Dystrophin - an overview | ScienceDirect Topics (2023)

Dystrophin is an important structural protein in many tissues, including skeletal muscle, cardiac muscle, and the brain.

Of:Neurology Secrets (Fifth Edition), 2010

Related terms:

  • exon
  • actin
  • distroglicano
  • Skeletal muscle
  • nested gene
  • glycoprotein
  • phenotype
  • Mutation
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Skeletal muscle disorders

Dr. Joseph Jankovic, emBradley and Daroff Neurology in Clinical Practice, 2022

Dystrophin deficiency (Duchenne muscular dystrophy, Becker muscular dystrophy, and atypical forms)

Absence or deficiency ofdystrophinit is responsible for two disorders that cause progressive muscle destruction. The absence of dystrophin impairs the integrity of the sarcolemma membrane, making it susceptible to mechanical damage. Molecules such as calcium can gain access to the fiber, initiating a chain of destructive processes that lead to muscle fiber necrosis. Eventually, this process leads to severe muscle wasting and the replacement of muscle fibers with fibrous tissue.

The responsible gene is located on the short arm of the X chromosome at the Xp21 locus. The gene is extremely large, comprising more than 2.5 million base pairs and 79 exons, or coding regions. Approximately 65% ​​to 75% of cases are associated with a deletion or duplication of one or more exons in the gene. Genetic testing assays designed to detect deletions and duplications, such as multiplex ligation-dependent probe amplification (MLPA) and microarray-based comparative genomic hybridization (CGH) should first be used (Hegde MR et al., 2008;Sansovic et al., 2013). There are "hot spots" for these gene deletions, mainly between exons 43 and 52 and particularly 44 and 49 (Noble et al., 1997). The remaining 25% to 35% of cases are due to point mutations (many of which introduce a premature stop codon), minor deletions, or small insertions or duplications, best detected by next-generation sequencing. Whether an exclusion is inside or outside the frame (seechapter 48) determines if dystrophin is absentmuscle or present in a reduced altered form. This is of clinical importance because the former is usually associated with severe DMD, while the latter can cause a milder Becker variant (BMD). In BMD, the abnormal dystrophin retains enough function to slow the progression of the disease. The reading of the DNA code is trio by trio. Maintenance of this reading frame across the gene is necessary for dystrophin production. If a deletion removes a multiple of three base pairs, the reading frame may be intact upstream and downstream and may have limited meaning, as if the sentence "You can't eat the cat" were changed to "You can't eat the cat." cat". ". cat" and some modified dystrophin can be formed. This is often the situation in the mild form of dystrophin deficiency (BMD). In the severe form, the reading frame is destroyed, as if a deletion would result in the phrase "Yoc ann ote att hec at". There are exceptions to this rule, as frameshift deletions have been associated with the milder form of the disease, particularly at the 5' end of the gene in exons 3-7. The prevalence of DMD in the general population is approximately 3 per 100,000, and the incidence among male live births is 1 per 3,500. BMD is about one tenthso common Although inheritance is clearly X-linked recessive, almost a third of cases are sporadic. Presumably this is due to a spontaneous mutation that occurs in the child or in the mother's eggs.

Structural Proteins | Dystrophin: a multifaceted protein essential for muscle health

D'anna M. Nelson, James M. Ervasti, arribaEncyclopedia of Biological Chemistry (Third Edition), 2021


dystrophinit is a large 427 kDa cytoligand protein that connects the interior of the cell with the extracellular matrix. Although expressed in many tissues in the body, dystrophin has the critical function of stabilizing the muscle membrane (sarcolemma) during muscle contraction, and its absence results in Duchenne muscular dystrophy (DMD). Dystrophin's cytoligand function is primarily performed by two dystrophin domains. The N-terminal domain binds to filamentous actin within the cell, while the dystrophin- and cysteine-rich domain binds to β-dystroglycan embedded in the sarcolemma. β-dystroglycan further associates with α-dystroglycan which binds to the extracellular matrix and completes the transmembrane connection of intracellular actin to the extracellular matrix.blakeand another., 2002; Guiraudand another., 2015). Dystrophin and dystroglycans, as well as other integral membrane proteins such as sarcoglycans and sarcospan, form a complex known as the dystrophin glycoprotein complex (DGC).Extracted from Sonnemann, 2008). Dystrophin and DGC further associate with many additional proteins, such as microtubules, intermediate filaments, and neuronal nitric oxide synthase (nNOS), which allow dystrophin to have a broad influence on the cytoskeleton and signaling pathways.allenand another., 2016).

