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1.
J Cardiovasc Magn Reson ; 22(1): 49, 2020 06 29.
Artigo em Inglês | MEDLINE | ID: mdl-32600420

RESUMO

BACKGROUND: The right ventricle (RV) often fails when functioning as the systemic ventricle, but the cause is not understood. We tested the hypothesis that myofiber organization is abnormal in the failing systemic right ventricle. METHODS: We used diffusion-weighted cardiovascular magnetic resonance imaging to examine 3 failing hearts explanted from young patients with a systemic RV and one structurally normal heart with postnatally acquired RV hypertrophy for comparison. Diffusion compartment imaging was computed to separate the free diffusive component representing free water from an anisotropic component characterizing the orientation and diffusion characteristics of myofibers. The orientation of each anisotropic compartment was displayed in glyph format and used for qualitative description of myofibers and for construction of tractograms. The helix angle was calculated across the ventricular walls in 5 locations and displayed graphically. Scalar parameters (fractional anisotropy and mean diffusivity) were compared among specimens. RESULTS: The hypertrophied systemic RV has an inner layer, comprising about 2/3 of the wall, composed of hypertrophied trabeculae and an epicardial layer of circumferential myofibers. Myofibers within smaller trabeculae are aligned and organized with parallel fibers while larger, composite bundles show marked disarray, largely between component trabeculae. We observed a narrow range of helix angles in the outer, compact part of the wall consistent with aligned, approximately circumferential fibers. However, there was marked variation of helix angle in the inner, trabecular part of the wall consistent with marked variation in fiber orientation. The apical whorl was disrupted or incomplete and we observed myocardial whorls or vortices at other locations. Fractional anisotropy was lower in abnormal hearts while mean diffusivity was more variable, being higher in 2 but lower in 1 heart, compared to the structurally normal heart. CONCLUSIONS: Myofiber organization is abnormal in the failing systemic RV and might be an important substrate for heart failure and arrhythmia. It is unclear if myofiber disorganization is due to hemodynamic factors, developmental problems, or both.


Assuntos
Imagem de Difusão por Ressonância Magnética , Cardiopatias Congênitas/diagnóstico por imagem , Insuficiência Cardíaca/diagnóstico por imagem , Ventrículos do Coração/diagnóstico por imagem , Miocárdio/patologia , Miofibrilas/patologia , Disfunção Ventricular Direita/diagnóstico por imagem , Função Ventricular Direita , Adolescente , Pré-Escolar , Feminino , Cardiopatias Congênitas/patologia , Cardiopatias Congênitas/fisiopatologia , Cardiopatias Congênitas/cirurgia , Insuficiência Cardíaca/patologia , Insuficiência Cardíaca/fisiopatologia , Insuficiência Cardíaca/cirurgia , Transplante de Coração , Ventrículos do Coração/patologia , Ventrículos do Coração/fisiopatologia , Ventrículos do Coração/cirurgia , Humanos , Masculino , Valor Preditivo dos Testes , Disfunção Ventricular Direita/patologia , Disfunção Ventricular Direita/fisiopatologia , Disfunção Ventricular Direita/cirurgia , Adulto Jovem
2.
PLoS One ; 15(7): e0232137, 2020.
Artigo em Inglês | MEDLINE | ID: mdl-32614896

RESUMO

In sarcomeres, α-actinin crosslinks thin filaments and anchors them at the Z-disc. Drosophila melanogaster Zasp52 also localizes at Z-discs and interacts with α-actinin via its extended PDZ domain, thereby contributing to myofibril assembly and maintenance, yet the detailed mechanism of Zasp52 function is unknown. Here we show a strong genetic interaction between actin and Zasp52 during indirect flight muscle assembly, indicating that this interaction plays a critical role during myofibril assembly. Our results suggest that Zasp52 contains an actin-binding site, which includes the extended PDZ domain and the ZM region. Zasp52 binds with micromolar affinity to monomeric actin. A co-sedimentation assay indicates that Zasp52 can also bind to F-actin. Finally, we use in vivo rescue assays of myofibril assembly to show that the α-actinin-binding domain of Zasp52 is not sufficient for a full rescue of Zasp52 mutants suggesting additional contributions of Zasp52 actin-binding to myofibril assembly.


