scholarly journals The Dystrophin Node as Integrator of Cytoskeletal Organization, Lateral Force Transmission, Fiber Stability and Cellular Signaling in Skeletal Muscle

Proteomes ◽  
2021 ◽  
Vol 9 (1) ◽  
pp. 9
Author(s):  
Paul Dowling ◽  
Stephen Gargan ◽  
Sandra Murphy ◽  
Margit Zweyer ◽  
Hemmen Sabir ◽  
...  
Keyword(s):  
Cellular Signaling ◽  
Lateral Force ◽  
Subcellular Fractionation ◽  
Protein Product ◽  
Force Transmission ◽  
Two Dimensional Gel Electrophoresis ◽  
Cytoskeletal Organization ◽  
Extracellular Region ◽  
Modern Mass ◽  
Dystrophin Complex

The systematic bioanalytical characterization of the protein product of the DMD gene, which is defective in the pediatric disorder Duchenne muscular dystrophy, led to the discovery of the membrane cytoskeletal protein dystrophin. Its full-length muscle isoform Dp427-M is tightly linked to a sarcolemma-associated complex consisting of dystroglycans, sarcoglyans, sarcospan, dystrobrevins and syntrophins. Besides these core members of the dystrophin–glycoprotein complex, the wider dystrophin-associated network includes key proteins belonging to the intracellular cytoskeleton and microtubular assembly, the basal lamina and extracellular matrix, various plasma membrane proteins and cytosolic components. Here, we review the central role of the dystrophin complex as a master node in muscle fibers that integrates cytoskeletal organization and cellular signaling at the muscle periphery, as well as providing sarcolemmal stabilization and contractile force transmission to the extracellular region. The combination of optimized tissue extraction, subcellular fractionation, advanced protein co-purification strategies, immunoprecipitation, liquid chromatography and two-dimensional gel electrophoresis with modern mass spectrometry-based proteomics has confirmed the composition of the core dystrophin complex at the sarcolemma membrane. Importantly, these biochemical and mass spectrometric surveys have identified additional members of the wider dystrophin network including biglycan, cavin, synemin, desmoglein, tubulin, plakoglobin, cytokeratin and a variety of signaling proteins and ion channels.

Phosphorylated and non-phosphorylated forms of catechol O-methyltransferase in rat liver, brain and other tissues

2008 ◽  
Vol 417 (2) ◽  
pp. 535-545 ◽  
Author(s):  
Anders Øverbye ◽  
Per O. Seglen
Keyword(s):  
Structural Modification ◽  
Ion Trap ◽  
Rat Hepatocytes ◽  
Subcellular Fractionation ◽  
Amino Acid Sequencing ◽  
Two Dimensional Gel Electrophoresis ◽  
Isolated Rat Hepatocytes ◽  
Ionization Time ◽  
Acidic Form ◽  
Liver And Kidney

Seven different forms of the enzyme COMT (catechol O-methyltransferase) were found in isolated rat hepatocytes by two-dimensional gel electrophoresis and immunoblotting: five small variants (S-COMT) and two large variants (L-COMT). The identities of these COMT forms were verified by tryptic fingerprinting using MALDI–TOF (matrix-assisted laser-desorption ionization–time-of-flight) MS, and by amino acid sequencing using ESI–IT–MS/MS (electrospray ionization with ion-trap tandem MS). Analysis of tissue distributions showed that the S-COMT forms were highly expressed in liver and kidney, whereas L-COMT was expressed more strongly in other tissues. Both of the L-COMT forms were found in all of the tissues examined except the heart, which expressed only the most acidic form, and the kidney, which expressed only the most basic form. Subcellular fractionation revealed the presence of both S-COMT and L-COMT in soluble, as well as sedimentable, fractions, suggesting that they should be classified by size rather than (as previously) by localization. Several of the S-COMT forms were N-acetylated, and the two most acidic forms were found to be phosphorylated at Ser260. One of the latter was unique to liver cells; the other was also found in kidney, brain and thymus. Among the non-phosphorylated S-COMT forms, one was ubiquitous, one was found in testis and liver, and a third was found in liver, kidney and thymus. No other phosphorylated sites were found, suggesting that the pI differences distinguishing between the various COMT forms are due to some as yet unidentified structural modification(s).

scholarly journals Syncoilin is required for generating maximum isometric stress in skeletal muscle but dispensable for muscle cytoarchitecture

2008 ◽  
Vol 294 (5) ◽  
pp. C1175-C1182 ◽  
Author(s):  
Jianlin Zhang ◽  
Marie-Louise Bang ◽  
David S. Gokhin ◽  
Yingchun Lu ◽  
Li Cui ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Development ◽  
Striated Muscle ◽  
Neuromuscular Diseases ◽  
Eccentric Contraction ◽  
Lateral Force ◽  
Force Transmission ◽  
Skeletal Muscle Contraction ◽  
Supportive Role

Syncoilin is a striated muscle-specific intermediate filament-like protein, which is part of the dystrophin-associated protein complex (DPC) at the sarcolemma and provides a link between the extracellular matrix and the cytoskeleton through its interaction with α-dystrobrevin and desmin. Its upregulation in various neuromuscular diseases suggests that syncoilin may play a role in human myopathies. To study the functional role of syncoilin in cardiac and skeletal muscle in vivo, we generated syncoilin-deficient ( syncoilin−/−) mice. Our detailed analysis of these mice up to 2 yr of age revealed that syncoilin is entirely dispensable for cardiac and skeletal muscle development and maintenance of cellular structure but is required for efficient lateral force transmission during skeletal muscle contraction. Notably, syncoilin−/− skeletal muscle generates less maximal isometric stress than wild-type (WT) muscle but is as equally susceptible to eccentric contraction-induced injury as WT muscle. This suggests that syncoilin may play a supportive role for desmin in the efficient coupling of mechanical stress between the myofibril and fiber exterior. It is possible that the reduction in isometric stress production may predispose the syncoilin skeletal muscle to a dystrophic condition.