Dystrophin plays a critical role in muscle structure and function, and its absence results in DMD, a disabling and ultimately fatal disease. Most current clinical strategies, such as steroids and respiratory support, only improve disease pathology in the short term.Flanigan, 2014). Currently, there are 3 strategies to restore the dystrophin protein that have been successful in clinical trials: gene therapy, exon skipping, and stop codon reading (Shieh, 2018). However, in most cases, these therapeutic strategies do not completely recapitulate endogenous dystrophin, but instead restore dystrophin expression with small or large internal deletions. As highlighted in this review, recent studies are expanding our knowledge of the many binding partners of dystrophin and the functional significance of these interactions. Dystrophin therapeutic proteins with internal deletions are likely to compromise dystrophin function. In the effort to develop therapies to prevent or delay the fatality of DMD, there has never been a more critical time to consider what functions of dystrophin are essential for healthy muscle.

In this article, we review the domain structure of dystrophin, its interaction partners, truncated dystrophin isoforms, dystrophin-related diseases, and therapeutic strategies to restore or replace dystrophin.

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(Video) Duchenne & Becker muscular dystrophy - causes, symptoms, treatment & pathology


The molecular, biochemical and cellular bases of genetic diseases

Robert L. Nussbaum MD, FACP, FACMG, emThompson & Thompson Genetics in Medicine, 2016

Dystrophin glycoprotein complex (DGC).

dystrophinit is a structural protein that anchors the DGC to the cell membrane. DGC is a veritable constellation of polypeptides associated with a dozen genetically distinct muscular dystrophies (Figure 12-20). This complex serves several important functions. First, it is believed to be essential for maintaining the integrity of the muscle membrane by linking the actin cytoskeleton to the extracellular matrix. Second, it is necessary to position the proteins of the complex in the sarcolemma. Although the function of many of the proteins in the complex is unknown, their association with muscle disease indicates that they are essential components of the complex. Mutations in several of these proteins cause autosomal recessive muscular dystrophies and other congenital muscular dystrophies.Figure 12-20).

The fact that each component of CGD is affected by mutations that cause other types of muscular dystrophies underscores the principle that no protein functions in isolation, but rather is a component of a biological pathway or multiprotein complex. Mutations in genes encoding other components of a pathway or complex often lead to genocopies, as we saw earlier in the case of CF.

Treatment and Management of Muscular Dystrophies

Diana M. Escolar MD, ... Robert Leshner MD, INeuromuscular disorders: treatment and management, 2011

mechanical fragility of the membrane

dystrophinIt is a link between the intracellular cytoskeleton and the extracellular matrix. The carboxy terminus of dystrophin is attached to the sarcolemma, the surface membrane of striated muscle cells,67–70binding to β-dystroglycan71and through it to other glycoproteins associated with dystrophin and α-dystroglycan, which binds the sarcolemma to the extracellular matrix.72When dystrophin is not present, disconnection of β-dystroglycan contractile proteins results in loss of β- and α-dystroglycan and CGD from the sarcolemma. This disruption results in membrane embrittlement and abnormal permeability, particularly to calcium ions.

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Neuromuscular disorders, including malignant hyperthermia and other genetic disorders

Michael A. Gropper MD, PhD, emAnesthesia by Miller, 2020

Duchenne muscular dystrophy and Becker muscular dystrophy

Duchenne muscular dystrophy (DMD) is the most common and severe type of muscular dystrophy, with an incidence of 1 per 3,500 male live births.277and a total male prevalence of about 50 to 60 × 10–6.278Becker muscular dystrophy (MBD) is relatively rare, with an incidence of approximately 1 in18,000 male live births and a prevalence of 23.8 × 10–6.278Both DMD and BMD are X-linked recessive diseases. The defect is located on the short arm of the X chromosome, in the Xp21 region, which contains the gene for the large protein Dp427, also known asdystrophin. The dystrophin gene is 2500 kilobases long with more than 70 exons.278Dystrophin is distributed not only in skeletal, cardiac, and smooth muscle, but also in the brain.279Due to the large size of the dystrophin gene, spontaneous new mutations are common, accounting for one third of new cases.280

