Journal articles on the topic 'Muscle proteins'
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1
Hooper, Scott L., and Jeffrey B. Thuma. "Invertebrate Muscles: Muscle Specific Genes and Proteins." Physiological Reviews 85, no. 3 (July 2005): 1001–60. http://dx.doi.org/10.1152/physrev.00019.2004.
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This is the first of a projected series of canonic reviews covering all invertebrate muscle literature prior to 2005 and covers muscle genes and proteins except those involved in excitation-contraction coupling (e.g., the ryanodine receptor) and those forming ligand- and voltage-dependent channels. Two themes are of primary importance. The first is the evolutionary antiquity of muscle proteins. Actin, myosin, and tropomyosin (at least, the presence of other muscle proteins in these organisms has not been examined) exist in muscle-like cells in Radiata, and almost all muscle proteins are present across Bilateria, implying that the first Bilaterian had a complete, or near-complete, complement of present-day muscle proteins. The second is the extraordinary diversity of protein isoforms and genetic mechanisms for producing them. This rich diversity suggests that studying invertebrate muscle proteins and genes can be usefully applied to resolve phylogenetic relationships and to understand protein assembly coevolution. Fully achieving these goals, however, will require examination of a much broader range of species than has been heretofore performed.
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Sansom, Clare. "Modelling muscle proteins." Biochemist 34, no. 3 (June 1, 2012): 50–51. http://dx.doi.org/10.1042/bio03403050.
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Holmes, Kenneth C., and Wolfgang Kabsch. "Muscle proteins: actin." Current Opinion in Structural Biology 1, no. 2 (April 1991): 270–80. http://dx.doi.org/10.1016/0959-440x(91)90073-3.
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Majerczak, Joanna, Agnieszka Kij, Hanna Drzymala-Celichowska, Kamil Kus, Janusz Karasinski, Zenon Nieckarz, Marcin Grandys, et al. "Nitrite Concentration in the Striated Muscles Is Reversely Related to Myoglobin and Mitochondrial Proteins Content in Rats." International Journal of Molecular Sciences 23, no. 5 (February 28, 2022): 2686. http://dx.doi.org/10.3390/ijms23052686.
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Skeletal muscles are an important reservoir of nitric oxide (NO•) stored in the form of nitrite [NO2−] and nitrate [NO3−] (NOx). Nitrite, which can be reduced to NO• under hypoxic and acidotic conditions, is considered a physiologically relevant, direct source of bioactive NO•. The aim of the present study was to determine the basal levels of NOx in striated muscles (including rat heart and locomotory muscles) with varied contents of tissue nitrite reductases, such as myoglobin and mitochondrial electron transport chain proteins (ETC-proteins). Muscle NOx was determined using a high-performance liquid chromatography-based method. Muscle proteins were evaluated using western-immunoblotting. We found that oxidative muscles with a higher content of ETC-proteins and myoglobin (such as the heart and slow-twitch locomotory muscles) have lower [NO2−] compared to fast-twitch muscles with a lower content of those proteins. The muscle type had no observed effect on the [NO3−]. Our results demonstrated that fast-twitch muscles possess greater potential to generate NO• via nitrite reduction than slow-twitch muscles and the heart. This property might be of special importance for fast skeletal muscles during strenuous exercise and/or hypoxia since it might support muscle blood flow via additional NO• provision (acidic/hypoxic vasodilation) and delay muscle fatigue.
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Norheim, Frode, Truls Raastad, Bernd Thiede, Arild C. Rustan, Christian A. Drevon, and Fred Haugen. "Proteomic identification of secreted proteins from human skeletal muscle cells and expression in response to strength training." American Journal of Physiology-Endocrinology and Metabolism 301, no. 5 (November 2011): E1013—E1021. http://dx.doi.org/10.1152/ajpendo.00326.2011.
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Regular physical activity protects against several types of diseases. This may involve altered secretion of signaling proteins from skeletal muscle. Our aim was to identify the most abundantly secreted proteins in cultures of human skeletal muscle cells and to monitor their expression in muscles of strength-training individuals. A total of 236 proteins were detected by proteome analysis in medium conditioned by cultured human myotubes, which was narrowed down to identification of 18 classically secreted proteins expressed in skeletal muscle, using the SignalP 3.0 and Human Genome Expression Profile databases together with a published mRNA-based reconstruction of the human skeletal muscle secretome. For 17 of the secreted proteins, expression was confirmed at the mRNA level in cultured human myotubes as well as in biopsies of human skeletal muscles. RT-PCR analyses showed that 15 of the secreted muscle proteins had significantly enhanced mRNA expression in m. vastus lateralis and/or m. trapezius after 11 wk of strength training among healthy volunteers. For example, secreted protein acidic and rich in cysteine, a secretory protein in the membrane fraction of skeletal muscle fibers, was increased 3- and 10-fold in m. vastus lateralis and m. trapezius, respectively. Identification of proteins secreted by skeletal muscle cells in vitro facilitated the discovery of novel responses in skeletal muscles of strength-training individuals.
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Xie, Yuchun, Nai Rile, Xuewu Li, Haijun Li, Meng Zhao, Tianyu Che, Ting Cai, Zhihong Liu, and Jinquan Li. "Analysis of cashmere goat meat by label-free proteomics shows that MYL3 is a potential molecular marker of meat toughness." Czech Journal of Animal Science 67, No. 4 (April 30, 2022): 137–46. http://dx.doi.org/10.17221/61/2021-cjas.
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The Inner Mongolia cashmere goat is famous for its bright white cashmere fibre. However, little attention is given to the excellent characteristics of this breed’s meat. We used label-free proteomics to analyse the total protein content in five different muscles, and 1 227 proteins were detected. Through sequential windowed acquisition of all theoretical fragment ions (SWATH), 16, 33, 49, 39, and 31 differentially expressed proteins were successfully detected in the five muscles. Protein–protein interaction network analysis of differentially expressed proteins revealed many strong interactions related to fatty acid beta oxidation and muscle development. Based on SWATH in five muscles, 25 differentially expressed proteins related to muscle development were detected, including seven muscle fibre structural proteins (ACTG2, ACTN4, TAGLN, MYL3, MYL1, MYL6B and MYH4). Finally, immunohistochemical analysis of MYL3 showed that the proportion of MYL3 may be a potential molecular marker for muscle toughness.
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Bezakova, Gabriela, and Terje Lømo. "Muscle Activity and Muscle Agrin Regulate the Organization of Cytoskeletal Proteins and Attached Acetylcholine Receptor (Achr) Aggregates in Skeletal Muscle Fibers." Journal of Cell Biology 153, no. 7 (June 25, 2001): 1453–64. http://dx.doi.org/10.1083/jcb.153.7.1453.
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In innervated skeletal muscle fibers, dystrophin and β-dystroglycan form rib-like structures (costameres) that appear as predominantly transverse stripes over Z and M lines. Here, we show that the orientation of these stripes becomes longitudinal in denervated muscles and transverse again in denervated electrically stimulated muscles. Skeletal muscle fibers express nonneural (muscle) agrin whose function is not well understood. In this work, a single application of ≥10 nM purified recombinant muscle agrin into denervated muscles preserved the transverse orientation of costameric proteins that is typical for innervated muscles, as did a single application of ≥1 μM neural agrin. At lower concentration, neural agrin induced acetylcholine receptor aggregates, which colocalized with longitudinally oriented β-dystroglycan, dystrophin, utrophin, syntrophin, rapsyn, and β2-laminin in denervated unstimulated fibers and with the same but transversely oriented proteins in innervated or denervated stimulated fibers. The results indicate that costameres are plastic structures whose organization depends on electrical muscle activity and/or muscle agrin.
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Ferreira, Jorge. "Gravity alters muscle proteins." Lab Animal 52, no. 11 (October 27, 2023): 266. http://dx.doi.org/10.1038/s41684-023-01281-3.
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Picard, Brigitte, Mohammed Gagaoua, Marwa Al-Jammas, Leanne De Koning, Albéric Valais, and Muriel Bonnet. "Beef tenderness and intramuscular fat proteomic biomarkers: muscle type effect." PeerJ 6 (June 7, 2018): e4891. http://dx.doi.org/10.7717/peerj.4891.
