steer and lamb carcasses, but the internal mechanism for this is still not reported. The marbling score and pH of muscle was mainly determined by skeletal muscle fiber type, which is due to expression of different myosin heavy-chain (MHC) isoforms. Here, we provide evidence that phytol can indeed affect the diversity of muscle fiber types both in vitro and in vivo and demonstrate that phytol can increase the expression of MHC I (p < 0.05), likely by upgrading the expression of PPARδ, PGC-1α, and related miRNAs. This fiber-type transformation process may not be caused by activated mitochondrial metabolism but by the structural changes in muscle fiber types.
[Mh] Termos MeSH primário: MicroRNAs/metabolismo
Mitocôndrias/metabolismo
Fibras Musculares de Contração Lenta/metabolismo
Coativador 1-alfa do Receptor gama Ativado por Proliferador de Peroxissomo/metabolismo
Fitol/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Masculino
Camundongos
MicroRNAs/genética
Mitocôndrias/genética
Fibras Musculares Esqueléticas/metabolismo
Oxirredução
Coativador 1-alfa do Receptor gama Ativado por Proliferador de Peroxissomo/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MicroRNAs); 0 (Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha); 0 (Ppargc1a protein, mouse); 150-86-7 (Phytol)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170809
[Lr] Data última revisão:
170809
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170628
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b01048


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[PMID]:28592414
[Au] Autor:Fajardo VA; Rietze BA; Chambers PJ; Bellissimo C; Bombardier E; Quadrilatero J; Tupling AR
[Ad] Endereço:Department of Kinesiology, University of Waterloo, Waterloo Ontario, Canada.
[Ti] Título:Effects of sarcolipin deletion on skeletal muscle adaptive responses to functional overload and unload.
[So] Source:Am J Physiol Cell Physiol;313(2):C154-C161, 2017 Aug 01.
[Is] ISSN:1522-1563
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Overexpression of sarcolipin (SLN), a regulator of sarco(endo)plasmic reticulum Ca -ATPases (SERCAs), stimulates calcineurin signaling to enhance skeletal muscle oxidative capacity. Some studies have shown that calcineurin may also control skeletal muscle mass and remodeling in response to functional overload and unload stimuli by increasing myofiber size and the proportion of slow fibers. To examine whether SLN might mediate these adaptive responses, we performed soleus and gastrocnemius tenotomy in wild-type (WT) and -null ( ) mice and examined the overloaded plantaris and unloaded/tenotomized soleus muscles. In the WT overloaded plantaris, we observed ectopic expression of SLN, myofiber hypertrophy, increased fiber number, and a fast-to-slow fiber type shift, which were associated with increased calcineurin signaling (NFAT dephosphorylation and increased stabilin-2 protein content) and reduced SERCA activity. In the WT tenotomized soleus, we observed a 14-fold increase in SLN protein, myofiber atrophy, decreased fiber number, and a slow-to-fast fiber type shift, which were also associated with increased calcineurin signaling and reduced SERCA activity. Genetic deletion of altered these physiological outcomes, with the overloaded plantaris myofibers failing to grow in size and number, and transition towards the slow fiber type, while the unloaded soleus muscles exhibited greater reductions in fiber size and number, and an accelerated slow-to-fast fiber type shift. In both the overloaded and unloaded muscles, these findings were associated with elevated SERCA activity and blunted calcineurin signaling. Thus, SLN plays an important role in adaptive muscle remodeling potentially through calcineurin stimulation, which could have important implications for other muscle diseases and conditions.