The most common form of mutation is a deletion within the gene (65%-70% of DMD cases and >80% of MBD). Duplication and point mutations account for the rest. It also appears that there are "hot spots" in the first 20 exons and in the central region of the gene (exons 45-55) where deletions and duplications are likely to occur.278Female cases of DMD with 45,X and 46,XX karyotypes have been reported. The disease mechanism for the female 46,XX karyotype was thought to be preferential loss of the paternal X chromosome due to postzygotic nondisjunction and manifestation of the DMD gene from the maternal X chromosome in muscle cells.281BMD is generally milder in severity than DMD because the disruption of the translation process occurs in the relatively distal part of the gene, leading to a reduced amount of truncated dystrophin protein.278.282

Dystrophin, along with dystrophin-associated glycoproteins (DAGs), is involved in the stability of the sarcolemma. Dystrophin is responsible for maintaining the integrity of the muscle membrane, despite the fact that it represents only about 0.002% of the protein in skeletal muscle.283Dystrophin aggregates and binds to actin (at its N-terminus) and the DAG complex (at its C-terminus) to form a stable structure that interacts with laminin in the extracellular matrix.Figure 35.4). The lack or dysfunction of dystrophin leads to cell and membrane instability, with progressive leakage of intracellular components and elevation of creatine phosphokinase (CPK) levels. Eventually, the damaged muscle cell units are invaded by macrophages and destroyed. The current study suggests that cytotoxic T cells are likely to be to blame. Consequently, clinical muscular pseudohypertrophy occurs when layers of dead muscle are replaced by fibrofatty infiltrates. The loss of muscle units is responsible for weakness and contracture.279

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(Video) Duchenne Muscular Dystrophy

Muscle and nerve development in health and disease.

Jeremy K. Deisch, emSwaiman's Pediatric Neurology (Sixth Edition), 2017


dystrophinit is a 427 kilodalton protein that constitutes 0.01% of the total muscle protein and 5% of the proteins of the sarcolemma cytoskeleton. Dystrophin is located on the inside of the sarcolemma and is abundant at the myotendinous junction and at the postsynaptic membrane of the neuromuscular junction. Dystrophin forms an integral part of the cytoskeleton of a muscle and links the contractile apparatus to the sarcolemma. The N-terminus is the actin-binding domain, and the carboxy-terminal domain interacts with β-dystroglycan, as well as dystrobrevin and syntrophin. The central domain of the rod comprises most of the mass of the dystrophin molecule, forming a flexible rod-like structure. The fourth cysteine-rich domain also binds β-dystroglycan. The dystrophin-glycoprotein complex consists of numerous proteins, including dystroglycans (α and β), sarcoglycans (α, β, γ, δ, ε), sarcospan, syntrophin, and dystrobrevin. Peripheral members of the complex include neuronal nitric oxide synthase, caveolin, laminin, and merosin.

The DMD gene encoding the dystrophin protein is located on the short arm of the X chromosome, near the Xp21 region. The dystrophin gene is the largest gene identified to date, spanning more than 2.5 megabases (Mb) and containing at least 79 exons; the high rate of spontaneous mutation is a reflection of the large size of the gene. Dystrophin is expressed primarily in skeletal, cardiac, and smooth muscle cells, with smaller amounts expressed in the brain and retina. Dystrophin isoforms, which are smaller in size, are expressed in almost all tissues examined. Dystrophin in the brain is important in the maintenance of synapses; Deficiency of the brain dystrophin isoform is associated with the cognitive deficits seen in patients with dystrophin mutations. Deletions or abnormalities of the dystrophin gene cause an absence or deficiency of dystrophin, resulting in X-linked Duchenne and Becker muscular dystrophies.chapter 146).

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viral infections of the heart

Kirk U. Knowlton, Hervé Duplain, emMolecular Basis of Cardiovascular Disease (Second Edition), 2004


dystrophinis a rod-shaped subsarcolemmal protein that stabilizes the sarcolemma by linking the actin cytoskeleton to the extracellular matrix via the dystrophin-associated glycoprotein complex.125This connection protects muscle cells from contraction-induced damage.179Enteroviruses are normally released from the cell by rupture of the cell membrane or by cell lysis.107Consistent with these concepts, dystrophin deficiency has been shown in mice to predispose to cardiac cytopathic effects induced by Coxsackie virus and lead to increased virus replication in the hearts of dystrophin-deficient animals.113In addition, cell culture experiments showed that dystrophin expression protected against Coxsackie virus-mediated cell damage.113The markedly increased susceptibility of dystrophin-deficient mice to viral infection of the heart suggests that one of the mechanisms for increased cardiomyopathy in Duchenne muscular dystrophy is through increased susceptibility to viral infection of the heart. heart.