Assuntos
Actinas/metabolismo , Proteínas de Transporte/metabolismo , Proteínas de Drosophila/metabolismo , Miofibrilas/metabolismo , Animais , Proteínas de Transporte/química , Proteínas de Transporte/genética , Proteínas de Drosophila/química , Proteínas de Drosophila/genética , Drosophila melanogaster/metabolismo , Domínios PDZ , Ligação Proteica
3.
Nat Commun ; 11(1): 3711, 2020 07 24.
Artigo em Inglês | MEDLINE | ID: mdl-32709891

RESUMO

The skeletal muscle T-tubule is a specialized membrane domain essential for coordinated muscle contraction. However, in the absence of genetically tractable systems the mechanisms involved in T-tubule formation are unknown. Here, we use the optically transparent and genetically tractable zebrafish system to probe T-tubule development in vivo. By combining live imaging of transgenic markers with three-dimensional electron microscopy, we derive a four-dimensional quantitative model for T-tubule formation. To elucidate the mechanisms involved in T-tubule formation in vivo, we develop a quantitative screen for proteins that associate with and modulate early T-tubule formation, including an overexpression screen of the entire zebrafish Rab protein family. We propose an endocytic capture model involving firstly, formation of dynamic endocytic tubules at transient nucleation sites on the sarcolemma, secondly, stabilization by myofibrils/sarcoplasmic reticulum and finally, delivery of membrane from the recycling endosome and Golgi complex.


Assuntos
Contração Muscular/fisiologia , Proteínas Musculares/metabolismo , Músculo Esquelético/metabolismo , Músculo Esquelético/ultraestrutura , Sarcolema/fisiologia , Sarcolema/ultraestrutura , Animais , Canais de Cálcio/metabolismo , Canais de Cálcio/ultraestrutura , Canais de Cálcio Tipo L/metabolismo , Proteínas de Transporte/metabolismo , Biologia do Desenvolvimento , Complexo de Golgi/metabolismo , Masculino , Microscopia Eletrônica , Proteínas Musculares/química , Músculo Esquelético/química , Miofibrilas/metabolismo , Sarcolema/química , Retículo Sarcoplasmático/metabolismo , Peixe-Zebra
4.
Nat Commun ; 11(1): 3722, 2020 07 24.
Artigo em Inglês | MEDLINE | ID: mdl-32709902

RESUMO

Human movement occurs through contraction of the basic unit of the muscle cell, the sarcomere. Sarcomeres have long been considered to be arranged end-to-end in series along the length of the muscle into tube-like myofibrils with many individual, parallel myofibrils comprising the bulk of the muscle cell volume. Here, we demonstrate that striated muscle cells form a continuous myofibrillar matrix linked together by frequently branching sarcomeres. We find that all muscle cells contain highly connected myofibrillar networks though the frequency of sarcomere branching goes down from early to late postnatal development and is higher in slow-twitch than fast-twitch mature muscles. Moreover, we show that the myofibrillar matrix is united across the entire width of the muscle cell both at birth and in mature muscle. We propose that striated muscle force is generated by a singular, mesh-like myofibrillar network rather than many individual, parallel myofibrils.


Assuntos
Fenômenos Mecânicos , Músculo Esquelético/fisiologia , Miofibrilas/fisiologia , Sarcômeros/fisiologia , Animais , Feminino , Humanos , Masculino , Camundongos , Camundongos Endogâmicos C57BL , Microscopia Eletrônica , Contração Muscular/fisiologia , Desenvolvimento Muscular , Músculo Esquelético/citologia , Miofibrilas/patologia , Sarcômeros/patologia
5.
Food Chem ; 328: 127144, 2020 Oct 30.
Artigo em Inglês | MEDLINE | ID: mdl-32474242

RESUMO

The combined effects of ultrasound (intensity of 15.6 W/cm2 and sonication for 5 min) with potassium alginate (PA) marination (UPA) on tenderizing old chicken breast meat, and possible mechanisms from tissue to protein, were investigated. UPA-treated meat exhibited the lowest moisture loss and shear force (optimized tenderness). The increased fiber space benefited PA invasion to form a heat-induced barrier for harder muscle contraction and avoid moisture withdrawal. Special scale-like structures of dried myofibrillar protein (MP) and the three-dimensional network induced by interactions between PA and MP increased the tenderness. UPA treatment induced stronger electrostatic repulsion between PA molecules and more ß-sheet structures of MP, accompanied by a smallest size. The more easily heat-denatured myosin and looser myofibrils accelerated the temperature rise. More immobilized water restricted to myofibrils and moisture captured in the gel network promoted water retention. UPA treatment could be a promising technology to tenderize old chicken breast meat.