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Tenderness and intramuscular fat content are key attributes for beef sensory qualities. Recently some proteomic analysis revealed several proteins which are considered as good biomarkers of these quality traits. This study focuses on the analysis of 20 of these proteins representative of several biological functions: muscle structure and ultrastructure, muscle energetic metabolism, cellular stress and apoptosis. The relative abundance of the proteins was measured by Reverse Phase Protein Array (RPPA) in five muscles known to have different tenderness and intramuscular lipid contents: Longissimus thoracis (LT), Semimembranosus (SM), Rectus abdominis (RA), Triceps brachii (TB) and Semitendinosus (ST). The main results showed a muscle type effect on 16 among the 20 analyzed proteins. They revealed differences in protein abundance depending on the contractile and metabolic properties of the muscles. The RA muscle was the most different by 11 proteins differentially abundant comparatively to the four other muscles. Among these 11 proteins, six were less abundant namely enolase 3 (ENO3), phosphoglucomutase 1 (PGK1), aldolase (ALDOA), myosin heavy chain IIX (MyHC-IIX), fast myosin light chain 1 (MLC1F), triosephosphate isomerase 1 (TPI1) and five more abundant: Heat shock protein (HSP27, HSP70-1A1, αB-crystallin (CRYAB), troponin T slow (TNNT1), and aldolase dehydrogenase 1 (ALDH1A1). Four proteins: HSP40, four and a half LIM domains protein 1 (FHL1), glycogen phosphorylase B (PYGB) and malate dehydrogenase (MDH1) showed the same abundance whatever the muscle. The correlations observed between the 20 proteins in all the five muscles were used to construct a correlation network. The proteins the most connected with the others were in the following order MyHC-IIX, CRYAB, TPI1, PGK1, ALDH1A1, HSP27 and TNNT1. This knowledge is important for understanding the biological functions related to beef tenderness and intramuscular fat content.
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Amirouche, Adel, Vanessa E. Jahnke, John A. Lunde, Nathalie Koulmann, Damien G. Freyssenet, and Bernard J. Jasmin. "Muscle-specific microRNA-206 targets multiple components in dystrophic skeletal muscle representing beneficial adaptations." American Journal of Physiology-Cell Physiology 312, no. 3 (March 1, 2017): C209—C221. http://dx.doi.org/10.1152/ajpcell.00185.2016.
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Over the last several years, converging lines of evidence have indicated that miR-206 plays a pivotal role in promoting muscle differentiation and regeneration, thereby potentially impacting positively on the progression of neuromuscular disorders, including Duchenne muscular dystrophy (DMD). Despite several studies showing the regulatory function of miR-206 on target mRNAs in skeletal muscle cells, the effects of overexpression of miR-206 in dystrophic muscles remain to be established. Here, we found that miR-206 overexpression in mdx mouse muscles simultaneously targets multiple mRNAs and proteins implicated in satellite cell differentiation, muscle regeneration, and at the neuromuscular junction. Overexpression of miR-206 also increased the levels of several muscle-specific mRNAs/proteins, while enhancing utrophin A expression at the sarcolemma. Finally, we also observed that the increased expression of miR-206 in dystrophin-deficient mouse muscle decreased the production of proinflammatory cytokines and infiltration of macrophages. Taken together, our results show that miR-206 acts as a pleiotropic regulator that targets multiple key mRNAs and proteins expected to provide beneficial adaptations in dystrophic muscle, thus highlighting its therapeutic potential for DMD.
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Tan, Xiaofan, Yu He, Yuqiao He, Zhiwei Yan, Jing Chen, Ruixue Zhao, Xin Sui, et al. "Comparative Proteomic Analysis of Glycolytic and Oxidative Muscle in Pigs." Genes 14, no. 2 (January 30, 2023): 361. http://dx.doi.org/10.3390/genes14020361.
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The quality of meat is highly correlated with muscle fiber type. However, the mechanisms via which proteins regulate muscle fiber types in pigs are not entirely understood. In the current study, we have performed proteomic profiling of fast/glycolytic biceps femoris (BF) and slow/oxidative soleus (SOL) muscles and identified several candidate differential proteins among these. We performed proteomic analyses based on tandem mass tags (TMTs) and identified a total of 26,228 peptides corresponding to 2667 proteins among the BF and SOL muscle samples. Among these, we found 204 differentially expressed proteins (DEPs) between BF and SOL muscle, with 56 up-regulated and 148 down-regulated DEPs in SOL muscle samples. KEGG and GO enrichment analyses of the DEPs revealed that the DEPs are involved in some GO terms (e.g., actin cytoskeleton, myosin complex, and cytoskeletal parts) and signaling pathways (PI3K-Akt and NF-kappa B signaling pathways) that influence muscle fiber type. A regulatory network of protein–protein interaction (PPI) between these DEPs that regulates muscle fiber types was constructed, which demonstrates how three down-regulated DEPs, including PFKM, GAPDH, and PKM, interact with other proteins to potentially control the glycolytic process. This study offers a new understanding of the molecular mechanisms in glycolytic and oxidative muscles as well as a novel approach for enhancing meat quality by transforming the type of muscle fibers in pigs.
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Blondelle, Jordan, Andrea Biju, and Stephan Lange. "The Role of Cullin-RING Ligases in Striated Muscle Development, Function, and Disease." International Journal of Molecular Sciences 21, no. 21 (October 26, 2020): 7936. http://dx.doi.org/10.3390/ijms21217936.
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The well-orchestrated turnover of proteins in cross-striated muscles is one of the fundamental processes required for muscle cell function and survival. Dysfunction of the intricate protein degradation machinery is often associated with development of cardiac and skeletal muscle myopathies. Most muscle proteins are degraded by the ubiquitin–proteasome system (UPS). The UPS involves a number of enzymes, including E3-ligases, which tightly control which protein substrates are marked for degradation by the proteasome. Recent data reveal that E3-ligases of the cullin family play more diverse and crucial roles in cross striated muscles than previously anticipated. This review highlights some of the findings on the multifaceted functions of cullin-RING E3-ligases, their substrate adapters, muscle protein substrates, and regulatory proteins, such as the Cop9 signalosome, for the development of cross striated muscles, and their roles in the etiology of myopathies.
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Clarkson, Priscilla M., and Stephen P. Sayers. "Etiology of Exercise-Induced Muscle Damage." Canadian Journal of Applied Physiology 24, no. 3 (June 1, 1999): 234–48. http://dx.doi.org/10.1139/h99-020.
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Muscle damage is caused by strenuous and unaccustomed exercise, especially exercise involving eccentric muscle contractions, where muscles lengthen as they exert force. Damage can be observed both directly at the cellular level and indirectly from changes in various indices of muscle function. Several mechanisms have been offered to explain the etiology of the damage/repair process, including mechanical factors such as tension and strain, disturbances in calcium homeostasis. the inflammatory response, and the synthesis of stress proteins (heat shock proteins). Changes in muscle function following eccentric exercise have been observed at the cellular level as an impairment in the amount and action of transport proteins for glucose and lactate/H+, and at the systems level as an increase in muscle stiffness and a prolonged loss in the muscle's ability to generate force. This paper will briefly review factors involved in the damage/repair process and alterations in muscle function following eccentric exercise. Key words: eccentric exercise, inflammation, stress proteins, muscle function
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Stronach, B. E., S. E. Siegrist, and M. C. Beckerle. "Two muscle-specific LIM proteins in Drosophila." Journal of Cell Biology 134, no. 5 (September 1, 1996): 1179–95. http://dx.doi.org/10.1083/jcb.134.5.1179.
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The LIM domain defines a zinc-binding motif found in a growing number of eukaryotic proteins that regulate cell growth and differentiation during development. Members of the cysteine-rich protein (CRP) family of LIM proteins have been implicated in muscle differentiation in vertebrates. Here we report the identification and characterization of cDNA clones encoding two members of the CRP family in Drosophila, referred to as muscle LIM proteins (Mlp). Mlp60A encodes a protein with a single LIM domain linked to a glycine-rich region. Mlp84B encodes a protein with five tandem LIM-glycine modules. In the embryo, Mlp gene expression is spatially restricted to somatic, visceral, and pharyngeal muscles. Within the somatic musculature, Mlp84B transcripts are enriched at the terminal ends of muscle fibers, whereas Mlp60A transcripts are found throughout the muscle fibers. The distributions of the Mlp60A and Mlp84B proteins mirror their respective mRNA localizations, with Mlp84B enrichment occurring at sites of muscle attachment. Northern blot analysis revealed that Mlp gene expression is developmentally regulated, showing a biphasic pattern over the course of the Drosophila life cycle. Peaks of expression occur late in embryogenesis and during metamorphosis, when the musculature is differentiating. Drosophila Mlp60A and Mlp84B, like vertebrate members of the CRP family, have the ability to associate with the actin cytoskeleton when expressed in rat fibroblast cells. The temporal expression and spatial distribution of muscle LIM proteins in Drosophila are consistent with a role for Mlps in myogenesis, late in the differentiation pathway.