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Muscular dystrophy, Becker and Duchenne

AA. Beloved, inEncyclopedia of Neurological Sciences (Second Edition), 2014

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Dystrophin-associated proteins/glycoproteins

dystrophinit is closely associated with a large oligomeric group of sarcolemmal proteins in a complex known as the dystrophin-glycoprotein complex (DGC).Figure 1). DGC is made up of dystrophin, syntrophin complex, dystroglycan complex, and sarcoglycan complex. The dystroglycan complex is composed of a transmembrane glycoprotein, β-dystroglycan, that binds dystrophin, and an extracellular glycoprotein, α-dystroglycan, that binds α-laminin in the basement membrane. The sarcoglycan complex includes four transmembrane proteins: α-sarcoglycan, formerly known as adhalin; β-sarcoglycan; y-sarcoglycan; and δ-sarcoglycan. In addition, there is a transmembrane protein, sarcospan, which couples with the sarcoglycan complex. The sarcoglycan complex associates with the cysteine-rich domain or the first carboxy-terminal half of dystrophin, either directly or indirectly through the dystroglycan complex. The exact relationship between the sarcoglycan complex and the dystrophin-dystroglycan complex is not clear. It is now known that mutations in the various genes encoding the different CGD proteins are responsible for most forms of muscular dystrophy.tabla 1).

Dystrophin - an overview | ScienceDirect Topics (1)

Figure 1. The dystrophin-glycoprotein complex and related proteins. The dystrophin-glycoprotein complex and related proteins are important in the structural integrity of the sarcolemma membrane. Mutations in genes encoding various subunits of the complex are responsible for many forms of muscular dystrophy. DG, dystroglycan; SG, sarcoglycan. Reprinted with permission from Cohn RD and Campbell KP (2000) Molecular basis of muscular dystrophies.muscles and nerves23: 1456-1471.

tabla 1. Molecular defects of muscular dystrophies

X-linked recessive dystrophies
Autosomal dominant dystrophies
LGMD-1B with heart disease/AD-EDMD1q11–12air conditioning nuclear blade
myotonic dystrophy19q13.2myotonin protein kinase
Myotonic dystrophy type 2/PROMM3qDM2
oculopharyngeal dystrophy14qPolyalanine-2 binding protein
Bethlem myopathy-121q22.3Collagen type VI (a1oa2subunits)
Bethlem myopathy-22q37Collagen type VI(a6subunits)
Autosomal recessive dystrophies
LGMD-2B/Miyoshi myopathy2p13dysferlin
LGMD-2H9q31–q33E3-ubiquitin ligase (TRIM-32)
LGMD-2I19q13.3fukutin Related Protein,FKRP1
Merosin negative classic type (CMD1)6q21–22merosine (a2subunit)
CMD319q13.3fukutin Related Protein,FKRP1
Tipo Fukuyama9q31–33fukutin
tipo Walker Warburg9q31–33?
CMD with stiff spine syndrome1p35–36selenoprotein

Abbreviations: AD, autosomal dominant; BMD, Becker muscular dystrophy; CMD, congenital muscular dystrophy; DMD, Duchenne muscular dystrophy; EDMD, Emery-Dreifuss muscular dystrophy; FSHD, facioscapulohumeral muscular dystrophy; LGMD, limb-girdle muscular dystrophy; MEB, muscle-eye-brain disease; POMGnT1,d-mannose β-1,2-norte- acetylglucosaminyltransferase.

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Basil T. Darras, ... Louis M. Kunkel, emNeuromuscular Disorders of Infancy, Childhood, and Adolescence (Second Edition), 2015


dystrophinis a rod-shaped molecule of 427kDa and can be readily detected on Western blots (immune blots) of 100 μg of total muscle protein derived from a small portion of a muscle biopsy using anti-dystrophin antibodies to the amino terminus, rod domain, and carboxy terminus. Dystrophin quantity and quality can be assessed visually or by densitometry. If the 427 kDa dystrophin protein is normal in size and quantity, the diagnosis of DMD or MBD can be excluded. More than 99% of DMD patients exhibit a complete or near complete absence of dystrophin in skeletal muscle biopsy specimens.24Most patients with BMD (about 85%) have dystrophin of abnormal molecular weight, lower (80%) or higher (5%) in cases of gene deletion or duplication, respectively; the amount of dystrophin is reduced to normal. However, about 15% of BMD patients have a reduced amount of normal-sized protein. The Western Blot test is highly specific, because patients with neuromuscular diseases other than DMD/BMD have normal dystrophin. Thus, dystrophin immunoblotting, in conjunction with immunostaining of muscle biopsy and other clinical and laboratory parameters, can be used to help predict the severity of the evolving muscular dystrophy phenotype.Table 30.2).92