[Mh] Termos MeSH primário: Calcineurina/metabolismo
Proteínas Musculares/genética
Músculo Esquelético/metabolismo
Proteolipídeos/genética
[Mh] Termos MeSH secundário: Animais
Regulação da Expressão Gênica
Seres Humanos
Camundongos
Camundongos Knockout
Fibras Musculares de Contração Rápida/metabolismo
Fibras Musculares de Contração Lenta/metabolismo
Proteínas Musculares/metabolismo
Músculo Esquelético/fisiologia
Músculo Esquelético/cirurgia
Proteolipídeos/metabolismo
ATPases Transportadoras de Cálcio do Retículo Sarcoplasmático/genética
ATPases Transportadoras de Cálcio do Retículo Sarcoplasmático/metabolismo
Tenotomia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Muscle Proteins); 0 (Proteolipids); 145018-73-1 (sarcolipin); EC 3.1.3.16 (Calcineurin); EC 3.6.3.8 (Sarcoplasmic Reticulum Calcium-Transporting ATPases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170814
[Lr] Data última revisão:
170814
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170609
[St] Status:MEDLINE
[do] DOI:10.1152/ajpcell.00291.2016


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[PMID]:28446426
[Au] Autor:Bondì M; Germinario E; Pirazzini M; Zanetti G; Cencetti F; Donati C; Gorza L; Betto R; Bruni P; Danieli-Betto D
[Ad] Endereço:Department of Biomedical Sciences, University of Padova, Padua, Italy.
[Ti] Título:Ablation of S1P receptor protects mouse soleus from age-related drop in muscle mass, force, and regenerative capacity.
[So] Source:Am J Physiol Cell Physiol;313(1):C54-C67, 2017 Jul 01.
[Is] ISSN:1522-1563
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We investigated the effects of S1P deficiency on the age-related atrophy, decline in force, and regenerative capacity of soleus muscle from 23-mo-old male (old) mice. Compared with muscle from 5-mo-old (adult) mice, soleus mass and muscle fiber cross-sectional area (CSA) in old wild-type mice were reduced by ~26% and 24%, respectively. By contrast, the mass and fiber CSA of soleus muscle in old S1P -null mice were comparable to those of adult muscle. Moreover, in soleus muscle of wild-type mice, twitch and tetanic tensions diminished from adulthood to old age. A slowing of contractile properties was also observed in soleus from old wild-type mice. In S1P -null mice, neither force nor the contractile properties of soleus changed during aging. We also evaluated the regenerative capacity of soleus in old S1P -null mice by stimulating muscle regeneration through myotoxic injury. After 10 days of regeneration, the mean fiber CSA of soleus in old wild-type mice was significantly smaller (-28%) compared with that of regenerated muscle in adult mice. On the contrary, the mean fiber CSA of regenerated soleus in old S1P -null mice was similar to that of muscle in adult mice. We conclude that in the absence of S1P , soleus muscle is protected from the decrease in muscle mass and force, and the attenuation of regenerative capacity, all of which are typical characteristics of aging.
[Mh] Termos MeSH primário: Envelhecimento/genética
Músculo Esquelético/metabolismo
Receptores de Lisoesfingolipídeo/genética
Sarcopenia/genética
[Mh] Termos MeSH secundário: Envelhecimento/metabolismo
Animais
Expressão Gênica
Masculino
Camundongos
Camundongos Knockout
Contração Muscular/fisiologia
Fibras Musculares de Contração Lenta/metabolismo
Fibras Musculares de Contração Lenta/patologia
Força Muscular/fisiologia
Músculo Esquelético/fisiopatologia
Receptores de Lisoesfingolipídeo/deficiência
Regeneração/fisiologia
Sarcopenia/metabolismo
Sarcopenia/fisiopatologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Edg3 protein, mouse); 0 (Receptors, Lysosphingolipid)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170802
[Lr] Data última revisão:
170802
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE
[do] DOI:10.1152/ajpcell.00027.2017


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[PMID]:28390800
[Au] Autor:Kelu JJ; Webb SE; Parrington J; Galione A; Miller AL
[Ad] Endereço:Division of Life Science & State Key Laboratory of Molecular Neuroscience, HKUST, Clear Water Bay, Hong Kong, PR China.
[Ti] Título:Ca release via two-pore channel type 2 (TPC2) is required for slow muscle cell myofibrillogenesis and myotomal patterning in intact zebrafish embryos.
[So] Source:Dev Biol;425(2):109-129, 2017 05 15.