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Dupont-Versteegden, Esther E., Radhakrishnan Nagarajan, Marjorie L. Beggs, Edward D. Bearden, Pippa M. Simpson, and Charlotte A. Peterson. "Identification of cold-shock protein RBM3 as a possible regulator of skeletal muscle size through expression profiling." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 295, no. 4 (October 2008): R1263—R1273. http://dx.doi.org/10.1152/ajpregu.90455.2008.
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Changes in gene expression associated with skeletal muscle atrophy due to aging are distinct from those due to disuse, suggesting that the response of old muscle to inactivity may be altered. The goal of this study was to identify changes in muscle gene expression that may contribute to loss of adaptability of old muscle. Muscle atrophy was induced in young adult (6-mo) and old (32-mo) male Brown Norway/F344 rats by 2 wk of hindlimb suspension (HS), and soleus muscles were analyzed by cDNA microarrays. Overall, similar changes in gene expression with HS were observed in young and old muscles for genes encoding proteins involved in protein folding (heat shock proteins), muscle structure, and contraction, extracellular matrix, and nucleic acid binding. More genes encoding transport and receptor proteins were differentially expressed in the soleus muscle from young rats, while in soleus muscle from old rats more genes that encoded ribosomal proteins were upregulated. The gene encoding the cold-shock protein RNA-binding motif protein-3 (RBM3) was induced most highly with HS in muscle from old rats, verified by real-time RT-PCR, while no difference with age was observed. The cold-inducible RNA-binding protein (Cirp) gene was also overexpressed with HS, whereas cold-shock protein Y-box-binding protein-1 was not. A time course analysis of RBM3 mRNA abundance during HS showed that upregulation occurred after apoptotic nuclei and markers of protein degradation increased. We conclude that a cold-shock response may be part of a compensatory mechanism in muscles undergoing atrophy to preserve remaining muscle mass and that RBM3 may be a therapeutic target to prevent muscle loss.
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Muslimovic, Aida, Vincent Fridén, Karin Starnberg, Olav Tenstad, Heidi Espedal, Kristina Vukusic, Susanne Nyström, et al. "Novel clearance of muscle proteins by muscle cells." European Journal of Cell Biology 99, no. 8 (November 2020): 151127. http://dx.doi.org/10.1016/j.ejcb.2020.151127.
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Akhremko, Anastasia, and Liliya Fedulova. "Comparative study of weaning pigs' muscle proteins using two-dimensional electrophoresis." Potravinarstvo Slovak Journal of Food Sciences 15 (January 28, 2021): 52–57. http://dx.doi.org/10.5219/1449.
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The proteostasis system of animals, including various types of protein modification during the growth stage, leads to an almost incomprehensible number of possible forms of protein, and each can regulate numerous functions. In the presented work, the composition of muscle tissue protein from different portions of piglets was studied to understand the main muscle protein formation. Comparative analysis of weaned piglets' main muscle protein from l. dorsi, biceps femoris, and brachiocephalicus were analyzed using two-dimensional electrophoresis. Changes in the staining intensity of protein fractions inherent in different muscles were revealed. As part of this work, candidate groups of pig muscle proteins have been selected. Eleven protein spots were revealed for the longest muscle of the back, and seven for the biceps; the muscles of the neck are characterized by indicators of low protein fraction volume. Among the proteins found, myosin light chains, phosphoglycerate mutase, troponins, and adenylate kinase is most likely present. The obtained results of protein identification in muscle tissues, obtained during the intensive growth period, will allow a more detailed understanding of protein regulation, function, and interactions in complex biological systems, which will subsequently be significantly important for biomonitoring health and predicting farm animals productivity.
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Wei, Wei, Chengwan Zha, Aiwen Jiang, Zhe Chao, Liming Hou, Honglin Liu, Ruihua Huang, and Wangjun Wu. "A Combined Differential Proteome and Transcriptome Profiling of Fast- and Slow-Twitch Skeletal Muscle in Pigs." Foods 11, no. 18 (September 14, 2022): 2842. http://dx.doi.org/10.3390/foods11182842.
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Skeletal muscle fiber types can contribute in part to affecting pork quality parameters. Biceps femoris (Bf) (fast muscle or white muscle) and Soleus (Sol) (slow muscle or red muscle) are two typical skeletal muscles characterized by obvious muscle fiber type differences in pigs. However, the critical proteins and potential regulatory mechanisms regulating porcine skeletal muscle fibers have yet to be clearly defined. In this study, the isobaric Tag for Relative and Absolute Quantification (iTRAQ)-based proteome was used to identify the key proteins affecting the skeletal muscle fiber types with Bf and Sol, by integrating the previous transcriptome data, while function enrichment analysis and a protein–protein interaction (PPI) network were utilized to explore the potential regulatory mechanisms of skeletal muscle fibers. A total of 126 differentially abundant proteins (DAPs) between the Bf and Sol were identified, and 12 genes were found to be overlapping between differentially expressed genes (DEGs) and DAPs, which are the critical proteins regulating the formation of skeletal muscle fibers. Functional enrichment and PPI analysis showed that the DAPs were mainly involved in the skeletal-muscle-associated structural proteins, mitochondria and energy metabolism, tricarboxylic acid cycle, fatty acid metabolism, and kinase activity, suggesting that PPI networks including DAPs are the main regulatory network affecting muscle fiber formation. Overall, these data provide valuable information for understanding the molecular mechanism underlying the formation and conversion of muscle fiber types, and provide potential markers for the evaluation of meat quality.
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Perry, S. V. "Properties of the muscle proteins--a comparative approach." Journal of Experimental Biology 115, no. 1 (March 1, 1985): 31–42. http://dx.doi.org/10.1242/jeb.115.1.31.
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The differences in performance that exist between skeletal muscles are in part determined by the presence of different forms of most of the contractile and regulatory proteins of the myofibril - isoforms. These isoforms have common properties but their amino acid sequences are not identical and they exhibit slight differences in biological activities, such as ATPase, affinity for calcium, etc., that are appropriate for the physiological properties of the muscle in which they are present. With the exception of actin, all the major proteins present in the I and A filaments of skeletal muscle have been shown to exist in two or more isoforms. Whereas proteins such as troponin I and troponin C are present as a single isoform in each fibre type in normal muscle, others such as myosin and tropomyosin are present as two or more isoforms, usually in relative amounts characteristic for the fibre type. Type I and type II muscle fibres possess the capacity of synthesizing all the skeletal muscle isoforms of the myofibrillar proteins. The complement of isoforms present in a muscle fibre, however, depends on a number of factors such as the stage of development or regeneration, type of innervation, hormonal effects, etc. Complex mechanisms involving the coordinated control of gene expression must operate to ensure that the set of isoforms of the myofibrillar proteins present is characteristic for the cell type.
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Gong, Henry, Weikang Ma, Shaoshuai Chen, Geng Wang, Ramzi Khairallah, and Thomas Irving. "Localization of the Elastic Proteins in the Flight Muscle of Manduca sexta." International Journal of Molecular Sciences 21, no. 15 (July 31, 2020): 5504. http://dx.doi.org/10.3390/ijms21155504.
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The flight muscle of Manduca sexta (DLM1) is an emerging model system for biophysical studies of muscle contraction. Unlike the well-studied indirect flight muscle of Lethocerus and Drosophila, the DLM1 of Manduca is a synchronous muscle, as are the vertebrate cardiac and skeletal muscles. Very little has been published regarding the ultrastructure and protein composition of this muscle. Previous studies have demonstrated that DLM1 express two projectin isoform, two kettin isoforms, and two large Salimus (Sls) isoforms. Such large Sls isoforms have not been observed in the asynchronous flight muscles of Lethocerus and Drosophila. The spatial localization of these proteins was unknown. Here, immuno-localization was used to show that the N-termini of projectin and Salimus are inserted into the Z-band. Projectin spans across the I-band, and the C-terminus is attached to the thick filament in the A-band. The C-terminus of Sls was also located in the A-band. Using confocal microscopy and experimental force-length curves, thin filament lengths were estimated as ~1.5 µm and thick filament lengths were measured as ~2.5 µm. This structural information may help provide an interpretive framework for future studies using this muscle system.
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OCHIAI, YOSHIHIRO. "Ⅰ-1. Fish muscle proteins." NIPPON SUISAN GAKKAISHI 83, no. 5 (2017): 816. http://dx.doi.org/10.2331/suisan.wa2442-2.
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&NA;. "SKELETAL MUSCLE CYTOSKELETAL PROTEINS 319." Medicine & Science in Sports & Exercise 28, Supplement (May 1996): 54. http://dx.doi.org/10.1097/00005768-199605001-00319.