Table 30.2. Genetic, clinical and pathological characteristics of dystrophinopathies

Typegene locationProteinInheritanceClinical featuresPathology
DuchenneXp21dystrophinXROnset: 2–5 yearssevere dystrophic changes
pseudohypertrophyComplete/almost complete absence of dystrophin by immunohistochemistrya
decreased IQ
commitment of the heart
rapid declineDystrophin 0-5% of the normal amountbby western transfera
Wheelchair confinement: 11–13 years or younger
Death: 15–30 years
IntermediaryXp21dystrophinXRintermediate severityDystrophin 5-20% of the normal amount by Western blot of muscle protein
Wheelchair confinement: 13-16 years
BeckerXp21dystrophinXROnset: 5-20 years or laterless marked changes
more benign courseNormal appearance or reduced intensity ± patchy dystrophin staining by immunohistochemistry
Wheelchair confinement: after 16 years
Normal or abnormal molecular weightCdystrophin, amount >20% by western blot

abbreviations: XR, X-linked recessive; IQ, intelligence quotient.

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It uses monoclonal antibodies against the carboxy-terminal, amino-terminal, and middle rod domains (antibody 6-10) of dystrophin.
The amount of dystrophin is expressed as a percentage of control values ​​(myosin standardized versus post-transfer with Coommasie stain).
The normal molecular weight is 427 kDa.

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Immunologization and structural configuration of membrane and cytoskeletal proteins involved in excitation-contraction coupling of cardiac muscle

Joy S. Frank, Alan Garfinkel, emThe Myocardium (Second Edition), 1997


dystrophinis a well-studied cytoskeletal protein that is most prominently expressed in skeletal and cardiac muscle.Hoffmannand another, 1987; Ahn and Kunkel, 1993). A large 400 kD protein, dystrophin is encoded by the Duchenne muscular dystrophy gene.Hoffman and Kunkel, 1989). Absent or greatly reduced dystrophin in muscle causes severe progressive skeletal damagemuscle weakness and may result in dilated cardiomyopathy. Lack of dystrophin expression also causes myopathy in mdx mice, a useful animal model for studying dystrophin function.

Recent analyzes of the complete amino acid sequence of the dystrophin molecule suggest strong structural homology to the core domain of spectrin.Koenigand another, 1988) and even more extensive sequence similarity to an α-actinin isoform (Koenigand another, 1988). Subcellular fractionation experiments and immunostaining studies clearly localize dystrophin as a network on the cytoplasmic side of the SL. Dystrophin exists in SL as a component of a large oligometric complex containing dystrophin-associated glycoproteins (DAG) and dystrophin-associated proteins (DAP) (Campbell and Kahl, 1989). Characterization of the dystrophin-glycoprotein complex produced a model (Figure 18) in which the amino-terminal domain of dystrophin is the cytoskeletal link between the subsarcolemmal actin cytoskeleton and the encompassing glycoprotein complexo SL (hemsand another, 1992;and another, 1994). The glycoprotein complex contains five glycoproteins that are attached to the cysteine-rich domain of dystrophin byb-dystroglycan. Located on the surface of the sarcolemma,a-Dystroglycan binds to dystrophin via the transmembrane glycoprotein complex and to the extracellular matrix via binding to merosin (muscular isoform of laminin) with high affinity in a calcium-dependent manner.Ervasti y Campbell, 1993). The link between the extracellular matrix and the cytoskeleton via dystroglycan bridges across the SL from the cytoplasmic side to the extracellular matrix and is the basis for the proposed role of dystrophin in providing membrane stability.

Dystrophin - an overview | ScienceDirect Topics (2)

Figure 18. Membrane organization of the dystrophin-glycoprotein complex. This model shows all known components of the dystrophin-glycoprotein complex in their structural associations with SL and the extracellular matrix. Five glycoproteins span the membrane to bind a-dystroglycan to dystrophin. The binding of α-dystroglycan to the extracellular matrix is ​​carried out through merosin.

