Dystrophin Sarcolemma
Dystrophin Sarcolemma - Related Videos
07:44
CRISPR/Cas9 Technology in Restoring Dystrophin Expression in iPSC-Derived Muscle Progenitors
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Cited by 6 •
2019
Here, we present a Cas9-based exon23 deletion protocol to restore dystrophin expression in iPSC from Dmdmdx mouse-derived skin fibroblasts and directly differentiate iPSCs into myogenic progenitor cells (MPC) using the Tet-on MyoD activation system.
10:30
Multi-exon Skipping Using Cocktail Antisense Oligonucleotides in the Canine X-linked Muscular Dystrophy
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Cited by 23 •
2016
Exon skipping is currently a most promising therapeutic option for Duchenne muscular dystrophy (DMD). To expand the applicability for DMD patients and to optimize the stability/function of the resulting truncated dystrophin proteins, a multi-exon skipping approach using cocktail antisense oligonucleotides was developed and we demonstrated systemic dystrophin rescue in a dog model.
07:52
DNA Electroporation, Isolation and Imaging of Myofibers
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Cited by 30 •
2015
This protocol utilizes electroporation to introduce and express fluorescently labeled proteins in mouse muscle fibers. Following recovery after electroporation, fibers are isolated. Individual fibers are then imaged using high resolution confocal microscopy to visualize muscle structure.
14:36
Evaluation of Muscle Function of the Extensor Digitorum Longus Muscle Ex vivo and Tibialis Anterior Muscle In situ in Mice
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Cited by 75 •
2013
Changes in limb muscle contractile and passive mechanical properties are important biomarkers for muscle diseases. This manuscript describes physiological assays to measure these properties in the murine extensor digitorum longus and tibialis anterior muscles.
07:28
Paraffin-Embedded and Frozen Sections of Drosophila Adult Muscles
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Cited by 42 •
2010
Identification of mechanisms underlying muscle damage is crucial. Here we present the histological technique for preparing paraffin-embedded and frozen sections of Drosophila thoracic muscles. This allows analysis of muscle morphology and localization of protein and other muscle cell components.
FAQs
During contraction, force generated within the fiber must be transmitted without overstressing the cell surface. Dystrophin’s intracellular connection to actin and its association with the dystrophin-glycoprotein complex provide a continuous route toward membrane-spanning proteins and the extracellular matrix. This arrangement distributes mechanical load across linked structures rather than leaving the sarcolemma to absorb contraction-related stress at isolated points.
Because dystrophin lies on the cytoplasmic side of the sarcolemma, it can connect internal actin filaments to the membrane-associated complex. Its position places it between the contractile apparatus and membrane-spanning components that connect outward to the extracellular matrix. This orientation explains how intracellular contraction is mechanically coupled to the cell surface and why disruption can compromise membrane stability.
Loss or defects in dystrophin weaken the mechanical support system rather than merely changing a soluble muscle component. With the actin-to-extracellular-matrix connection impaired, the sarcolemma becomes less able to withstand forces generated during contraction. The resulting membrane vulnerability helps explain why dystrophin abnormalities are associated with muscular dystrophies and why membrane integrity is central to their disease mechanisms.
Although skeletal and cardiac muscle fibers perform different physiological roles, dystrophin-dependent sarcolemmal stabilization is relevant to both. Studying the system in these two muscle contexts connects a shared structural principle with tissue-specific disease questions. Defects can therefore be considered in relation to the integrity of either muscle fiber type, rather than being treated as an issue limited to skeletal muscle.
Diagnostic research can use the dystrophin-sarcolemma system as a framework for interpreting muscular dystrophy mechanisms. The key question is how defects or loss affect the links among actin, the dystrophin-glycoprotein complex, membrane-spanning proteins, and the extracellular matrix. Focusing on these connections helps relate a molecular abnormality to weakened membrane integrity and the muscle-cell consequences described in the overview.
Therapeutic research can target the consequences of a weakened dystrophin system or seek strategies that preserve sarcolemmal integrity. The relevant outcome is not simply restoration of one protein, but improvement of the mechanical linkage connecting intracellular actin with extracellular support. This structural perspective helps evaluate whether a proposed strategy could reduce contraction-related membrane damage in skeletal and cardiac muscle fibers.