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Ordered disorder of the astrocytic dystrophin-associated protein complex in the norm and pathology.
Forced expression of embryonic dystrophin in zebrafish using an exon-skipping approach severely impairs the mobility and muscle architecture.
Spatio-temporal differences in dystrophin dynamics at mRNA and protein levels have been revealed using a novel reporter system.
Data indicate that ataluren (0.1-1 muM, 3-5 dpf) improved contractile function (~60% improvement of force at 0.5 muM) and dystrophin expression.
early expression of the short carboxyl-terminal dystrophin transcript, with expression of the full length muscle transcript occurring during myogenesis.
Data suggest that dystrophin functions in regulation of calcium signaling during early stages of slow muscle cell differentiation; calcium signaling in these cells coincide with first spontaneous contractions of embryonic trunk.
analysis of the dystrophin associated protein complex in zebrafish
Data suggest that the progressive muscle degeneration phenotype of dystrophin mutant zebrafish embryos is caused by the failure of embryonic muscle end attachments.
Dystrophin family gene expression in zebrafish is reported.
reduction of dystrophin, dystroglycan and sarcoglycan (显示 SGCD 蛋白) at translational level in embryos with overexpressed myostatin2
Dys protein regulates tarsal joint formation in response to Notch (显示 NOTCH1 蛋白) activity during Drosophila leg development.
The findings suggest that the signaling functions of Dystrophin protein are able to ameliorate dilated cardiomyopathy, and thus might help to improve heart muscle function in micro-Dystrophin-based gene therapy approaches.
Nrk, mbl, capt and Cam genetically interact with dystrophin and/or dystroglycan in the process of axon path-finding in the eye.
only dystroglycan, but not dystrophin deficiency causes myodegeneration induced by energetic stress suggesting that dystroglycan might be a component of the low-energy pathway and act as a transducer of energetic stress in normal and dystrophic muscles
Dystrophin and the Rho GTPase (显示 RACGAP1 蛋白) crossveinless-c signaling pathway likely interact at the postsynaptic side of the NMJ to maintain synaptic homeostasis.
Lack of the large dystrophin isoforms in the postsynaptic muscle cell leads to elevated evoked neurotransmitter release from presynaptic terminals.
Our results indicate the existence of at least two possibly separate roles of dystrophin in muscle, maintaining synaptic homeostasis and preserving the structural stability of the muscle.
The det locus encodes Drosophila dys, which acts with other components of the DAPC to influence intercellular signalling in developing wing veins.
Possibility that Dp186 modulates other non-Gbb/Wit-dependent retrograde signaling pathways required to maintain normal synaptic physiology.
Study provides evidence that dystrophin contains multiple independent membrane-binding domains. These structurally and functionally distinctive membrane-binding domains provide a molecular framework for dystrophin to function as a shock absorber and signaling hub.
ultiplex ligation-dependent probe amplification combined with next-generation sequencing was effective for detection of the mutations in dystrophin gene exons in patient with Duchenne and Becker muscular dystrophies.
a very infrequently reported deletion of a single exon 48 of the dystrophin gene caused a subclinical or very mild form of Becker muscular dystrophy in nine non-consanguineous families
This study describe a series of patients of Greek origin who carry a c.5068_5070delCAC mutation in the DMD gene.
These data support the hypothesis that skewed XCI is involved in the onset of phenotype in DMD carriers, the X chromosome carrying the normal DMD gene being preferentially inactivated and leading to a moderate-severe muscle involvement.
DMD reversion leads to somatic mosaicism in DMD patient.
In this study, we focused on the phenotype of patients with BMD (显示 BEST1 蛋白), who had in-frame deletion starting at exon 45 of the DMD gene, to investigate the appropriate restoration of the reading frame by exon skipping therapy
It concluded that Dp71, comprising Dp71b and Dp71ab, was expressed exclusively in HEK293 cells and that Dp71ab was specifically localized to the nucleus. Our findings suggest that Dp71ab in the nucleus contributes to the diverse functions of HEK293 cells.
This study aimed to provide in vitro quantitative evidence of the ability of human mesoangioblasts to restore dystrophin, in terms of protein accumulation and distribution, within myotubes derived from patients with Duchenne muscular dystrophy.