Assuntos
Alginatos/química , Galinhas , Produtos Avícolas , Animais , Dicroísmo Circular , Culinária , Fibras na Dieta/análise , Indústria de Processamento de Alimentos/métodos , Miofibrilas/química , Miofibrilas/ultraestrutura , Miosinas/química , Proteínas de Aves Domésticas/química , Ultrassom , Água/análise
6.
Food Chem ; 329: 127032, 2020 Nov 01.
Artigo em Inglês | MEDLINE | ID: mdl-32505986

RESUMO

In this work, the effect of oxidation induced by hydroxyl radicals on the binding abilities of myofibrillar protein (MP) gels to aldehydes and ketones and their relationship with MP gel properties were investigated. Mild oxidation (0-0.2 mM H2O2) could induce partial unfolding of MP, thus slightly increasing the salt solubility of MP and enhancing the hardness of MP gels. MP suffering a higher oxidative attack could undergo a reduction in water-holding capacity, with increased mobility of water in MP gels. Oxidation could make MP gel more disordered. The ability of oxidised MP gels to bind to flavours decreased as the carbon chain length of the flavour compound increased. MP oxidation only significantly affected the binding of MP gels to hexanal, heptanal, and 2-octanone, while other flavour compounds were not affected.


Assuntos
Aromatizantes/química , Proteínas Musculares/química , Miofibrilas/química , Animais , Géis/química , Peróxido de Hidrogênio/química , Oxirredução , Solubilidade , Suínos
7.
Nat Commun ; 11(1): 2699, 2020 06 01.
Artigo em Inglês | MEDLINE | ID: mdl-32483185

RESUMO

Nebulin is a giant protein that winds around the actin filaments in the skeletal muscle sarcomere. Compound-heterozygous mutations in the nebulin gene (NEB) cause typical nemaline myopathy (NM), a muscle disorder characterized by muscle weakness with limited treatment options. We created a mouse model with a missense mutation p.Ser6366Ile and a deletion of NEB exon 55, the Compound-Het model that resembles typical NM. We show that Compound-Het mice are growth-retarded and have muscle weakness. Muscles have a reduced myofibrillar fractional-area and sarcomeres are disorganized, contain rod bodies, and have longer thin filaments. In contrast to nebulin-based severe NM where haplo-insufficiency is the disease driver, Compound-Het mice express normal amounts of nebulin. X-ray diffraction revealed that the actin filament is twisted with a larger radius, that tropomyosin and troponin behavior is altered, and that the myofilament spacing is increased. The unique disease mechanism of nebulin-based typical NM reveals novel therapeutic targets.


Assuntos
Proteínas Musculares/genética , Mutação de Sentido Incorreto , Miofibrilas/metabolismo , Miopatias da Nemalina/genética , Citoesqueleto de Actina/química , Citoesqueleto de Actina/metabolismo , Animais , Heterozigoto , Camundongos da Linhagem 129 , Camundongos Endogâmicos C57BL , Microscopia Eletrônica de Transmissão , Proteínas Musculares/química , Proteínas Musculares/metabolismo , Músculo Esquelético/metabolismo , Músculo Esquelético/patologia , Músculo Esquelético/ultraestrutura , Miofibrilas/patologia , Miofibrilas/ultraestrutura , Miopatias da Nemalina/metabolismo , Sarcômeros/metabolismo , Sarcômeros/patologia , Sarcômeros/ultraestrutura , Tropomiosina/química , Tropomiosina/metabolismo , Troponina/química , Troponina/metabolismo , Difração de Raios X
8.
PLoS One ; 15(5): e0227720, 2020.
Artigo em Inglês | MEDLINE | ID: mdl-32407314

