scholarly journals Annexin-A6 in Membrane Repair of Human Skeletal Muscle Cell: A Role in the Cap Subdomain

Cells ◽  
2020 ◽  
Vol 9 (7) ◽  
pp. 1742 ◽  
Author(s):  
Coralie Croissant ◽  
Céline Gounou ◽  
Flora Bouvet ◽  
Sisareuth Tan ◽  
Anthony Bouter

Defects in membrane repair contribute to the development of some muscular dystrophies, highlighting the importance to decipher the membrane repair mechanisms in human skeletal muscle. In murine myofibers, the formation of a cap subdomain composed notably by annexins (Anx) is critical for membrane repair. We applied membrane damage by laser ablation to human skeletal muscle cells and assessed the behavior of annexin-A6 (AnxA6) tagged with GFP by correlative light and electron microscopy (CLEM). We show that AnxA6 was recruited to the site of membrane injury within a few seconds after membrane injury. In addition, we show that the deficiency in AnxA6 compromises human sarcolemma repair, demonstrating the crucial role played by AnxA6 in this process. An AnxA6-containing cap-subdomain was formed in damaged human myotubes in about one minute. Through transmission electron microscopy (TEM), we observed that extension of the sarcolemma occurred during membrane resealing, which participated in forming a dense lipid structure in order to plug the hole. By properties of membrane folding and curvature, AnxA6 helped in the formation of this tight structure. The compaction of intracellular membranes—which are used for membrane resealing and engulfed in extensions of the sarcolemma—may also facilitate elimination of the excess of lipid and protein material once cell membrane has been repaired. These data reinforce the role played by AnxA6 and the cap subdomain in membrane repair of skeletal muscle cells.

2016 ◽  
Vol 1863 (9) ◽  
pp. 2267-2279 ◽  
Author(s):  
Romain Carmeille ◽  
Flora Bouvet ◽  
Sisareuth Tan ◽  
Coralie Croissant ◽  
Céline Gounou ◽  
...  

2011 ◽  
Vol 301 (5) ◽  
pp. E1013-E1021 ◽  
Author(s):  
Frode Norheim ◽  
Truls Raastad ◽  
Bernd Thiede ◽  
Arild C. Rustan ◽  
Christian A. Drevon ◽  
...  

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.


2012 ◽  
Vol 2012 ◽  
pp. 1-12 ◽  
Author(s):  
Nataša Nikolić ◽  
Magdalena Rhedin ◽  
Arild C. Rustan ◽  
Len Storlien ◽  
G. Hege Thoresen ◽  
...  

We investigated the effects of PGC-1α(peroxisome proliferator-activated receptorγcoactivator-1α) overexpression on the oxidative capacity of human skeletal muscle cellsex vivo. PGC-1αoverexpression increased the oxidation rate of palmitic acid and mRNA expression of genes regulating lipid metabolism, mitochondrial biogenesis, and function in human myotubes. Basal and insulin-stimulated deoxyglucose uptake were decreased, possibly due to upregulation of PDK4 mRNA. Expression of fast fiber-type gene marker (MHCIIa) was decreased. Compared to skeletal musclein vivo, PGC-1αoverexpression increased expression of several genes, which were downregulated during the process of cell isolation and culturing. In conclusion, PGC-1αoverexpression increased oxidative capacity of cultured myotubes by improving lipid metabolism, increasing expression of genes involved in regulation of mitochondrial function and biogenesis, and decreasing expression of MHCIIa. These results suggest that therapies aimed at increasing PGC-1αexpression may have utility in treatment of obesity and obesity-related diseases.


2018 ◽  
Author(s):  
S Höckele ◽  
P Huypens ◽  
C Hoffmann ◽  
T Jeske ◽  
M Hastreiter ◽  
...  

2021 ◽  
Vol 22 (10) ◽  
pp. 5276
Author(s):  
Coralie Croissant ◽  
Romain Carmeille ◽  
Charlotte Brévart ◽  
Anthony Bouter

Muscular dystrophies constitute a group of genetic disorders that cause weakness and progressive loss of skeletal muscle mass. Among them, Miyoshi muscular dystrophy 1 (MMD1), limb girdle muscular dystrophy type R2 (LGMDR2/2B), and LGMDR12 (2L) are characterized by mutation in gene encoding key membrane-repair protein, which leads to severe dysfunctions in sarcolemma repair. Cell membrane disruption is a physiological event induced by mechanical stress, such as muscle contraction and stretching. Like many eukaryotic cells, muscle fibers possess a protein machinery ensuring fast resealing of damaged plasma membrane. Members of the annexins A (ANXA) family belong to this protein machinery. ANXA are small soluble proteins, twelve in number in humans, which share the property of binding to membranes exposing negatively-charged phospholipids in the presence of calcium (Ca2+). Many ANXA have been reported to participate in membrane repair of varied cell types and species, including human skeletal muscle cells in which they may play a collective role in protection and repair of the sarcolemma. Here, we discuss the participation of ANXA in membrane repair of healthy skeletal muscle cells and how dysregulation of ANXA expression may impact the clinical severity of muscular dystrophies.


2003 ◽  
Vol 14 (15) ◽  
pp. 1473-1487 ◽  
Author(s):  
Martha Wootton ◽  
Karen Steeghs ◽  
Diana Watt ◽  
June Munro ◽  
Katrina Gordon ◽  
...  

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Ashok Kumar ◽  
Yashwant Kumar ◽  
Jayesh Kumar Sevak ◽  
Sonu Kumar ◽  
Niraj Kumar ◽  
...  

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