Affordable Access

deepdyve-link
Publisher Website

Membrane repair of human skeletal muscle cells requires Annexin-A5.

Authors
  • Carmeille, Romain1
  • Bouvet, Flora1
  • Tan, Sisareuth1
  • Croissant, Coralie1
  • Gounou, Céline1
  • Mamchaoui, Kamel2
  • Mouly, Vincent2
  • Brisson, Alain R1
  • Bouter, Anthony3
  • 1 Institute of Chemistry and Biology of Membranes and Nano-objects, UMR 5248, CNRS, University of Bordeaux, IPB, F-33600 Pessac, France.
  • 2 Sorbonne Universités, UPMC Univ Paris 06, Inserm UMRS974, CNRS FRE3617, Center for Research in Myology, 47 Boulevard de l'hôpital, 75013 Paris, France.
  • 3 Institute of Chemistry and Biology of Membranes and Nano-objects, UMR 5248, CNRS, University of Bordeaux, IPB, F-33600 Pessac, France. Electronic address: [email protected]
Type
Published Article
Journal
Biochimica et Biophysica Acta
Publisher
Elsevier
Publication Date
September 2016
Volume
1863
Issue
9
Pages
2267–2279
Identifiers
DOI: 10.1016/j.bbamcr.2016.06.003
PMID: 27286750
Source
Medline
Keywords
License
Unknown

Abstract

Defect in membrane repair contributes to the development of limb girdle muscular dystrophy type 2B (LGMD2B) and Miyoshi myopathy. In healthy skeletal muscle, unraveling membrane repair mechanisms requires to establish an exhaustive list of the components of the resealing machinery. Here we show that human myotubes rendered deficient for Annexin-A5 (AnxA5) suffer from a severe defect in membrane resealing. This defect is rescued by the addition of recombinant AnxA5 while an AnxA5 mutant, which is unable to form 2D protein arrays, has no effect. Using correlative light and electron microscopy, we show that AnxA5 binds to the edges of the torn membrane, as early as a few seconds after sarcolemma injury, where it probably self-assembles into 2D arrays. In addition, we observed that membrane resealing is associated with the presence of a cluster of lipid vesicles at the wounded site. AnxA5 is present at the surface of these vesicles and may thus participate in plugging the cell membrane disruption. Finally, we show that AnxA5 behaves similarly in myotubes from a muscle cell line established from a patient suffering from LGMD2B, a myopathy due to dysferlin mutations, which indicates that trafficking of AnxA5 during sarcolemma damage is independent of the presence of dysferlin.

Report this publication

Statistics

Seen <100 times