RESUMO

Numerous mutational studies have demonstrated that circadian clock proteins regulate behavior and metabolism. Nr1d1(Rev-erbα) is a key regulator of circadian gene expression and a pleiotropic regulator of skeletal muscle homeostasis and lipid metabolism. Loss of Rev-erbα expression induces muscular atrophy, high adiposity, and metabolic syndrome in mice. Here we show that, unlike knockout mice, Nr1d1 heterozygous mice are not susceptible to muscular atrophy and in fact paradoxically possess larger myofiber diameters and improved neuromuscular function, compared to wildtype mice. Heterozygous mice lacked dyslipidemia, a characteristic of Nr1d1 knockout mice and displayed increased whole-body fatty-acid oxidation during periods of inactivity (light cycle). Heterozygous mice also exhibited higher rates of glucose uptake when fasted, and had elevated basal rates of gluconeogenesis compared to wildtype and knockout littermates. Rev-erbα ablation suppressed glycolysis and fatty acid-oxidation in white-adipose tissue (WAT), whereas partial Rev-erbα loss, curiously stimulated these processes. Our investigations revealed that Rev-erbα dose-dependently regulates glucose metabolism and fatty acid oxidation in WAT and muscle.


Assuntos
Dislipidemias/genética , Músculo Esquelético/metabolismo , Atrofia Muscular/genética , Membro 1 do Grupo D da Subfamília 1 de Receptores Nucleares/genética , Tecido Adiposo Branco/metabolismo , Adiposidade/genética , Animais , Comportamento Animal/fisiologia , Relógios Circadianos/genética , Dislipidemias/metabolismo , Dislipidemias/patologia , Ácidos Graxos/metabolismo , Gluconeogênese/genética , Glucose/metabolismo , Heterozigoto , Humanos , Metabolismo dos Lipídeos/genética , Síndrome Metabólica/genética , Síndrome Metabólica/metabolismo , Síndrome Metabólica/patologia , Camundongos , Camundongos Knockout , Atrofia Muscular/metabolismo , Atrofia Muscular/patologia , Miofibrilas/genética , Miofibrilas/metabolismo , Miofibrilas/patologia , Fotoperíodo
9.
Food Chem ; 326: 126896, 2020 Oct 01.
Artigo em Inglês | MEDLINE | ID: mdl-32416422

RESUMO

This study investigated the combined effects of low frequency magnetic field (LF-MF) (3.8 mT) and pH (5-7) on pork myofibrillar protein (MP) gel quality. With LF-MF applying, the water ratio and migration rate both changed to varying extents. LF-MF modified secondary structure of MP by exposing tryptophan and tyrosine residues to participate in hydrogen bonding with water, as well changing α-helix and ß-sheet to varying extents; LF-MF also drove molecular rearrangement and crosslinking. LF-MF brought gel larger and more ordered network to trap more water. And the water holding capacity of gels significantly increased by 2.50% and 2.47% when LF-MF involved at appropriate pH (pH 6.5 and 7.0). Collectively, our results support an optimum treatment (pH 6.5 or 7.0 with applying LF-MF) for the improvement in gel quality of pork MP, and the combination of physical and chemical treatments casts a new light into improving product quality during meat processing.


Assuntos
Proteínas Musculares/química , Miofibrilas/química , Animais , Géis/química , Ligação de Hidrogênio , Concentração de Íons de Hidrogênio , Campos Magnéticos , Imagem por Ressonância Magnética , Espectroscopia de Ressonância Magnética , Carne de Porco , Estrutura Secundária de Proteína , Análise Espectral Raman , Suínos
10.
Food Chem ; 321: 126728, 2020 Aug 15.
Artigo em Inglês | MEDLINE | ID: mdl-32259736

RESUMO

The effects of low-frequency magnetic field combined with different heating rates on pork myofibrillar protein (MP) gels were investigated. Samples were treated under different heating rates (1 °C/min and 2 °C/min) in the presence or absence of 9.5 mT low-frequency magnetic field. The highest levels of intermolecular and intramolecular ionic and hydrogen bonds in MP were observed at the heating rate of 2 °C/min under the 9.5 mT magnetic field. These bonds resulted in decreasing the α-helix and increasing the ß-sheet and ß-turn, which promoted the formation of a more uniform microstructure. It also increased the proportion of bound water, increasing the ability of MP to bind with water. This effect, combined with the weaker hydrophobic interactions, as confirmed by the reduced content of tryptophan and aliphatic residues, explained well the high water-holding capacity of MP induced by heating at 2 °C/min under the 9.5 mT magnetic field.


