Related Experiment Video

Updated: Aug 31, 2026

Cell Membrane Repair Assay Using a Two-photon Laser Microscope
06:35

Cell Membrane Repair Assay Using a Two-photon Laser Microscope

Published on: January 2, 2018

Dysferlin interacts with annexins A1 and A2 and mediates sarcolemmal wound-healing

Niall J Lennon1, Alvin Kho, Brian J Bacskai

  • 1Day Neuromuscular Research Laboratory, Massachusetts General Hospital, Charlestown, Massachusetts 02129, USA.

The Journal of Biological Chemistry
|September 25, 2003
PubMed

Insights

Dysferlin protein interacts with annexins A1 and A2 to repair muscle membrane injuries. This discovery offers new insights into muscular dystrophies and potential therapeutic targets.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Genetics

Background:

  • Mutations in the dysferlin gene are linked to limb girdle muscular dystrophy type 2B and Miyoshi myopathy.
  • Understanding the molecular mechanisms underlying muscle membrane repair is crucial for developing effective treatments.

Purpose of the Study:

  • To investigate the interaction between dysferlin and Ca2+-binding proteins, annexins A1 and A2.
  • To elucidate the role of dysferlin in Ca2+-dependent sarcolemmal repair.

Main Methods:

  • Expression profile analyses in dysferlinopathic mice.
  • Co-immunofluorescence and co-immunoprecipitation assays.
  • Fluorescence lifetime imaging microscopy (FLIM).

Main Results:

  • Dysferlin interacts with annexins A1 and A2 in a Ca2+ and membrane injury-dependent manner.
  • Dysferlin facilitates Ca2+-dependent sarcolemmal repair via vesicle fusion.
  • Annexin distribution and muscle wound-healing efficiency are impaired in dysferlin-deficient muscle.

Conclusions:

  • Dysferlin plays a key role in muscle membrane healing through a mechanism involving annexins A1 and A2.
  • Annexins A1 and A2 are identified as potential therapeutic targets for muscular dystrophies.
  • This study provides a novel model for muscle membrane repair relevant to both normal and diseased muscle.

More Related Videos

DNA Electroporation, Isolation and Imaging of Myofibers07:52

DNA Electroporation, Isolation and Imaging of Myofibers

Published on: December 23, 2015

A Thermoplasmonic Approach for Investigating Plasma Membrane Repair in Living Cells and Model Membranes06:32

A Thermoplasmonic Approach for Investigating Plasma Membrane Repair in Living Cells and Model Membranes

Published on: January 19, 2024

Related Concept Videos

Desmosomes01:05

Desmosomes

The term desmosome derives from the Greek words "desmo" and "soma" meaning "adhesion bodies." This structure was first observed during the late 1800s and described as small, dense nodules in the epidermis. Desmosomes are button-like structures that help form an interlinked network of intermediate filaments across the cells. These junctions are  essential to hold cells together under mechanical stress and to maintain tissue integrity. Desmosomes are multi-protein complexes comprising desmosomal...
Anchoring Junctions01:03

Anchoring Junctions

Anchoring junctions are multiprotein complexes that help cells connect to other cells and the extracellular matrix. Anchoring junctions are present on the lateral and basal surfaces of cells, providing strong and flexible connections. Focal adhesions are often formed due to cell interactions with the ECM substrata, which initiate signal transduction via kinase cascades and other mechanisms. Together, they provide stability and tissue integrity. There are three types of anchoring junctions:...
Fibronectins Connect Cells with ECM01:25

Fibronectins Connect Cells with ECM

Fibronectin is an adhesive glycoprotein present in the extracellular matrix of embryogenic and adult tissue. These molecules primarily aid in regulating cell motility and attachment. A fibronectin molecule is composed of two identical polypeptide chains attached to each other by a pair of disulfide bonds at the C-terminal.
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Actin Filament Depolymerization01:19

Actin Filament Depolymerization

Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...
Fibril-associated Collagen01:11

Fibril-associated Collagen

Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...