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PATESTOS, NIKOS P., and MICHAEL G. HARRINGTON. "The extraction of muscle proteins." Biochemical Society Transactions 14, no. 2 (April 1, 1986): 444–45. http://dx.doi.org/10.1042/bst0140444.
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Yomosa, S. "Solitary excitations in muscle proteins." Physical Review A 32, no. 3 (September 1, 1985): 1752–58. http://dx.doi.org/10.1103/physreva.32.1752.
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Slater, C. R. "Muscle proteins and muscular dystrophy." Current Opinion in Cell Biology 1, no. 1 (February 1989): 110–14. http://dx.doi.org/10.1016/s0955-0674(89)80046-8.
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Caswell, A. H., and N. R. Brandt. "Triadic proteins of skeletal muscle." Journal of Bioenergetics and Biomembranes 21, no. 2 (April 1989): 149–62. http://dx.doi.org/10.1007/bf00812067.
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BULLARD, B. "Modular proteins of insect muscle." Advances in Biophysics 33 (1996): 211–21. http://dx.doi.org/10.1016/0065-227x(96)81676-5.
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Weir, Lawrence. "Transcriptional control of muscle proteins." Trends in Cardiovascular Medicine 1, no. 1 (January 1991): 46–49. http://dx.doi.org/10.1016/1050-1738(91)90059-n.
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Lim, Megan S., and Michael P. Walsh. "Phosphorylation of skeletal and cardiac muscle C-proteins by the catalytic subunit of cAMP-dependent protein kinase." Biochemistry and Cell Biology 64, no. 7 (July 1, 1986): 622–30. http://dx.doi.org/10.1139/o86-086.
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Catecholamines are known to influence the contractility of cardiac and skeletal muscles, presumably via cAMP-dependent phosphorylation of specific proteins. We have investigated the in vitro phosphorylation of myofibrillar proteins by the catalytic subunit of cAMP-dependent protein kinase of fast- and slow-twitch skeletal muscles and cardiac muscle with a view to gaining a better understanding of the biochemical basis of catecholamine effects on striated muscles. Incubation of canine red skeletal myofibrils with the isolated catalytic subunit of cAMP-dependent protein kinase and Mg-[γ-32P]ATP led to the rapid incorporation of [32P]phosphate into five major protein substrates of subunit molecular weights (MWs) 143 000, 60 000, 42 000, 33 000, and 11 000. The 143 000 MW substrate was identified as C-protein; the 42 000 MW substrate is probably actin; the 33 000 MW substrate was shown not to be a subunit of tropomyosin and, like the 60 000 and 11 000 MW substrates, is an unidentified myofibrillar protein. Isolated canine red skeletal muscle C-protein was phosphorylated to the extent of ~0.5 mol Pi/mol C-protein. Rabbit white skeletal muscle and bovine cardiac muscle C-proteins were also phosphorylated by the catalytic subunit of cAMP-dependent protein kinase, both in myofibrils and in the isolated state. Cardiac C-protein was phosphorylated to the extent of 5–6 mol Pi/mol C-protein, whereas rabbit white skeletal muscle C-protein was phosphorylated at the level of ~0.5 mol Pi/mol C-protein. As demonstrated earlier by others, C-protein of skeletal and cardiac muscles inhibited the actin-activated myosin Mg2+-ATPase activity at low ionic strength in a system reconstituted from the purified skeletal muscle contractile proteins (actin and myosin). Phosphorylation of skeletal or cardiac C-proteins had no effect on their inhibition of this actomyosin Mg2+-ATPase activity. Furthermore, cardiac C-protein inhibited the Mg2+-ATPase activity of desensitized cardiac actomyosin; in this case, phosphorylation of cardiac C-protein enhanced its inhibitory effect on the actomyosin Mg2+-ATPase. These observations suggest that C-proteins of fast- and slow-twitch skeletal muscle fibers and cardiac muscle fibers are phosphorylated in response to catecholamines and other agents which induce cAMP formation and that, at least in the heart, this phosphorylation may affect actin–myosin interaction and the contractile state of the muscle.
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Massheimer, Virginia, Luis M. Fernandez, and Ana R. de Boland. "Stimulation of Calmodulin Binding to Skeletal Muscle Membrane Proteins by 1,25-Dihydroxy-Vitamin D 3." Zeitschrift für Naturforschung C 45, no. 6 (June 1, 1990): 663–70. http://dx.doi.org/10.1515/znc-1990-0616.
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Abstract Previous work has shown that 1,25-dihydroxy-vitamin D 3 rapidly increases calmodulin levels of skeletal muscle membranes without altering the muscle cell calmodulin content. Therefore, the effects of the sterol on the binding of calmodulin to specific muscle membrane proteins were investigated. Soleus muscles from vitamin D-deficient chicks were treated in vitro for short intervals (5-15 min) with physiological concentrations of 1,25-dihydroxy-vitamin D3. Proteins of mitochondria and microsomes isolated by differential centrifugation were separated on sodium dodecyl sulfate polyacrylamide gels. Calmodulin-binding proteins were identified by a [125I]calmodulin gel overlay procedure followed by autoradiography. 1,25-Dihydroxy- vitamin D3 increased the binding of labelled calmodulin to a major, calcium-independent, calmodulin-binding protein of 28 Kda localized in microsomes, and to minor calmodulin- binding proteins of 78 and 130 Kda proteins localized in mitochondria. The binding of [125I]calmodulin to these proteins was abolished by flufenazine or excess non-radioactive calmodulin. 1,25-Dihydroxy-vitamin D3 rapidly increased muscle tissue Ca uptake and cyclic AM P levels and stimulated the phosphorylation of several membrane proteins including those whose calmodulin-binding capacity potentiates. Analogously to the sterol, forskolin increased membrane calmodulin content, calmodulin binding to the 28 Kda microsomal protein and 45Ca uptake by soleus muscle preparations. Forskolin also induced a similar profile of changes in muscle membrane protein phosphorylation as the hormone. These results suggest that 1,25- dihydroxy-vitamin D 3 affects calmodulin distribution in muscle cells through cyclic AMP-dependent phosphorylation of membrane calmodulin-binding proteins. These changes may play a role in the stimulation of muscle Ca uptake by the sterol.
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Setyabrata, Derico, Danyi Ma, Shaojun Xie, Jyothi Thimmapuram, Bruce Cooper, Uma Aryal, and Brad H. B. Kim. "PSV-4 Proteomics and Metabolomics Profiling of Meat Exudate to Understand the Impact of Postmortem Aging on Oxidative Stability of Beef Muscles." Journal of Animal Science 101, Supplement_2 (October 28, 2023): 268–69. http://dx.doi.org/10.1093/jas/skad341.304.
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Abstract The objectives of this study were to characterize the meat exudate proteome and metabolome composition that may be related to the color and oxidative stability of beef muscles during aging. Beef longissimus lumborum (LD) and psoas major (PM) muscles from seven carcasses were obtained at 2 d postmortem. Each muscle was cut into three sections, vacuum packaged and assigned into three aging periods (9, 16 and 23 d). At the end of each aging period, the exudate was collected from each sample and immediately frozen for both proteomics and metabolomics analyses. Steak cuts were made for display color and oxidative stability analyses. Exudate samples were prepared and analyzed using the UPLC-ESI-MS for metabolomics profiling and HPLC-MS/MS for proteomics analyses. The metabolites were annotated using the HMDB database, and proteins were compared with the UniProt database. The relative abundance of the metabolites and proteins was quantified and normalized for statistical analysis. Both proteomes and metabolites were analyzed using ANOVA (P < 0.05). Principal component analysis (PCA), hierarchical cluster analysis (HCA) and correlation test between color and lipid oxidative stability and metabolites/proteins were performed. Untargeted protein profiling identified a total of 737 proteins from the meat exudate, of which 222 proteins were affected by the treatments (P < 0.05). PCA analysis indicated an apparent clustering of the proteins, mainly separating the cluster by the muscle types. A greater number of oxidative metabolism enzymes was identified in PM exudate, while more glycolytic metabolism enzymes were identified in LD exudate. Additionally, a greater abundance of cytochrome c was observed in PM muscle exudate along with laminin proteins, indicating a greater extent of degradation in the muscle, potentially explaining the lower oxidative stability of PM muscle. A total of 518 metabolite features was detected from the meat exudate using untargeted metabolomics analysis, in which 167 features were affected by the treatments (P < 0.05). The PCA analysis exhibited a distinct grouping of the treatments, separating not only muscle types but also the aging periods. Greater antioxidant compounds, such as carnitines and glucosides, were identified in LD muscle exudate. A greater number of lipid and nucleotide metabolites were also observed in LD exudate and 23d exudate. HSP70 and laminin proteins, along with glucosides metabolites identified in the exudates, which were significantly correlated (r > 0.5) to muscle color and oxidative stability. The current results indicated that meat exudate could be a viable analytical matrix to understand oxidative stability and protein degradation of muscles during aging. The proteomics and metabolomics profiling identified specific compounds in meat exudate that could be related to different oxidative stability of beef muscles. Further research should be warranted to validate the identified compounds as potential biomarkers to predict oxidative stability and quality attributes of specific muscles during aging.