Assuntos
Géis/química , Campos Magnéticos , Proteínas Musculares/química , Miofibrilas/química , Carne de Porco , Animais , Calefação , Ligação de Hidrogênio , Interações Hidrofóbicas e Hidrofílicas , Reologia , Água/química
11.
Food Chem ; 319: 126535, 2020 Jul 30.
Artigo em Inglês | MEDLINE | ID: mdl-32187565

RESUMO

The improvement mechanism of high pressure processing (HPP, 100-300 MPa, 10 min) on the gelation properties of reduced-sodium (0.3 M sodium chloride) myofibrillar protein containing 20 mM CaCl2 (MP-Ca) were explored. The results showed that the water holding capacity (WHC) and strength of MP-Ca gel reached the maximum values under 200 MPa. This was attributed to substantial solubilization of myosin heavy chain and actin, a decreased protein aggregation ability and the exposure of both tyrosine and tryptophan residues resulting from the unfolding of the protein tertiary structure. However, 300 MPa induced the hydrophobic rearrangement of MP and the disulfide cross-linking of the myosin S-1 subfragment, leading to the formation of large protein aggregates and decreased solubility of MP, thus resulting in a weaker gel with a reduced WHC. Therefore, moderate HPP (approximately 200 MPa) and low concentrations of CaCl2 could potentially improve the gelation properties of reduced-sodium meat products.


Assuntos
Cloreto de Cálcio/química , Galinhas , Miofibrilas/química , Sódio/química , Actinas/química , Animais , Fenômenos Químicos , Géis/química , Interações Hidrofóbicas e Hidrofílicas , Pressão , Solubilidade , Água/química
12.
Food Chem ; 319: 126571, 2020 Jul 30.
Artigo em Inglês | MEDLINE | ID: mdl-32169769

RESUMO

This study aims to investigate the changes in mitochondrial apoptotic factors and proteolysis of two porcine muscles (psoas major - PM and longissimus dorsi - LD) during aging. Results found that during 2-168 h postmortem mitochondrial membrane permeability, mitochondrial lipid peroxidation, Ca2+ levels were increased, while the reduction level and abundance of cytochrome c were decreased (P < 0.05) in both muscle types. Furthermore, the activation of caspase-3 along with increases in troponin-T and desmin degradation, and µ-calpain autolysis were found (P < 0.05), regardless of muscle type. PM maintained higher mitochondrial apoptotic factors, but had more intact desmin, less troponin-T degradation and less extent of autolyzed products of µ-calpain compared to LD (P < 0.05). These results indicate that the rapid onset of mitochondrial apoptosis of PM would not lead to a subsequent impact on myofibrillar protein degradation, suggesting that the mitochondrial apoptosis mediated tenderization process could be muscle-specific.


Assuntos
Apoptose , Mitocôndrias/metabolismo , Músculo Esquelético/metabolismo , Carne Vermelha , Animais , Autólise/metabolismo , Calpaína/metabolismo , Desmina/metabolismo , Miofibrilas/metabolismo , Proteólise , Suínos , Fatores de Tempo , Troponina T/metabolismo
13.
PLoS Comput Biol ; 16(3): e1007676, 2020 03.
Artigo em Inglês | MEDLINE | ID: mdl-32130207

RESUMO

As sarcomeres produce the force necessary for contraction, assessment of sarcomere order is paramount in evaluation of cardiac and skeletal myocytes. The uniaxial force produced by sarcomeres is ideally perpendicular to their z-lines, which couple parallel myofibrils and give cardiac and skeletal myocytes their distinct striated appearance. Accordingly, sarcomere structure is often evaluated by staining for z-line proteins such as α-actinin. However, due to limitations of current analysis methods, which require manual or semi-manual handling of images, the mechanism by which sarcomere and by extension z-line architecture can impact contraction and which characteristics of z-line architecture should be used to assess striated myocytes has not been fully explored. Challenges such as isolating z-lines from regions of off-target staining that occur along immature stress fibers and cell boundaries and choosing metrics to summarize overall z-line architecture have gone largely unaddressed in previous work. While an expert can qualitatively appraise tissues, these challenges leave researchers without robust, repeatable tools to assess z-line architecture across different labs and experiments. Additionally, the criteria used by experts to evaluate sarcomeric architecture have not been well-defined. We address these challenges by providing metrics that summarize different aspects of z-line architecture that correspond to expert tissue quality assessment and demonstrate their efficacy through an examination of engineered tissues and single cells. In doing so, we have elucidated a mechanism by which highly elongated cardiomyocytes become inefficient at producing force. Unlike previous manual or semi-manual methods, characterization of z-line architecture using the metrics discussed and implemented in this work can quantitatively evaluate engineered tissues and contribute to a robust understanding of the development and mechanics of striated muscles.