In TMD patients, a novel locus at genome-wide level of significance (rs73460075, OR = 0.56, P = 3.8 x 10(-8)) in the intron of the dystrophin gene DMD (X chromosome), and a suggestive locus on chromosome 7 (rs73271865, P = 2.9 x 10(-7)) upstream of the Sp4 Transcription Factor ( SP4) gene were identified in the discovery cohort, but neither of these was replicated.
Data indicate that skeletal muscles from with a missense mutation in the dystrophin gene is associated with muscle histophatology.
CRIPSR-mediated genome editing efficiently excised the mutant exon 23 in dystrophic mice, restoring the expression of dystrophin protein expression in dystrophic cardiac muscles to a level approaching 40% and improving myocardial contraction.
We show that strong and specific expression of exogenous Dp71 in Muller cells leads to correct localization of Dp71 protein restoring all protein interactions in order to re-establish a proper functional BRB (显示 PTBP1 蛋白) and retina homeostasis thus preventing retina from oedema.
avoiding vector genome loss after AAV injection by PPMO pre-treatment would allow efficient long-term restoration of dystrophin and the use of lower and thus safer vector doses for Duchenne patients.
To optimize a dystrophin cDNA construct for therapeutic application we designed and produced four human minidystrophins within the packaging capacity of lentiviral vectors. Two novel minidystrophins retained the centrally located neuronal nitric oxide synthase (nNOS (显示 NOS1 蛋白))-anchoring domain in order to achieve sarcolemmal nNOS (显示 NOS1 蛋白) restoration, which is lost in most internally deleted dystrophin constructs.
Our study demonstrates for the first time that low-level dystrophin can partially preserve heart function.
Dp71 expression in hepatic cells is carried out, in part, by YY1 (显示 YY1 蛋白)-, Sp1 (显示 SP1 蛋白)- and Sp3-mediated transcription from the Dp71 promoter.
Deficit in cognitive flexibility was observed in mdx mice in the absence of motor dysfunction or general learning impairments.
Our data also support the hypothesis that altered spatial localization of GABAA (显示 GABRg1 蛋白) receptors due to Dp427 loss is a pathological mechanism associated with brain dysfunction in DMD, suggesting that extrasynaptic GABAA (显示 GABRg1 蛋白) receptors might be candidate targets for future therapeutic developments.
This finding represents the first functional evidence for a significant role of the dystrophin-associated protein complex in the regulation of Kir2.x channels.
Lack of dystrophin in mdx mice appears associated with defective epithelial differentiation
The dystrophin gene is the largest gene found in nature, measuring 2.4 Mb. The gene was identified through a positional cloning approach, targeted at the isolation of the gene responsible for Duchenne (DMD) and Becker (BMD) Muscular Dystrophies. DMD is a recessive, fatal, X-linked disorder occurring at a frequency of about 1 in 3,500 new-born males. BMD is a milder allelic form. In general, DMD patients carry mutations which cause premature translation termination (nonsense or frame shift mutations), while in BMD patients dystrophin is reduced either in molecular weight (derived from in-frame deletions) or in expression level. The dystrophin gene is highly complex, containing at least eight independent, tissue-specific promoters and two polyA-addition sites. Furthermore, dystrophin RNA is differentially spliced, producing a range of different transcripts, encoding a large set of protein isoforms. Dystrophin (as encoded by the Dp427 transcripts) is a large, rod-like cytoskeletal protein which is found at the inner surface of muscle fibers. Dystrophin is part of the dystrophin-glycoprotein complex (DGC), which bridges the inner cytoskeleton (F-actin) and the extra-cellular matrix.
dystrophin (muscular dystrophy, Duchenne and Becker types)
, Duchenne muscular dystrophy
, dystrophin isoform Dp116
, dystrophin Dp71 isoform
, X-linked muscular dystrophy
, dystrophin transcript variant Dp71e
, dystrophin, muscular dystrophy
, Dystrophin-like protein 1
, Dystrophin-like protein 186
, Dystrophin-like protein 2
, Dystrophin-like protein 3
, dystrophin Dp186