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Fagan, J. M., E. F. Wajnberg, L. Culbert, and L. Waxman. "ATP depletion stimulates calcium-dependent protein breakdown in chick skeletal muscle." American Journal of Physiology-Endocrinology and Metabolism 262, no. 5 (May 1, 1992): E637—E643. http://dx.doi.org/10.1152/ajpendo.1992.262.5.e637.
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The contribution of metabolic energy to the degradation of intracellular proteins in skeletal muscle was investigated. Isolated chick skeletal muscles deprived of oxygen and muscles incubated in buffer under nonphysiological conditions containing inhibitors of glycolysis and mitochondrial respiration had lower concentrations or undetectable levels of ATP and faster rates of proteolysis. Both total protein breakdown and the breakdown of myofibrillar proteins were stimulated 35-124% in ATP-depleted tissues. However, ATP-depleted muscles incubated in buffer to which no Ca2+ was added showed slower rates of total protein breakdown and no significant change in myofibrillar proteolysis compared with control muscles. Trans-epoxysuccinyl-L-leucylamido(4-guanidino)butane (E-64), a compound that inhibits the calpains and the lysosomal cysteine proteases, completely blocked the Ca(2+)-stimulated breakdown of nonmyofibrillar and myofibrillar proteins in ATP-depleted muscles. However, Ca(2+)-stimulated proteolysis was not inhibited in ATP-depleted muscles incubated with weak bases to prevent lysosome function. These data suggest that intracellular proteins can be degraded in skeletal muscle in the absence of metabolic energy and that the calpains play a major role in the enhanced proteolysis in skeletal muscles depleted of ATP.
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Belkin, A. M., I. V. Klimanskaya, M. E. Lukashev, K. Lilley, D. R. Critchley, and V. E. Koteliansky. "A novel phosphoglucomutase-related protein is concentrated in adherens junctions of muscle and nonmuscle cells." Journal of Cell Science 107, no. 1 (January 1, 1994): 159–73. http://dx.doi.org/10.1242/jcs.107.1.159.
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Using five monoclonal antibodies raised against a human uterine smooth muscle extract, we have identified a novel antigen which runs as a closely spaced doublet in SDS-gels. The proteins (60/63 kDa) co-purify, are present in a 1:1 ratio as judged by Coomassie Blue staining, and are immunologically closely related, if not identical. No N-terminal sequence could be obtained from a mixture of the 60/63 kDa proteins, but the sequence of four polypeptides liberated by V8 protease or cyanogen bromide cleavage showed that the proteins are closely related to the glycolytic enzyme phosphoglucomutase type 1. Affinity-purified polyclonal antibodies and three different monoclonal antibodies to the 60/63 kDa proteins cross-reacted with rabbit skeletal muscle phosphoglucomutase type 1, whilst two additional monoclonal antibodies were specific for the 60/63 kDa proteins. Peptide maps of the 60/63 kDa proteins and phosphoglucomutase 1 are markedly different, and the purified proteins have no detectable phosphoglucomutase activity. Staining of cultured smooth muscle cells and fibroblasts with antibodies to 60/63 kDa proteins showed that the antigen is concentrated in focal contacts at the ends of actin bundles and is also associated with actin filaments. About 60% of the cellular 60/63 kDa proteins were found in the detergent-insoluble fraction, suggesting a physical association with the cytoskeleton. The highest levels of protein immunoreactivity were found in muscles. The antigen is concentrated in muscle adherens junctions, including smooth muscle dense plaques, cardiomyocyte intercalated disks, and striated muscle myotendinous junctions. Among epithelial cells, the 63 kDa isoform of the protein was found only in cultured keratinocytes where immunofluorescent staining was localized in cell-to-cell adherens junctions. Expression of the 60/63 kDa proteins in vascular smooth muscle cells is developmentally regulated and correlates with the differentiated contractile phenotype of these cells.
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Kristensen, Michael, Thomas Hansen, and Carsten Juel. "Membrane proteins involved in potassium shifts during muscle activity and fatigue." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 290, no. 3 (March 2006): R766—R772. http://dx.doi.org/10.1152/ajpregu.00534.2004.
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Muscle activity is associated with potassium displacements, which may cause fatigue. It was reported previously that the density of the large-conductance Ca2+-dependent K+ (BKCa) channel is higher in the T tubule membrane than in the sarcolemmal membrane and that the opposite is the case for the ATP-sensitive K+ (KATP) channel. In the present experiments, we investigated the subcellular localizations of the strong inward rectifier 2.1 K+ (Kir2.1) channel and the Na+-K+-2Cl− (NKCC)1 cotransporter with Western blot analysis of different muscle fractions. Furthermore, muscle function was studied while trying to manipulate the opening probability or transport capacity of these proteins during electrical stimulation of isolated soleus muscles. All experiments were made with excised muscle from male Wistar rats. Kir2.1 channels were almost undetectable in the sarcolemmal membrane but present in the T tubule membrane, whereas NKCC1 cotransporters were present in the sarcolemmal membrane. For muscles incubated in a buffer containing pinacidil, NS1619, Ba2+, or bumetanide, there was a faster reduction in peak force ( P < 0.05). Furthermore, bumetanide incubation reduced the peak force at the onset of electrical stimulation ( P < 0.05). Thus the effects on muscle force indicate that these drugs can affect K+-transporting proteins and thereby influence K+ accumulation, especially in the T tubules, suggesting that KATP and BKCa channels are responsible for K+ release and decrease in force during repeated muscle contractions, whereas Kir2.1 and NKCC1 may have a role in K+ reuptake.
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Crippa, Valeria, Mariarita Galbiati, Alessandra Boncoraglio, Paola Rusmini, Elisa Onesto, Elisa Giorgetti, Riccardo Cristofani, Arianna Zito, and Angela Poletti. "Motoneuronal and muscle-selective removal of ALS-related misfolded proteins." Biochemical Society Transactions 41, no. 6 (November 20, 2013): 1598–604. http://dx.doi.org/10.1042/bst20130118.
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ALS (amyotrophic lateral sclerosis), a fatal motoneuron (motor neuron) disease, occurs in clinically indistinguishable sporadic (sALS) or familial (fALS) forms. Most fALS-related mutant proteins identified so far are prone to misfolding, and must be degraded in order to protect motoneurons from their toxicity. This process, mediated by molecular chaperones, requires proteasome or autophagic systems. Motoneurons are particularly sensitive to misfolded protein toxicity, but other cell types such as the muscle cells could also be affected. Muscle-restricted expression of the fALS protein mutSOD1 (mutant superoxide dismutase 1) induces muscle atrophy and motoneuron death. We found that several genes have an altered expression in muscles of transgenic ALS mice at different stages of disease. MyoD, myogenin, atrogin-1, TGFβ1 (transforming growth factor β1) and components of the cell response to proteotoxicity [HSPB8 (heat shock 22kDa protein 8), Bag3 (Bcl-2-associated athanogene 3) and p62] are all up-regulated by mutSOD1 in skeletal muscle. When we compared the potential mutSOD1 toxicity in motoneuron (NSC34) and muscle (C2C12) cells, we found that muscle ALS models possess much higher chymotryptic proteasome activity and autophagy power than motoneuron ALS models. As a result, mutSOD1 molecular behaviour was found to be very different. MutSOD1 clearance was found to be much higher in muscle than in motoneurons. MutSOD1 aggregated and impaired proteasomes only in motoneurons, which were particularly sensitive to superoxide-induced oxidative stress. Moreover, in muscle cells, mutSOD1 was found to be soluble even after proteasome inhibition. This effect could be associated with a higher mutSOD1 autophagic clearance. Therefore muscle cells seem to manage misfolded mutSOD1 more efficiently than motoneurons, thus mutSOD1 toxicity in muscle may not directly depend on aggregation.