Assuntos
Processamento de Imagem Assistida por Computador/métodos , Fibras Musculares Esqueléticas , Miócitos Cardíacos , Sarcômeros , Algoritmos , Animais , Células Cultivadas , Humanos , Microscopia de Fluorescência , Fibras Musculares Esqueléticas/química , Fibras Musculares Esqueléticas/ultraestrutura , Músculo Esquelético/citologia , Miócitos Cardíacos/citologia , Miócitos Cardíacos/ultraestrutura , Miofibrilas/fisiologia , Ratos , Ratos Sprague-Dawley , Sarcômeros/química , Sarcômeros/ultraestrutura
14.
Food Chem ; 315: 126226, 2020 Jun 15.
Artigo em Inglês | MEDLINE | ID: mdl-32018081

RESUMO

The aim of this study was to investigate the effects of oxidation on the structure of pork myofibrillar proteins (MPs) and the water retention mechanism of MPs gel. In a Fenton reaction system, protein oxidation increases (P < 0.05) with hydrogen peroxide (H2O2) concentration (0, 0.5, 1, 3, 5, 10, and 20 mmol/L). The Brunauer-Emmett-Teller surface area of the proteins gel gradually increased (P < 0.05) from 6.17 m2/g to 14.73 m2/g. Low field nuclear magnetic resonance results showed that immobilized water in the gel gradually decreased but free water content gradually increased (P < 0.05). Gel strength and water holding capacity (WHC) increased and then decreased. The results reveal that moderate oxidation contributes to the compact and uniform pore structure, higher WHC of proteins gel as well. However, excessive oxidation leads to increase pores and changes in water states of gel, leading to lower WHC.


Assuntos
Proteínas Musculares/metabolismo , Músculos/metabolismo , Miofibrilas/metabolismo , Carne Vermelha/análise , Água/química , Animais , Géis/química , Peróxido de Hidrogênio/química , Interações Hidrofóbicas e Hidrofílicas , Proteínas Musculares/química , Músculos/química , Miofibrilas/química , Oxirredução , Suínos
15.
J Food Sci ; 85(3): 682-688, 2020 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-31999363

RESUMO

The aim of this study was to evaluate the effect of µ-calpain oxidation on Coregonus peled myofibrillar protein degradation. In the present study, a hydroxyl radical oxidation system was selected to investigate oxidative modification on µ-calpain activity and its degradation on C. peled myofibrillar protein. When subjected to oxidation, the carbonyl content of µ-calpain significantly increased with the increasing of oxidation levels, and oxidation modification promoted the µ-calpain activity. Incubation of C. peled myofibrillar protein with oxidized µ-calpain resulted in the enhanced degradation of myosin heavy chains, actin, and troponin T, but the degradation of desmin at higher levels of oxidation was slightly inhibited, based on sodium dodecyl sulfate polyacrylamide gel electrophoresis and western blotting. This study suggests that oxidation treatment of µ-calpain could accelerate myofibrillar proteolysis through regulating the enzyme activity during postmortem aging. PRACTICAL APPLICATION: Endogenous proteases, especially µ-calpain, are reported to be involved in fish softening during early postmortem storage, which is critical to muscle quality. The cysteine residues of proteins are particularly sensitive to oxidation. The investigation of the effect of oxidation on µ-calpain (a cysteine protease) activity allows for the monitoring of its role in the postmortem proteolysis of fish myofibrils and the associated softening of fish meat, in an attempt to minimize this softening.


Assuntos
Calpaína/química , Proteínas de Peixes/química , Carne/análise , Miofibrilas/química , Animais , Eletroforese em Gel de Poliacrilamida , Músculo Esquelético/química , Oxirredução , Mudanças Depois da Morte , Proteólise , Salmonidae
16.
Am J Physiol Endocrinol Metab ; 318(2): E117-E130, 2020 02 01.
Artigo em Inglês | MEDLINE | ID: mdl-31743039