scholarly journals Biomechanical Properties of the Sarcolemma and Costameres of Skeletal Muscle Lacking Desmin

2021 ◽  
Vol 12 ◽  
Author(s):  
Karla P. Garcia-Pelagio ◽  
Robert J. Bloch
Keyword(s):  
Skeletal Muscle ◽  
Lateral Force ◽  
Biomechanical Properties ◽  
Contractile Force ◽  
Contractile Apparatus ◽  
Force Transmission ◽  
Fast Twitch Muscle ◽  
Intracellular Organelles ◽  
Time Required ◽  
Fast Twitch

Intermediate filaments (IFs), composed primarily by desmin and keratins, link the myofibrils to each other, to intracellular organelles, and to the sarcolemma. There they may play an important role in transfer of contractile force from the Z-disks and M-lines of neighboring myofibrils to costameres at the membrane, across the membrane to the extracellular matrix, and ultimately to the tendon (“lateral force transmission”). We measured the elasticity of the sarcolemma and the connections it makes at costameres with the underlying contractile apparatus of individual fast twitch muscle fibers of desmin-null mice. By positioning a suction pipet to the surface of the sarcolemma and applying increasing pressure, we determined the pressure at which the sarcolemma separated from nearby sarcomeres, Pseparation, and the pressure at which the isolated sarcolemma burst, Pbursting. We also examined the time required for the intact sarcolemma-costamere-sarcomere complex to reach equilibrium at lower pressures. All measurements showed the desmin-null fibers to have slower equilibrium times and lower Pseparation and Pbursting than controls, suggesting that the sarcolemma and its costameric links to nearby contractile structures were weaker in the absence of desmin. Comparisons to earlier values determined for muscles lacking dystrophin or synemin suggest that the desmin-null phenotype is more stable than the former and less stable than the latter. Our results are consistent with the moderate myopathy seen in desmin-null muscles and support the idea that desmin contributes significantly to sarcolemmal stability and lateral force transmission.

Investigation and Comparison of Tires Perfomance on Ice

2017 ◽  
Author(s):  
Andrius Ružinskas ◽  
Henrikas Sivilevicius
Keyword(s):  
Lateral Force ◽  
Operating Conditions ◽  
Slip Angle ◽  
Transmission Measurement ◽  
Force Transmission ◽  
Force Coefficient ◽  
Slip Ratio ◽  
The Road ◽  
Tire Force ◽  
Main Component

The risk of accident increases significantly when tire rolls on ice comparing to the dry surface. The vehicle tire becomes the main component of force transmission to the road and necessity of investigating the tire behavior becomes of high importance. This paper presents results of tire force transmission measurement with two different winter tires at the same operating conditions. Longitudinal and lateral force coefficient characteristics as the functions of slip ratio and slip angle are presented and discussed. The results showed a different lateral and longitudinal performance because of different tread pattern and rubber compound.

scholarly journals The Differential Composition of Whey Proteomes in Hu Sheep Colostrum and Milk during Different Lactation Periods

Animals ◽  
2020 ◽  
Vol 10 (10) ◽  
pp. 1784
Author(s):  
Xueying Zhang ◽  
Xinxin Liu ◽  
Fadi Li ◽  
Xiangpeng Yue
Keyword(s):  
Milk Proteins ◽  
Differentially Expressed ◽  
Cell Organelle ◽  
Hippo Signaling ◽  
Lactation Period ◽  
Biological Functions ◽  
Two Dimensional Gel Electrophoresis ◽  
Go Annotation ◽  
Extracellular Region ◽  
Hu Sheep

Colostrum and milk proteins are essential resources for the growth and development of the newborns, while their kinds and amounts vary greatly during the lactation period. This study was conducted to better understand whey proteome and its changes at six lactation time points (0 d, 3 d, 7 d, 14 d, 28 d, and 56 d after lambing) in Hu sheep. Using two-dimensional gel electrophoresis (2-DE) and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI TOF/TOF MS) technologies, a total of 52 differentially expressed protein spots (DEPS), corresponding to 25 differentially expressed proteins (DEPs), were obtained. The protein spots abundance analysis revealed that the proteins are the most abundant at 0 d after lambing. Gene ontology (GO) annotation and Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway analysis were used to explore the biological functions of the DEPs. The biological process was mainly involved in localization, the single-organism process, the cellular process, and a series of immune processes. The cellular components engaged in the extracellular region were the cell, organelle, and membrane. The most prevalent molecular function was binding activity. In addition, the DEPs were involved in nine significant pathways, including the Hippo signaling pathway and Complement and coagulation cascades. These results intuitively presented the changes in Hu sheep whey proteins during a 56-d lactation period, and revealed potential biological functions of the DEPs, providing a scientific basis for early weaning.

Lateral Force Transmission Across Costameres in Skeletal Muscle

2003 ◽  
Vol 31 (2) ◽  
pp. 73-78 ◽  
Author(s):  
Robert J. Bloch ◽  
Hugo Gonzalez-Serratos
Keyword(s):  
Skeletal Muscle ◽  
Lateral Force ◽  
Force Transmission
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