[Is] ISSN:1095-564X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We recently demonstrated a critical role for two-pore channel type 2 (TPC2)-mediated Ca release during the differentiation of slow (skeletal) muscle cells (SMC) in intact zebrafish embryos, via the introduction of a translational-blocking morpholino antisense oligonucleotide (MO). Here, we extend our study and demonstrate that knockdown of TPC2 with a non-overlapping splice-blocking MO, knockout of TPC2 (via the generation of a tpcn2 mutant line of zebrafish using CRISPR/Cas9 gene-editing), or the pharmacological inhibition of TPC2 action with bafilomycin A1 or trans-ned-19, also lead to a significant attenuation of SMC differentiation, characterized by a disruption of SMC myofibrillogenesis and gross morphological changes in the trunk musculature. When the morphants were injected with tpcn2-mRNA or were treated with IP /BM or caffeine (agonists of the inositol 1,4,5-trisphosphate receptor (IP R) and ryanodine receptor (RyR), respectively), many aspects of myofibrillogenesis and myotomal patterning (and in the case of the pharmacological treatments, the Ca signals generated in the SMCs), were rescued. STED super-resolution microscopy revealed a close physical relationship between clusters of RyR in the terminal cisternae of the sarcoplasmic reticulum (SR), and TPC2 in lysosomes, with a mean estimated separation of ~52-87nm. Our data therefore add to the increasing body of evidence, which indicate that localized Ca release via TPC2 might trigger the generation of more global Ca release from the SR via Ca -induced Ca release.
[Mh] Termos MeSH primário: Padronização Corporal
Canais de Cálcio/metabolismo
Cálcio/metabolismo
Embrião não Mamífero/metabolismo
Cinesina/metabolismo
Desenvolvimento Muscular
Fibras Musculares de Contração Lenta/metabolismo
Proteínas de Peixe-Zebra/metabolismo
Peixe-Zebra/embriologia
Peixe-Zebra/metabolismo
[Mh] Termos MeSH secundário: Animais
Sequência de Bases
Comportamento Animal/efeitos dos fármacos
Padronização Corporal/efeitos dos fármacos
Sistemas CRISPR-Cas/genética
Cafeína/farmacologia
Sinalização do Cálcio/efeitos dos fármacos
Morte Celular/efeitos dos fármacos
Células Cultivadas
Embrião não Mamífero/efeitos dos fármacos
Técnicas de Silenciamento de Genes
Técnicas de Inativação de Genes
Receptores de Inositol 1,4,5-Trifosfato/metabolismo
Macrolídeos/farmacologia
Modelos Biológicos
Morfolinos/farmacologia
Atividade Motora/efeitos dos fármacos
Células Musculares/citologia
Células Musculares/efeitos dos fármacos
Células Musculares/metabolismo
Desenvolvimento Muscular/efeitos dos fármacos
Fibras Musculares de Contração Lenta/citologia
Fibras Musculares de Contração Lenta/efeitos dos fármacos
Fenótipo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Canal de Liberação de Cálcio do Receptor de Rianodina/metabolismo
Sarcômeros/efeitos dos fármacos
Sarcômeros/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Calcium Channels); 0 (Inositol 1,4,5-Trisphosphate Receptors); 0 (Kif7 protein, zebrafish); 0 (Macrolides); 0 (Morpholinos); 0 (RNA, Messenger); 0 (Ryanodine Receptor Calcium Release Channel); 0 (TPC2 protein, zebrafish); 0 (Zebrafish Proteins); 3G6A5W338E (Caffeine); 88899-55-2 (bafilomycin A1); EC 3.6.4.4 (Kinesin); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171110
[Lr] Data última revisão:
171110
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170410
[St] Status:MEDLINE


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[PMID]:28278204
[Au] Autor:Fajardo VA; Gamu D; Mitchell A; Bloemberg D; Bombardier E; Chambers PJ; Bellissimo C; Quadrilatero J; Tupling AR
[Ad] Endereço:Department of Kinesiology, University of Waterloo, Waterloo, Ontario, Canada, N2L 3G1.
[Ti] Título:Sarcolipin deletion exacerbates soleus muscle atrophy and weakness in phospholamban overexpressing mice.