RESUMO

Short-term muscle disuse has been reported to lower both postabsorptive and postprandial myofibrillar protein synthesis rates. This study assessed the impact of disuse on daily myofibrillar protein synthesis rates following short-term (2 and 7 days) muscle disuse under free living conditions. Thirteen healthy young men (age: 20 ± 1 yr; BMI: 23 ± 1 kg/m-2) underwent 7 days of unilateral leg immobilization via a knee brace, with the nonimmobilized leg acting as a control. Four days before immobilization participants ingested 400 mL of 70% deuterated water, with 50-mL doses consumed daily thereafter. Upper leg bilateral MRI scans and muscle biopsies were collected before and after 2 and 7 days of immobilization to determine quadriceps volume and daily myofibrillar protein synthesis rates. Immobilization reduced quadriceps volume in the immobilized leg by 1.7 ± 0.3 and 6.7 ± 0.6% after 2 and 7 days, respectively, with no changes in the control leg. Over the 1-wk immobilization period, myofibrillar protein synthesis rates were 36 ± 4% lower in the immobilized (0.81 ± 0.04%/day) compared with the control (1.26 ± 0.04%/day) leg (P < 0.001). Myofibrillar protein synthesis rates in the control leg did not change over time (P = 0.775), but in the immobilized leg they were numerically lower during the 0- to 2-day period (16 ± 6%, 1.11 ± 0.09%/day, P = 0.153) and were significantly lower during the 2- to 7-day period (44 ± 5%, 0.70 ± 0.06%/day, P < 0.001) when compared with the control leg. We conclude that 1 wk of muscle disuse induces a rapid and sustained decline in daily myofibrillar protein synthesis rates in healthy young men.


Assuntos
Proteínas Musculares/biossíntese , Músculo Esquelético/metabolismo , Atrofia Muscular/metabolismo , Miofibrilas/metabolismo , Água Corporal/metabolismo , Dieta , Exercício Físico , Expressão Gênica , Voluntários Saudáveis , Humanos , Imobilização , Cinética , Perna (Membro) , Imagem por Ressonância Magnética , Masculino , Proteínas Musculares/genética , Força Muscular , Músculo Esquelético/diagnóstico por imagem , Atrofia Muscular/diagnóstico por imagem , Músculo Quadríceps/diagnóstico por imagem , Músculo Quadríceps/metabolismo , Adulto Jovem
17.
Am J Physiol Cell Physiol ; 318(1): C103-C110, 2020 01 01.
Artigo em Inglês | MEDLINE | ID: mdl-31618078

RESUMO

In the present study we evaluated the load dependence of force produced by isolated muscle myosin filaments interacting with fluorescently labeled actin filaments, using for the first time whole native myosin filaments. We used a newly developed approach that allowed the use of physiological levels of ATP. Single filaments composed of either skeletal or smooth muscle myosin and single filaments of actin were attached between pairs of nano-fabricated cantilevers of known stiffness. The filaments were brought into contact to produce force, which caused sliding of the actin filaments over the myosin filaments. We applied load to the system by either pushing or pulling the filaments during interactions and observed that increasing the load increased the force produced by myosin and decreasing the load decreased the force. We also performed additional experiments in which we clamped the filaments at predetermined levels of force, which caused the filaments to slide to adjust the different loads, allowing us to measure the velocity of length changes to construct a force-velocity relation. Force values were in the range observed previously with myosin filaments and molecules. The force-velocity curves for skeletal and smooth muscle myosins resembled the relations observed for muscle fibers. The technique can be used to investigate many issues of interest and debate in the field of muscle biophysics.


Assuntos
Citoesqueleto de Actina/fisiologia , Contração Muscular , Força Muscular , Músculo Liso/fisiologia , Miofibrilas/fisiologia , Miosinas/fisiologia , Músculos Psoas/fisiologia , Citoesqueleto de Actina/metabolismo , Trifosfato de Adenosina/metabolismo , Animais , Feminino , Músculo Liso/metabolismo , Miofibrilas/metabolismo , Miosinas/metabolismo , Mytilus edulis , Músculos Psoas/metabolismo , Coelhos , Fatores de Tempo
18.
J Sci Food Agric ; 100(3): 1195-1203, 2020 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-31721226

RESUMO

BACKGROUND: The present study investigated the effect of two-step heat treatments on the structure of grass carp myofibrillar proteins (MPs) and their binding ability for selected aldehydes (hexanal, heptanal, octanal and nonanal). RESULTS: Within 30 min of the first heating step at 40 °C and 5-10 min of the second heating step at 90 °C, the enhancement of the flavor-binding ability was likely explained by the increases in surface hydrophobicity and total sulfhydryl content due to the unfolding of secondary structures of MPs through exposure of hydrophobic amino acids and sulfhydryl groups. Nevertheless, lengthy heating at 90 °C accelerated the aggregation of unfolded MPs and reduced the hydrophobic bonding sites, thus weakening the hydrophobic interactions and decreasing the resultant binding ability of MPs with aldehydes. CONCLUSION: The binding ability of aldehydes to MPs was found to be strongly influenced by changes in protein structure and surface during the two-step heating process. The results provided insight into improving the flavor characteristics of freshwater fish surimi products. © 2019 Society of Chemical Industry.


