Annexins and Membrane Repair Dysfunctions in Muscular Dystrophies

Croissant, Coralie; Carmeille, Romain; Brévart, Charlotte; Bouter, Anthony

doi:10.3390/ijms22105276

Cited by 25 publications

(26 citation statements)

References 136 publications

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“…Part of ANXA1 may therefore dissociate from the wounding site. ANXA1 has been described as a crucial component in the lipid patch, acting for the aggregation of intracellular vesicles [3], whereas ANXA6 may interact with the damaged sarcolemma, probably to induce the membrane remodeling responsible for membrane resealing [17]. Our data support this hypothesis, since ANXA1, interacting with intracellular vesicles and located inside the cell after membrane repair, may be released from the wounding site to return to the cytoplasm.…”

Section: Kinetics Of Anx Recruitment To the Site Of Membrane Injurysupporting

confidence: 77%

“…Key membrane repair proteins, such as dysferlin [19], MG-53 [34] or ANX [3,14] are rapidly recruited to the membrane disruption site in damaged skeletal muscle cells. While most previous studies have been performed in mouse or fish, we investigated the trafficking of ANXA1, ANXA2 and ANXA4 fused to GFP in laser-damaged human LHCN myotubes.…”

Section: Trafficking Of Anx After Sarcolemma Injurymentioning

confidence: 99%

“…Cells from tissues, such as skeletal or cardiac muscle, gut epithelium or vascular endothelium, are exposed to mechanical stress, which often induces the formation of tears in their plasma membrane [1]. Normal cells are able to repair these ruptures at the minute scale, through a coordinated Ca 2+ -dependent response, including intracellular vesicle recruitment and cell membrane remodeling, driven by a protein machinery that involves dysferlin, MG-53, AHNAK and ANX [2,3]. ANX (12 members in humans) are proteins that share the property of binding to negatively charged lipid membranes, principally those containing phosphatidylserine, in a Ca 2+ -dependent manner [4].…”

Section: Introductionmentioning

confidence: 99%

“…Defective membrane repair leads to cell death and may contribute to the development of degenerative diseases, such as muscular dystrophies [3,19,20]. Major attention has therefore focused on membrane repair in skeletal muscle cells.…”

Section: Introductionmentioning

confidence: 99%

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Trafficking of Annexins during Membrane Repair in Human Skeletal Muscle Cells

et al. 2022

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Defects in membrane repair contribute to the development of muscular dystrophies, such as Miyoshi muscular dystrophy 1, limb girdle muscular dystrophy (LGMD), type R2 or R12. Deciphering membrane repair dysfunctions in the development of muscular dystrophies requires precise and detailed knowledge of the membrane repair machinery in healthy human skeletal muscle cells. Using correlative light and electron microscopy (CLEM), we studied the trafficking of four members of the annexin (ANX) family, in myotubes damaged by laser ablation. Our data support a model in which ANXA4 and ANXA6 are recruited to the disruption site by propagating as a wave-like motion along the sarcolemma. They may act in membrane resealing by proceeding to sarcolemma remodeling. On the other hand, ANXA1 and A2 exhibit a progressive cytoplasmic recruitment, likely by interacting with intracellular vesicles, in order to form the lipid patch required for membrane resealing. Once the sarcolemma has been resealed, ANXA1 is released from the site of the membrane injury and returns to the cytosol, while ANXA2 remains accumulated close to the wounding site on the cytoplasmic side. On the other side of the repaired sarcolemma are ANXA4 and ANXA6 that face the extracellular milieu, where they are concentrated in a dense structure, the cap subdomain. The proposed model provides a basis for the identification of cellular dysregulations in the membrane repair of dystrophic human muscle cells.

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Section: Kinetics Of Anx Recruitment To the Site Of Membrane Injurysupporting

confidence: 77%

Section: Trafficking Of Anx After Sarcolemma Injurymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Trafficking of Annexins during Membrane Repair in Human Skeletal Muscle Cells

et al. 2022

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“…Reduction of ANXA6 inhibits the aggregation of ANXA1, ANXA2, and ANXA5, thus negatively affecting the repair process [ 79 ]. Moreover, an excess of ANXA2 that leaks from injured myofibers can activate muscle-resident fibro-adipogenic precursors that differentiate into adipocytes which gradually lead to muscle degeneration [ 80 ].…”

Section: Discussionmentioning

confidence: 99%

Age-Related Changes in the Matrisome of the Mouse Skeletal Muscle

Lofaro

Cisterna

Lacavalla

et al. 2021

IJMS

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Aging is characterized by a progressive decline of skeletal muscle (SM) mass and strength which may lead to sarcopenia in older persons. To date, a limited number of studies have been performed in the old SM looking at the whole, complex network of the extracellular matrix (i.e., matrisome) and its aging-associated changes. In this study, skeletal muscle proteins were isolated from whole gastrocnemius muscles of adult (12 mo.) and old (24 mo.) mice using three sequential extractions, each one analyzed by liquid chromatography with tandem mass spectrometry. Muscle sections were investigated using fluorescence- and transmission electron microscopy. This study provided the first characterization of the matrisome in the old SM demonstrating several statistically significantly increased matrisome proteins in the old vs. adult SM. Several proteomic findings were confirmed and expanded by morphological data. The current findings shed new light on the mutually cooperative interplay between cells and the extracellular environment in the aging SM. These data open the door for a better understanding of the mechanisms modulating myocellular behavior in aging (e.g., by altering mechano-sensing stimuli as well as signaling pathways) and their contribution to age-dependent muscle dysfunction.

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FLIM‐FRET‐based analysis of S100A11/annexin interactions in living cells

Melle,

Hoffmann,

Wiesenburg

et al. 2024

FEBS Open Bio

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Proteins achieve their biological functions in cells by cooperation in protein complexes. In this study, we employed fluorescence lifetime imaging microscopy (FLIM)‐based Förster resonance energy transfer (FRET) measurements to investigate protein complexes comprising S100A11 and different members of the annexin (ANX) family, such as ANXA1, ANXA2, ANXA4, ANXA5, and AnxA6, in living cells. Using an S100A11 mutant without the capacity for Ca2+ binding, we found that Ca2+ binding of S100A11 is important for distinct S100A11/ANXA2 complex formation; however, ANXA1‐containing complexes were unaffected by this mutant. An increase in the intracellular calcium concentration induced calcium ionophores, which strengthened the ANXA2/S100A11 interaction. Furthermore, we were able to show that S100A11 also interacts with ANXA4 in living cells. The FLIM‐FRET approach used here can serve as a tool to analyze interactions between S100A11 and distinct annexins under physiological conditions in living cells.

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Annexins and Membrane Repair Dysfunctions in Muscular Dystrophies

Cited by 25 publications

References 136 publications

Trafficking of Annexins during Membrane Repair in Human Skeletal Muscle Cells

Trafficking of Annexins during Membrane Repair in Human Skeletal Muscle Cells

Age-Related Changes in the Matrisome of the Mouse Skeletal Muscle

FLIM‐FRET‐based analysis of S100A11/annexin interactions in living cells

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