[So] Source:PLoS One;12(3):e0173708, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sarcolipin (SLN) and phospholamban (PLN) are two small proteins that regulate the sarco(endo)plasmic reticulum Ca2+-ATPase pumps. In a recent study, we discovered that Pln overexpression (PlnOE) in slow-twitch type I skeletal muscle fibers drastically impaired SERCA function and caused a centronuclear myopathy-like phenotype, severe muscle atrophy and weakness, and an 8 to 9-fold upregulation of SLN protein in the soleus muscles. Here, we sought to determine the physiological role of SLN upregulation, and based on its role as a SERCA inhibitor, we hypothesized that it would represent a maladaptive response that contributes to the SERCA dysfunction and the overall myopathy observed in the PlnOE mice. To this end, we crossed Sln-null (SlnKO) mice with PlnOE mice to generate a PlnOE/SlnKO mouse colony and assessed SERCA function, CNM pathology, in vitro contractility, muscle mass, calcineurin signaling, daily activity and food intake, and proteolytic enzyme activity. Our results indicate that genetic deletion of Sln did not improve SERCA function nor rescue the CNM phenotype, but did result in exacerbated muscle atrophy and weakness, due to a failure to induce type II fiber compensatory hypertrophy and a reduction in total myofiber count. Mechanistically, our findings suggest that impaired calcineurin activation and resultant decreased expression of stabilin-2, and/or impaired autophagic signaling could be involved. Future studies should examine these possibilities. In conclusion, our study demonstrates the importance of SLN upregulation in combating muscle myopathy in the PlnOE mice, and since SLN is upregulated across several myopathies, our findings may reveal SLN as a novel and universal therapeutic target.
[Mh] Termos MeSH primário: Proteínas de Ligação ao Cálcio/fisiologia
Fibras Musculares de Contração Lenta/patologia
Proteínas Musculares/fisiologia
Músculo Esquelético/patologia
Atrofia Muscular/patologia
Proteolipídeos/fisiologia
ATPases Transportadoras de Cálcio do Retículo Sarcoplasmático/metabolismo
Retículo Sarcoplasmático/patologia
[Mh] Termos MeSH secundário: Animais
Cálcio/metabolismo
Modelos Animais de Doenças
Feminino
Transporte de Íons
Masculino
Camundongos
Camundongos Knockout
Contração Muscular
Fibras Musculares de Contração Lenta/metabolismo
Músculo Esquelético/metabolismo
Atrofia Muscular/metabolismo
Retículo Sarcoplasmático/metabolismo
Deleção de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Calcium-Binding Proteins); 0 (Muscle Proteins); 0 (Proteolipids); 0 (phospholamban); 145018-73-1 (sarcolipin); EC 3.6.3.8 (Sarcoplasmic Reticulum Calcium-Transporting ATPases); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170310
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0173708


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[PMID]:28207742
[Au] Autor:Julien SG; Kim SY; Brunmeir R; Sinnakannu JR; Ge X; Li H; Ma W; Yaligar J; Kn BP; Velan SS; Röder PV; Zhang Q; Sim CK; Wu J; Garcia-Miralles M; Pouladi MA; Xie W; McFarlane C; Han W; Xu F
[Ad] Endereço:Singapore Institute for Clinical Sciences, Agency for Science, Technology and Research (A*STAR), Singapore, Republic of Singapore.
[Ti] Título:Narciclasine attenuates diet-induced obesity by promoting oxidative metabolism in skeletal muscle.
[So] Source:PLoS Biol;15(2):e1002597, 2017 Feb.
[Is] ISSN:1545-7885
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Obesity develops when caloric intake exceeds metabolic needs. Promoting energy expenditure represents an attractive approach in the prevention of this fast-spreading epidemic. Here, we report a novel pharmacological strategy in which a natural compound, narciclasine (ncls), attenuates diet-induced obesity (DIO) in mice by promoting energy expenditure. Moreover, ncls promotes fat clearance from peripheral metabolic tissues, improves blood metabolic parameters in DIO mice, and protects these mice from the loss of voluntary physical activity. Further investigation suggested that ncls achieves these beneficial effects by promoting a shift from glycolytic to oxidative muscle fibers in the DIO mice thereby enhancing mitochondrial respiration and fatty acid oxidation (FAO) in the skeletal muscle. Moreover, ncls strongly activates AMPK signaling specifically in the skeletal muscle. The beneficial effects of ncls treatment in fat clearance and AMPK activation were faithfully reproduced in vitro in cultured murine and human primary myotubes. Mechanistically, ncls increases cellular cAMP concentration and ADP/ATP ratio, which further lead to the activation of AMPK signaling. Blocking AMPK signaling through a specific inhibitor significantly reduces FAO in myotubes. Finally, ncls also enhances mitochondrial membrane potential and reduces the formation of reactive oxygen species in cultured myotubes.