Assuntos
Aldeídos/análise , Produtos Pesqueiros/análise , Proteínas de Peixes/química , Miofibrilas/química , Animais , Carpas , Aromatizantes/química , Temperatura Alta , Interações Hidrofóbicas e Hidrofílicas , Estrutura Secundária de Proteína
19.
Food Chem ; 308: 125576, 2020 Mar 05.
Artigo em Inglês | MEDLINE | ID: mdl-31648092

RESUMO

This study investigated the effects of cold storage at different temperatures (4, -0.5, -3, and -20 °C) on protein degradation and its relationship to structural changes of black carp muscle. At -0.5 and 4 °C, major structural changes occurred, including the formation of gaps between myofibers and myofibrils, breakage of myofibrils and myofibers, and degradation of sarcoplasmic reticulum. Gel-based proteomic analysis showed that these structural changes were accompanied by degradation of a series of myofibrillar proteins, including titin, nebulin, troponin, myosin, myomesin, myosin-binding protein, and α-actinin. Loss of extractable gelatinolytic and caseinolytic protease activities was also observed. At -3 and -20 °C, formation of ice crystals was the most noticeable change. The major proteins were degraded at different locations in the black carp muscle, and gelatinolytic and caseinolytic proteases appear to contribute to the degradation of those proteins.


Assuntos
Carpas/metabolismo , Actinina/metabolismo , Animais , Proteínas de Transporte , Temperatura Baixa , Conectina/metabolismo , Cyprinidae/metabolismo , Proteínas Musculares/metabolismo , Miofibrilas/metabolismo , Miosinas/metabolismo , Proteólise , Proteômica
20.
Am J Physiol Cell Physiol ; 318(2): C422-C429, 2020 02 01.
Artigo em Inglês | MEDLINE | ID: mdl-31875694

RESUMO

Aerobic exercise capacity is critical to bodily health. As a model to investigate the mechanisms that determine health and disease, we employed low (LCR) and high (HCR) capacity running rat models selectively bred to concentrate the genes responsible for divergent aerobic running capacity. To investigate the skeletal muscle contribution to this innate difference in running capacity we employed an approach combining examination of the myofilament protein composition and contractile properties of the fast fiber extensor digitorum longus (EDL) and slow fiber soleus (SOL) muscles from LCR and HCR rats. Intact muscle force experiments demonstrate that SOL, but not EDL, muscles from LCR rats exhibit a three times greater decrease in fatigued force. To investigate the mechanism of this increased fatigability in the LCR SOL muscle, we determined the myofilament protein composition and functional properties. Force-Ca2+ measurements demonstrate decreased Ca2+ sensitivity of single skinned SOL muscle fibers from LCR compared with that of HCR rats. Segregating SOL fibers into fast and slow types demonstrates that the decreased Ca2+ sensitivity in LCR SOL results from a specific decrease in slow-type SOL fiber Ca2+ sensitivity such that it was similar to that of fast-type fibers. These results identify that the altered myofilament contractile properties of LCR SOL slow-type fibers result in a fast muscle type Ca2+ sensitivity and the LCR muscle phenotype. Overall our findings demonstrate alterations of the myofilament proteins could contribute to fatigability of the SOL muscle and the decreased innate aerobic running performance of LCR compared with HCR rats.


Assuntos
Tolerância ao Exercício/fisiologia , Fibras Musculares de Contração Rápida/fisiologia , Fibras Musculares de Contração Lenta/fisiologia , Miofibrilas/fisiologia , Condicionamento Físico Animal/fisiologia , Animais , Cálcio/metabolismo , Feminino , Masculino , Contração Muscular/fisiologia , Fibras Musculares de Contração Rápida/metabolismo , Fibras Musculares de Contração Lenta/metabolismo , Miofibrilas/metabolismo , Ratos , Corrida/fisiologia
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