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Thakur, Savant S., Kristy Swiderski, James G. Ryall, and Gordon S. Lynch. "Therapeutic potential of heat shock protein induction for muscular dystrophy and other muscle wasting conditions." Philosophical Transactions of the Royal Society B: Biological Sciences 373, no. 1738 (December 4, 2017): 20160528. http://dx.doi.org/10.1098/rstb.2016.0528.
Full textAbstract:
Duchenne muscular dystrophy is the most common and severe of the muscular dystrophies, a group of inherited myopathies caused by different genetic mutations leading to aberrant expression or complete absence of cytoskeletal proteins. Dystrophic muscles are prone to injury, and regenerate poorly after damage. Remorseless cycles of muscle fibre breakdown and incomplete repair lead to progressive and severe muscle wasting, weakness and premature death. Many other conditions are similarly characterized by muscle wasting, including sarcopenia, cancer cachexia, sepsis, denervation, burns, and chronic obstructive pulmonary disease. Muscle trauma and loss of mass and physical capacity can significantly compromise quality of life for patients. Exercise and nutritional interventions are unlikely to halt or reverse the conditions, and strategies promoting muscle anabolism have limited clinical acceptance. Heat shock proteins (HSPs) are molecular chaperones that help proteins fold back to their original conformation and restore function. Since many muscle wasting conditions have pathophysiologies where inflammation, atrophy and weakness are indicated, increasing HSP expression in skeletal muscle may have therapeutic potential. This review will provide evidence supporting HSP induction for muscular dystrophy and other muscle wasting conditions. This article is part of the theme issue ‘Heat shock proteins as modulators and therapeutic targets of chronic disease: an integrated perspective’.
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Corasolla Carregari, Victor, Mauro Monforte, Giuseppe Di Maio, Luisa Pieroni, Andrea Urbani, Enzo Ricci, and Giorgio Tasca. "Proteomics of Muscle Microdialysates Identifies Potential Circulating Biomarkers in Facioscapulohumeral Muscular Dystrophy." International Journal of Molecular Sciences 22, no. 1 (December 30, 2020): 290. http://dx.doi.org/10.3390/ijms22010290.
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Facioscapulohumeral muscular dystrophy (FSHD) is caused by a complex epigenetic mechanism finally leading to the misexpression of DUX4 in skeletal muscle. Detecting DUX4 and quantifying disease progression in FSHD is extremely challenging, thus increasing the need for surrogate biomarkers. We applied a shotgun proteomic approach with two different setups to analyze the protein repertoire of interstitial fluids obtained from 20 muscles in different disease stages classified by magnetic resonance imaging (MRI) and serum samples from 10 FSHD patients. A total of 1156 proteins were identified in the microdialysates by data independent acquisition, 130 of which only found in muscles in active disease stage. Proteomic profiles were able to distinguish FSHD patients from controls. Two innate immunity mediators (S100-A8 and A9) and Dermcidin were upregulated in muscles with active disease and selectively present in the sera of FSHD patients. Structural muscle and plasminogen pathway proteins were downregulated. Together with the upstream inhibition of myogenic factors, this suggests defective muscle regeneration and increased fibrosis in early/active FSHD. Our MRI targeted exploratory approach confirmed that inflammatory response has a prominent role, together with impaired muscle regeneration, before clear muscle wasting occurs. We also identified three proteins as tissue and possibly circulating biomarkers in FSHD.
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Price, M. G. "Skelemins: cytoskeletal proteins located at the periphery of M-discs in mammalian striated muscle." Journal of Cell Biology 104, no. 5 (May 1, 1987): 1325–36. http://dx.doi.org/10.1083/jcb.104.5.1325.
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The cytoskeletons of mammalian striated and smooth muscles contain a pair of high molecular weight (HMW) polypeptides of 220,000 and 200,000 mol wt, each with isoelectric points of about 5 (Price, M. G., 1984, Am. J. Physiol., 246:H566-572) in a molar ratio of 1:1:20 with desmin. The HMW polypeptides of mammalian muscle have been named "skelemins," because they are in the insoluble cytoskeletons of striated muscle and are at the M-discs. I have used two-dimensional peptide mapping to show that the two skelemin polypeptides are closely related to each another. Polyclonal antibodies directed against skelemins were used to demonstrate that they are immunologically distinct from talin, fodrin, myosin heavy chain, synemin, microtubule-associated proteins, and numerous other proteins of similar molecular weight, and are not oligomers of other muscle proteins. Skelemins appear not to be proteolytic products of larger proteins, as shown by immunoautoradiography on 3% polyacrylamide gels. Skelemins are predominantly cytoskeletal, with little extractable from myofibrils by various salt solutions. Human, bovine, and rat cardiac, skeletal, and smooth muscles, but not chicken muscles, contain proteins cross-reacting with anti-skelemin antibodies. Skelemins are localized by immunofluorescence at the M-lines of cardiac and skeletal muscle, in 0.4-micron-wide smooth striations. Cross sections reveal that skelemins are located at the periphery of the M-discs. Skelemins are seen in threads linking isolated myofibrils at the M-discs. There is sufficient skelemin in striated muscle to wrap around the M-disc about three times, if the skelemin molecules are laid end to end, assuming a length-to-weight ratio similar to M-line protein and other elongated proteins. The results indicate that skelemins form linked rings around the periphery of the myofibrillar M-discs. These cytoskeletal rings may play a role in the maintenance of the structural integrity of striated muscle throughout cycles of contraction and relaxation.
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Locke, M., E. G. Noble, and B. G. Atkinson. "Inducible isoform of HSP70 is constitutively expressed in a muscle fiber type specific pattern." American Journal of Physiology-Cell Physiology 261, no. 5 (November 1, 1991): C774—C779. http://dx.doi.org/10.1152/ajpcell.1991.261.5.c774.
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The most prominent group of stress or heat-shock proteins (HSPs) has an Mr of approximately 70,000 and is collectively referred to as the HSP70 family. The extent of stress inducibility and subcellular location of the various HSP70 isoforms differ, but all appear to be involved with ATP-dependent stabilization or solubilization of proteins. One isoform, termed the inducible isoform of HSP70 (HSP72i), is normally absent in unstressed cells. In a previous study, we detected a protein corresponding in Mr and pI to HSP72i in unstressed rat muscle. Therefore, it was of interest to determine if this expression in unstressed muscle cells is general or confined to specific muscle fiber types. To answer this question we have employed various rat hindlimb muscles that differ in fiber type proportion from predominantly type I (soleus) to predominantly type IIB (white gastrocnemius). Proteins from muscle homogenates were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, blotted to a nylon membrane, probed with a monoclonal antibody for HSP72i, and visualized using an alkaline phosphatase-conjugated secondary antibody. Immunoblot analyses demonstrate the constitutive expression of HSP72i in rat muscles comprised primarily of type I muscle fibers (soleus), but not in muscles comprised primarily of type IIB fibers (white gastrocnemius). In muscles of mixed fiber type, HSP72i content is roughly proportional to the percentage of type I fibers. These results substantiate that unstressed rat muscles express the inducible HSP72 isoform and demonstrate that its constitutive expression is proportional to the type I muscle fiber composition.
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Cohen, Shenhav, Jeffrey J. Brault, Steven P. Gygi, David J. Glass, David M. Valenzuela, Carlos Gartner, Esther Latres, and Alfred L. Goldberg. "During muscle atrophy, thick, but not thin, filament components are degraded by MuRF1-dependent ubiquitylation." Journal of Cell Biology 185, no. 6 (June 8, 2009): 1083–95. http://dx.doi.org/10.1083/jcb.200901052.
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Loss of myofibrillar proteins is a hallmark of atrophying muscle. Expression of muscle RING-finger 1 (MuRF1), a ubiquitin ligase, is markedly induced during atrophy, and MuRF1 deletion attenuates muscle wasting. We generated mice expressing a Ring-deletion mutant MuRF1, which binds but cannot ubiquitylate substrates. Mass spectrometry of the bound proteins in denervated muscle identified many myofibrillar components. Upon denervation or fasting, atrophying muscles show a loss of myosin-binding protein C (MyBP-C) and myosin light chains 1 and 2 (MyLC1 and MyLC2) from the myofibril, before any measurable decrease in myosin heavy chain (MyHC). Their selective loss requires MuRF1. MyHC is protected from ubiquitylation in myofibrils by associated proteins, but eventually undergoes MuRF1-dependent degradation. In contrast, MuRF1 ubiquitylates MyBP-C, MyLC1, and MyLC2, even in myofibrils. Because these proteins stabilize the thick filament, their selective ubiquitylation may facilitate thick filament disassembly. However, the thin filament components decreased by a mechanism not requiring MuRF1.
