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Artykuły w czasopismach na temat „Muscle proteins”

Autor: Grafiati

Data publikacji: 4 czerwca 2021

Data aktualizacji: 1 sierpnia 2024

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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 presen

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2

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-performanc

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5

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 Pr

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6

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

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7

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

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8

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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9

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: Longissim

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10

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 pr

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11

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 expr

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12

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 c

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13

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 follow

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14

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.

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15

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 f

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16

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 fract

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18

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 wi

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19

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 hav

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20

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

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21

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 &amp Science in Sports &amp 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

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30

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 polyacryla

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31

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 dis

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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 slowe

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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 ty

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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

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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

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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.

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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 chroni

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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 t

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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 aga

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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

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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 m

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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 sit

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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 Spectro

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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 unloadi

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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

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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 galactosyla

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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 FA

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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.

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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 extre

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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.

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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 fo

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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.

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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

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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.

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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 exerci

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