[Mh] Termos MeSH primário: Alcaloides de Amaryllidaceae/farmacologia
Alcaloides de Amaryllidaceae/uso terapêutico
Dieta/efeitos adversos
Músculo Esquelético/metabolismo
Obesidade/tratamento farmacológico
Obesidade/metabolismo
Fenantridinas/farmacologia
Fenantridinas/uso terapêutico
[Mh] Termos MeSH secundário: Proteínas Quinases Ativadas por AMP/metabolismo
Difosfato de Adenosina/metabolismo
Trifosfato de Adenosina/metabolismo
Animais
Biomarcadores/metabolismo
Respiração Celular/efeitos dos fármacos
Células Cultivadas
AMP Cíclico/metabolismo
Dieta Hiperlipídica
Metabolismo Energético/efeitos dos fármacos
Ativação Enzimática/efeitos dos fármacos
Ácidos Graxos/metabolismo
Seres Humanos
Masculino
Potencial da Membrana Mitocondrial/efeitos dos fármacos
Camundongos
Camundongos Endogâmicos C57BL
Mitocôndrias/efeitos dos fármacos
Mitocôndrias/metabolismo
Fibras Musculares Esqueléticas/efeitos dos fármacos
Fibras Musculares Esqueléticas/metabolismo
Fibras Musculares de Contração Lenta/efeitos dos fármacos
Fibras Musculares de Contração Lenta/metabolismo
Músculo Esquelético/efeitos dos fármacos
Oxirredução/efeitos dos fármacos
Condicionamento Físico Animal
Substâncias Protetoras/farmacologia
Substâncias Protetoras/uso terapêutico
Espécies Reativas de Oxigênio/metabolismo
Transdução de Sinais/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amaryllidaceae Alkaloids); 0 (Biomarkers); 0 (Fatty Acids); 0 (Phenanthridines); 0 (Protective Agents); 0 (Reactive Oxygen Species); 29477-83-6 (narciclasine); 61D2G4IYVH (Adenosine Diphosphate); 8L70Q75FXE (Adenosine Triphosphate); E0399OZS9N (Cyclic AMP); EC 2.7.11.31 (AMP-Activated Protein Kinases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170217
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pbio.1002597


  9 / 2224 MEDLINE  
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[PMID]:28161523
[Au] Autor:Zhang W; Roy S
[Ad] Endereço:Institute of Molecular and Cell Biology, Proteos, 61 Biopolis Drive, Singapore 138673, Singapore.
[Ti] Título:Myomaker is required for the fusion of fast-twitch myocytes in the zebrafish embryo.
[So] Source:Dev Biol;423(1):24-33, 2017 03 01.
[Is] ISSN:1095-564X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:During skeletal muscle development, myocytes aggregate and fuse to form multinucleated muscle fibers. Inhibition of myocyte fusion is thought to significantly derail the differentiation of functional muscle fibers. Despite the purported importance of fusion in myogenesis, in vivo studies of this process in vertebrates are rather limited. Myomaker, a multipass transmembrane protein, has been shown to be the first muscle-specific fusion protein essential for myocyte fusion in the mouse. We have generated loss-of-function alleles in zebrafish myomaker, and found that fusion of myocytes into syncytial fast-twitch muscles was significantly compromised. However, mutant myocytes could be recruited to fuse with wild-type myocytes in chimeric embryos, albeit rather inefficiently. Conversely, overexpression of Myomaker was sufficient to induce hyperfusion among fast-twitch myocytes, and it also induced fusion among slow-twitch myocytes that are normally fusion-incompetent. In line with this, Myomaker overexpression also triggered fusion in another myocyte fusion mutant compromised in the function of the junctional cell adhesion molecule, Jam2a. We also provide evidence that Rac, a regulator of actin cytoskeleton, requires Myomaker activity to induce fusion, and that an approximately 3kb of myomaker promoter sequence, with multiple E-box motifs, is sufficient to direct expression within the fast-twitch muscle lineage. Taken together, our findings underscore a conserved role for Myomaker in vertebrate myocyte fusion. Strikingly, and in contrast to the mouse, homozygous myomaker mutants are viable and do not exhibit discernible locomotory defects. Thus, in the zebrafish, myocyte fusion is not an absolute requirement for skeletal muscle morphogenesis and function.