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Fujii, Nobuharu, Marni D. Boppart, Scott D. Dufresne, Patricia F. Crowley, Alison C. Jozsi, Kei Sakamoto, Haiyan Yu, et al. "Overexpression or ablation of JNK in skeletal muscle has no effect on glycogen synthase activity." American Journal of Physiology-Cell Physiology 287, no. 1 (July 2004): C200—C208. http://dx.doi.org/10.1152/ajpcell.00415.2003.
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c-Jun NH2-terminal kinase (JNK) is highly expressed in skeletal muscle and is robustly activated in response to muscle contraction. Little is known about the biological functions of JNK signaling in terminally differentiated muscle cells, although this protein has been proposed to regulate insulin-stimulated glycogen synthase activity in mouse skeletal muscle. To determine whether JNK signaling regulates contraction-stimulated glycogen synthase activation, we applied an electroporation technique to induce JNK overexpression (O/E) in mouse skeletal muscle. Ten days after electroporation, in situ muscle contraction increased JNK activity 2.6-fold in control muscles and 15-fold in the JNK O/E muscles. Despite the enormous activation of JNK activity in JNK O/E muscles, contraction resulted in similar increases in glycogen synthase activity in control and JNK O/E muscles. Consistent with these findings, basal and contraction-induced glycogen synthase activity was normal in muscles of both JNK1- and JNK2-deficient mice. JNK overexpression in muscle resulted in significant alterations in the basal phosphorylation state of several signaling proteins, such as extracellular signal-regulated kinase 1/2, p90 S6 kinase, glycogen synthase kinase 3, protein kinase B/Akt, and p70 S6 kinase, in the absence of changes in the expression of these proteins. These data suggest that JNK signaling regulates the phosphorylation state of several kinases in skeletal muscle. JNK activation is unlikely to be the major mechanism by which contractile activity increases glycogen synthase activity in skeletal muscle.
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Nagendra, Apoorva H., Animikh Ray, Debajit Chaudhury, Akash Mitra, Anu Vinod Ranade, Bipasha Bose, and Sudheer Shenoy P. "Sodium fluoride induces skeletal muscle atrophy via changes in mitochondrial and sarcomeric proteomes." PLOS ONE 17, no. 12 (December 22, 2022): e0279261. http://dx.doi.org/10.1371/journal.pone.0279261.
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Sodium Fluoride (NaF) can change the expression of skeletal muscle proteins. Since skeletal muscle is rich in mitochondrial and contractile (sarcomeric) proteins, these proteins are sensitive to the effects of NaF, and the changes are dose-and time-dependent. In the current study, we have analysed the effect of high concentrations of NaF (80ppm) on mouse skeletal muscle at two different time points, i.e., 15 days and 60 days. At the end of the experimental time, the animals were sacrificed, skeletal muscles were isolated, and proteins were extracted and subjected to bioinformatic (Mass Spectrometric) analysis. The results were analysed based on changes in different mitochondrial complexes, contractile (sarcomeric) proteins, 26S proteasome, and ubiquitin-proteasome pathway. The results showed that the mitochondrial proteins of complex I, II, III, IV and V were differentially regulated in the groups treated with 80ppm of NaF for 15 days and 60 days. The network analysis indicated more changes in mitochondrial proteins in the group treated with the higher dose for 15 days rather than 60 days. Furthermore, differential expression of (sarcomeric) proteins, downregulation of 26S proteasome subunits, and differential expression in proteins related to the ubiquitin-proteasome pathway lead to muscle atrophy. The differential expression might be due to the adaptative mechanism to counteract the deleterious effects of NaF on energy metabolism. Data are available via ProteomeXchange with identifier PXD035014.
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Chen, Chiao-nan, Deborah A. Ferrington, and LaDora V. Thompson. "Carbonic anhydrase III and four-and-a-half LIM protein 1 are preferentially oxidized with muscle unloading." Journal of Applied Physiology 105, no. 5 (November 2008): 1554–61. http://dx.doi.org/10.1152/japplphysiol.90680.2008.
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The identities of proteins that show disuse-related changes in the content of oxidative modification are unknown. Furthermore, it is unknown whether the global accumulation of oxidized proteins is greater in aged animals with muscle disuse. The purposes of this study are 1) to identify the exact proteins that show disuse-related changes in oxidation levels and 2) to test the hypothesis that the global accumulation of oxidized proteins with muscle disuse would be greater in aged animals. Adult and old rats were randomized into four groups: weight bearing and 3, 7, or 14 days of hindlimb unloading. Soleus muscles were harvested to investigate the protein oxidation with unloading. Slot blot, SDS-PAGE, and Western blot analyses were used to detect the accumulation of 4-hydroxy-2-nonenol (HNE)- and nitrotyrosine (NT)-modified proteins. Matrix-assisted laser desorption ionization-time of flight and tandem mass spectroscopy were used to identify modified proteins. We found that global HNE- and NT-modified proteins accumulated significantly with aging but not with muscle unloading. Two HNE and NT target proteins, four-and-a-half LIM protein 1 (FHL1) and carbonic anhydrase III (CAIII), showed changes in the oxidation levels with muscle unloading. The changes in the oxidation levels happened to adult rats but not old rats. However, old rats had higher baseline levels of HNE-modified FHL1. In summary, the data suggest that the muscle unloading-related changes of protein oxidation are more significant in specific proteins and that the changes are age related.
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Lyons, G. E., M. E. Buckingham, and H. G. Mannherz. "alpha-Actin proteins and gene transcripts are colocalized in embryonic mouse muscle." Development 111, no. 2 (February 1, 1991): 451–54. http://dx.doi.org/10.1242/dev.111.2.451.
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The alpha-actins are among the earliest muscle-specific mRNAs to appear in developing cardiac and skeletal muscle. To determine if there is coexpression of the alpha-actin proteins at early stages of myogenesis, we have used an alpha-actin-specific polyclonal antibody and in situ hybridization with specific cRNA probes to cardiac and skeletal alpha-actin transcripts on serial slides of mouse embryo sections. As soon as we can detect alpha-actin mRNAs in embryonic striated muscle, we also detect the protein suggesting that alpha-actin transcripts are translated very rapidly after transcription during myogenesis. In skeletal muscle, this colocalization of alpha-actin mRNA and protein was observed both in the myotomes of somites and in developing muscles in the limbs. In cardiac muscle, alpha-actin transcripts and proteins are abundantly expressed as soon as a cardiac tube forms.
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Buse, Maria G., Katherine A. Robinson, Bess A. Marshall, Richard C. Hresko, and Mike M. Mueckler. "Enhanced O-GlcNAc protein modification is associated with insulin resistance in GLUT1-overexpressing muscles." American Journal of Physiology-Endocrinology and Metabolism 283, no. 2 (August 1, 2002): E241—E250. http://dx.doi.org/10.1152/ajpendo.00060.2002.
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O-linked glycosylation on Ser/Thr with single N-acetylglucosamine ( O-GlcNAcylation) is a reversible modification of many cytosolic/nuclear proteins, regulated in part by UDP-GlcNAc levels. Transgenic (T) mice that overexpress GLUT1 in muscle show increased basal muscle glucose transport that is resistant to insulin stimulation. Muscle UDP-GlcNAc levels are increased. To assess whether GLUT4 is a substrate for O-GlcNAcylation, we translated GLUT4 mRNA (mutated at the N-glycosylation site) in rabbit reticulocyte lysates supplemented with [35S]methionine. O-GlcNAcylated proteins were galactosylated and separated by lectin affinity chromatography; >20% of the translated GLUT4 appeared to be O-GlcNAcylated. To assess whether GLUT4 or GLUT4-associated proteins were O-GlcNAcylated in muscles, muscle membranes were prepared from T and control (C) mice labeled with UDP-[3H]galactose and immunoprecipitated with anti-GLUT4 IgG (or nonimmune serum), and N-glycosyl side chains were removed enzymatically. Upon SDS-PAGE, several bands showed consistently two- to threefold increased labeling in T vs. C. Separating galactosylated products by lectin chromatography similarly revealed approximately threefold more O-GlcNAc-modified proteins in T vs. C muscle membranes. RL-2 immunoblots confirmed these results. In conclusion, chronically increased glucose flux, which raises UDP-GlcNAc in muscle, results in enhanced O-GlcNAcylation of membrane proteins in vivo. These may include GLUT4 and/or GLUT4-associated proteins and may contribute to insulin resistance in this model.
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Gordon, Scott E., Martin Flück, and Frank W. Booth. "Selected Contribution: Skeletal muscle focal adhesion kinase, paxillin, and serum response factor are loading dependent." Journal of Applied Physiology 90, no. 3 (March 1, 2001): 1174–83. http://dx.doi.org/10.1152/jappl.2001.90.3.1174.