(Reproduced with permission fromCampbell, 1995.)

Dystrophin is found in both skeletal and cardiac muscle along the peripheral SL.francoand another, 1994; Arahataand another, 1988; Byersand another, 1991; Klietchand another, 1993), consistent with its role as part of a transsarcolemmal bridging structure. In skeletal muscle, most biochemical and immunocytochemical reports agree that dystrophin is not present in the T tubular portion of the SL. This difference in dystrophin distribution between peripheral SL and tubular T SL is consistent with previous studies demonstrating that in skeletal muscle the peripheral T and SL tubules have distinct ultrastructural features, contain several unique proteins, and appear to perform different functions at least relative to with E-C coupling. .

In most cardiac myocytes, dystrophin is present and abundant in both the peripheral SL and the T tubular membrane.Figura 19A) (francoand another, 1994; Klietschand another, 1993). In experiments performed to determine the location of dystrophin during development in rabbit cardiomyocytes, it appears that dystrophin is present in association with the T tubular membrane as it develops.Fig. 19B y C) (francoand another, 1994).Klietschand another(1993)demonstrated that in cardiac muscle dystrophin-associated proteins, dystrophin and laminin (merosin) co-distribute to the peripheral membranes of the SL and T tubule. However, there may be tissue-species differences in dystrophin localization. . For example, studies in rat and mouse ventricular myocytes report strong immunostaining for dystrophin in the peripheral SL, but no staining in the T tubules.Byersand another, 1991). More recent studies support the absence of detectable dystrophin in mouse T tubules, but find a low level of dystrophin in mouse T tubules.Millerand another, In the press). The complexities about the subcellular localization of dystrophin are not well understood because the role of dystrophin in cardiomyocytes is still unclear. Dystrophin can play several roles through its various associations. Recent work in cardiac cells shows that a significant portion (~35%) of dystrophin is found in the Z disc myofibrils (Mengand another, 1996). The function of this unique non-membrane location of dystrophin is unknown, although the myofibrillar dystrophin hypothesis is central to the maintenance of sarcomeric structure. Variations in the distribution of dystrophin along the SL of different cardiac speciessuggest that dystrophin functions may also vary by species. Although the dystrophin-glycoprotein complex is believed to play an important role in SL stabilization and protection against mechanical stress during muscle contraction, dystrophin also appears to play a unique role in signal transduction, associating directly with oxidation. nitric synthase and localizing it for SL.Brenmannand another, 1995). Although the role of dystrophin along the T-tubules of cardiomyocytes is still uncertain, it is possible that dystrophin plays a role in maintaining a heterogeneous domain arrangement for some of the membrane glycoproteins. In this capacity, dystrophin could play a role in maintaining a non-uniform distribution of ion channels or cell surface receptors. This would be analogous to the role played by ankyrins in the membrane. In fact, the relationship of these cytoskeletal proteins, both located below the SL, requires further study.

Dystrophin - an overview | ScienceDirect Topics (3)

Figure 19.Dystrophin immunolocalization in rabbit myocytes. (A) Confocal micrograph of an adult myocyte labeled with anti-dystrophin antibodies. Note the uniform labeling of the peripheral SL and T tubules and the lack of labeling in the intercalated discs (cell ends). Original magnification x1140. (B) Confocal micrographs of 4-day-old rabbit myocytes labeled with anti-dystrophin antibodies. At this stage of development, dystrophin staining is intense but somewhat discontinuous along the cell periphery. There is no marking inside the cell, since the T tubules are absent. Original magnification x2760. (C) Confocal micrograph of a 1-week-old rabbit myocyte. Antidystrophin antibody labeling is present as intense fluorescence on the peripheral cell membrane and in developing T-tubules, seen here as short projections from the cell surface into the cytoplasm. Original enlargement xl065.

(Reproduced with permission fromfrancoand another, 1994.)

In summary, cytoskeletal proteins have many functions in cardiac muscle, including the structure of intracellular organelles, especially the sarcomeric units of the muscle; stabilize the SL at intercellular binding sites such as the intercalated disc or attach sarcomeres to the extracellular matrix in Z lines; and, most importantly, form cytoskeletal membrane junctions to integral membrane proteins. This binding of the cytoskeleton directly or through associated cytoskeletal proteins, such as ankyrin, can bind channels, exchangers, and receptors to form regional specializations within the membrane.

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