[Mh] Termos MeSH primário: Embrião não Mamífero/citologia
Embrião não Mamífero/metabolismo
Proteínas de Membrana/metabolismo
Células Musculares/citologia
Células Musculares/metabolismo
Fibras Musculares de Contração Rápida/citologia
Proteínas Musculares/metabolismo
Proteínas de Peixe-Zebra/metabolismo
Peixe-Zebra/embriologia
[Mh] Termos MeSH secundário: Animais
Sequência de Bases
Fusão Celular
Linhagem da Célula/genética
Elementos E-Box/genética
Genes Reporter
Locomoção
Proteínas de Membrana/genética
Fibras Musculares de Contração Rápida/metabolismo
Fibras Musculares de Contração Lenta/metabolismo
Proteínas Musculares/genética
Mutação/genética
Fenótipo
Regiões Promotoras Genéticas/genética
Natação
Peixe-Zebra/genética
Proteínas de Peixe-Zebra/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Membrane Proteins); 0 (Muscle Proteins); 0 (Zebrafish Proteins); 0 (myomaker protein, zebrafish)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171110
[Lr] Data última revisão:
171110
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170206
[St] Status:MEDLINE


  10 / 2224 MEDLINE  
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[PMID]:28076365
[Au] Autor:Gambara G; Salanova M; Ciciliot S; Furlan S; Gutsmann M; Schiffl G; Ungethuem U; Volpe P; Gunga HC; Blottner D
[Ad] Endereço:Center for Space Medicine Berlin, Neuromuscular Group, Charité Universitätsmedizin Berlin, Berlin, Germany.
[Ti] Título:Gene Expression Profiling in Slow-Type Calf Soleus Muscle of 30 Days Space-Flown Mice.
[So] Source:PLoS One;12(1):e0169314, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Microgravity exposure as well as chronic disuse are two main causes of skeletal muscle atrophy in animals and humans. The antigravity calf soleus is a reference postural muscle to investigate the mechanism of disuse-induced maladaptation and plasticity of human and rodent (rats or mice) skeletal musculature. Here, we report microgravity-induced global gene expression changes in space-flown mouse skeletal muscle and the identification of yet unknown disuse susceptible transcripts found in soleus (a mainly slow phenotype) but not in extensor digitorum longus (a mainly fast phenotype dorsiflexor as functional counterpart to soleus). Adult C57Bl/N6 male mice (n = 5) flew aboard a biosatellite for 30 days on orbit (BION-M1 mission, 2013), a sex and age-matched cohort were housed in standard vivarium cages (n = 5), or in a replicate flight habitat as ground control (n = 5). Next to disuse atrophy signs (reduced size and myofiber phenotype I to II type shift) as much as 680 differentially expressed genes were found in the space-flown soleus, and only 72 in extensor digitorum longus (only 24 genes in common) compared to ground controls. Altered expression of gene transcripts matched key biological processes (contractile machinery, calcium homeostasis, muscle development, cell metabolism, inflammatory and oxidative stress response). Some transcripts (Fzd9, Casq2, Kcnma1, Ppara, Myf6) were further validated by quantitative real-time PCR (qRT-PCR). Besides previous reports on other leg muscle types we put forth for the first time a complete set of microgravity susceptible gene transcripts in soleus of mice as promising new biomarkers or targets for optimization of physical countermeasures and rehabilitation protocols to overcome disuse atrophy conditions in different clinical settings, rehabilitation and spaceflight.
[Mh] Termos MeSH primário: Fibras Musculares de Contração Lenta/metabolismo
Músculo Esquelético/metabolismo
Atrofia Muscular/genética
Voo Espacial
Ausência de Peso
[Mh] Termos MeSH secundário: Animais
Perfilação da Expressão Gênica
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Análise em Microsséries
Atrofia Muscular/etiologia
Atrofia Muscular/metabolismo
Fatores de Tempo
Ausência de Peso/efeitos adversos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170810
[Lr] Data última revisão:
170810
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170112
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0169314



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