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This investigation examined the effect of mechanical loading state on focal adhesion kinase (FAK), paxillin, and serum response factor (SRF) in rat skeletal muscle. We found that FAK concentration and tyrosine phosphorylation, paxillin concentration, and SRF concentration are all lower in the lesser load-bearing fast-twitch plantaris and gastrocnemius muscles compared with the greater load-bearing slow-twitch soleus muscle. Of these three muscles, 7 days of mechanical unloading via tail suspension elicited a decrease in FAK tyrosine phosphorylation only in the soleus muscle and decreases in FAK and paxillin concentrations only in the plantaris and gastrocnemius muscles. Unloading decreased SRF concentration in all three muscles. Mechanical overloading (via bilateral gastrocnemius ablation) for 1 or 8 days increased FAK and paxillin concentrations in the soleus and plantaris muscles. Additionally, whereas FAK tyrosine phosphorylation and SRF concentration were increased by ≤1 day of overloading in the soleus muscle, these increases did not occur until somewhere between 1 and 8 days of overloading in the plantaris muscle. These data indicate that, in the skeletal muscles of rats, the focal adhesion complex proteins FAK and paxillin and the transcription factor SRF are generally modulated in association with the mechanical loading state of the muscle. However, the somewhat different patterns of adaptation of these proteins to altered loading in slow- vs. fast-twitch skeletal muscles indicate that the mechanisms and time course of adaptation may partly depend on the prior loading state of the muscle.
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Lee, Jun-Hoe, Kevin M. Lewis, Timothy W. Moural, Bogdan Kirilenko, Barbara Borgonovo, Gisa Prange, Manfred Koessl, Stefan Huggenberger, ChulHee Kang, and Michael Hiller. "Molecular parallelism in fast-twitch muscle proteins in echolocating mammals." Science Advances 4, no. 9 (September 2018): eaat9660. http://dx.doi.org/10.1126/sciadv.aat9660.
Full textAbstract:
Detecting associations between genomic changes and phenotypic differences is fundamental to understanding how phenotypes evolved. By systematically screening for parallel amino acid substitutions, we detected known as well as novel cases (Strc, Tecta, and Cabp2) of parallelism between echolocating bats and toothed whales in proteins that could contribute to high-frequency hearing adaptations. Our screen also showed that echolocating mammals exhibit an unusually high number of parallel substitutions in fast-twitch muscle fiber proteins. Both echolocating bats and toothed whales produce an extremely rapid call rate when homing in on their prey, which was shown in bats to be powered by specialized superfast muscles. We show that these genes with parallel substitutions (Casq1, Atp2a1, Myh2, and Myl1) are expressed in the superfast sound-producing muscle of bats. Furthermore, we found that the calcium storage protein calsequestrin 1 of the little brown bat and the bottlenose dolphin functionally converged in its ability to form calcium-sequestering polymers at lower calcium concentrations, which may contribute to rapid calcium transients required for superfast muscle physiology. The proteins that our genomic screen detected could be involved in the convergent evolution of vocalization in echolocating mammals by potentially contributing to both rapid Ca2+ transients and increased shortening velocities in superfast muscles.
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Swynghedauw, B. "Developmental and functional adaptation of contractile proteins in cardiac and skeletal muscles." Physiological Reviews 66, no. 3 (July 1, 1986): 710–71. http://dx.doi.org/10.1152/physrev.1986.66.3.710.
Full textAbstract:
The goal of this review is to summarize our knowledge of the plasticity of striated muscles in terms of contractile proteins. During development or when the working conditions are changed, the intrinsic physiological properties of both cardiac and skeletal muscles are modified. These modifications generally adapt the muscle to the new environmental requirements. One of the best examples is compensatory overload obtained in fast skeletal muscle by synergistic tenotomy and in a fast ventricle, such as in rats, by aortic banding. In both cases, after a few weeks the initial speed of shortening for the unloaded muscle drops, whereas the maximum tension developed remains unchanged. Heat measurements show that efficiency (i.e., g work/mol ATP) is improved at the fiber level. The fast skeletal muscle becomes slow, fatigue resistant, and then more adapted to endurance. For the ventricle as a whole to become slow is beneficial only if one contraction is considered; however, it is detrimental in terms of cardiac output and leads finally to failure. This adaptational process is partly explained by quantitative and qualitative changes in contractile proteins. Protein synthesis is rapidly enhanced and muscles hypertrophy, which in turn multiplies the contractile units and for the cardiac cylinder normalizes the wall stress. In the meantime the structure and, for myosin, the biological activity of several contractile proteins are modified. These modifications are very unlikely to be posttranscriptional and are in fact explained by several isoform shifts. In both tissues, for example, the expression of the gene coding for a fast myosin (MHCf in skeletal muscle, alpha-MHC in ventricles) is repressed and that of the gene coding for a slow myosin (beta-MHC in both tissues) is stimulated. This is accompanied by a coordinated increase in synthesis of other contractile proteins and, in skeletal muscle only, by isoform shifts of myosin light chains and of the TM-TN regulatory system. Other changes are less well understood. During development it has recently been discovered that three different MHCs (MHCemb, MHCneo, and MHCf) appear sequentially in fast skeletal muscle, which explains, for example, several contradictions of immunological cross-reactions. Currently, however, the functional significance of this finding is unknown, and the well-known decrease of shortening velocity observed in cardiac and skeletal muscles during fetal life is unexplained in terms of contractile proteins.(ABSTRACT TRUNCATED AT 400 WORDS)
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Flück, Martin, James A. Carson, Scott E. Gordon, Andrew Ziemiecki, and Frank W. Booth. "Focal adhesion proteins FAK and paxillin increase in hypertrophied skeletal muscle." American Journal of Physiology-Cell Physiology 277, no. 1 (July 1, 1999): C152—C162. http://dx.doi.org/10.1152/ajpcell.1999.277.1.c152.
Full textAbstract:
Components of signaling pathways for mechanotransduction during load-induced enlargement of skeletal muscle have not been completely defined. We hypothesized that loading of skeletal muscle would result in an adaptive increase in the expression of two focal adhesion complex (FAC)-related proteins, focal adhesion kinase (FAK) and paxillin, as well as increased FAK activity. FAK protein was immunolocalized to the sarcolemmal region of rooster anterior latissimus dorsi (ALD) myofibers in the middle of the ALD muscle. FAK (77 and 81%) and paxillin (206 and 202%) protein concentrations per unit of total protein in Western blots increased significantly after 1.5 and 7 days, but not after 13 days, of stretch-induced hypertrophy-hyperplasia of the ALD muscle. FAK autokinase activity in immunoprecipitates was increased after 1.5, 7, and 13 days in stretched ALD muscles. To determine whether increased FAK and paxillin protein concentrations are associated with hypertrophy and/or new fiber formation, two additional experiments were performed. First, during formation of primary chicken myotubes (a model of new fiber formation), FAK protein concentration (63%), FAK activity (157%), and paxillin protein concentration (97%) increased compared with myoblasts. Second, FAK (112% and 611%) and paxillin (87% and 431%) protein concentrations per unit of total protein in the soleus muscle increased at 1 and 8 days after surgical ablation of the synergistic gastrocnemius muscle (a model of hypertrophy without hyperplasia). Thus increases in components of the FAC occur in hypertrophying muscle of animals and in newly formed muscle fibers in culture. Furthermore, increased FAK activity suggests a possible convergence of signaling at the FAC in load-induced growth of skeletal muscle.
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McDonagh, Brian, Giorgos K. Sakellariou, and Malcolm J. Jackson. "Application of redox proteomics to skeletal muscle aging and exercise." Biochemical Society Transactions 42, no. 4 (August 1, 2014): 965–70. http://dx.doi.org/10.1042/bst20140085.
Full textAbstract:
Skeletal muscle represents a physiologically relevant model for the application of redox proteomic techniques to dissect its response to exercise and aging. Contracting skeletal muscles generate ROS (reactive oxygen species) and RNS (reactive nitrogen species) necessary for the regulation of many proteins involved in excitation–contraction coupling. The magnitude and species of ROS/RNS generated by contracting muscles will have downstream effects on specific protein targets and cellular redox signalling. Redox modifications on specific proteins are essential for the adaptive response to exercise and skeletal muscle can develop a dysregulated redox response during aging. In the present article, we discuss how redox proteomics can be applied to identify and quantify the reversible modifications on susceptible cysteine residues within those redox-sensitive proteins, and the integration of oxidative and non-oxidative protein modifications in relation to the functional proteome.