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Journal articles on the topic 'DYSF'

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Author: Grafiati

Published: 10 March 2023

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1

Xiao, Yizhi, Honglin Zhu, Liya Li, Siming Gao, Di Liu, Bingying Dai, Qiuxiang Li, et al. "Global analysis of protein expression in muscle tissues of dermatomyositis/polymyosisits patients demonstrated an association between dysferlin and human leucocyte antigen A." Rheumatology 58, no. 8 (March 25, 2019): 1474–84. http://dx.doi.org/10.1093/rheumatology/kez085.

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Abstract Objectives DM and PM are characterized by myofibre damage with inflammatory cell infiltration due to the strong expressions of MHC class I HLA-A and monocyte chemoattractant protein-1 (MCP-1). Dysferlin (DYSF) is a transmembrane glycoprotein that anchors in the sarcolemma of myofibres. DYSF mutation is closely associated with inherited myopathies. This study aimed to determine the role of DYSF in the development of DM/PM. Methods Mass spectrometry was performed in muscle tissues from DM/PM patients and controls. The DYSF levels in muscle tissue, peripheral blood cells and serum were detected by Western blotting, IF, flow cytometry or ELISA. Double IF and co-immunoprecipitation were used to investigate the relationship between DYSF and HLA-A. Results Mass spectrometry and bioinformatics analysis findings suggested the dysregulated proteins in DM/PM patients participated in common biological processes and pathways, such as the generation of precursor metabolites and energy. DYSF was upregulated in the muscle tissue and serum of DM/PM patients. DYSF was mainly expressed in myofibres and co-localized with HLA-A and MCP-1. DYSF and HLA-A expressions were elevated in myocytes and endothelial cells after being stimulated by patient serum and IFN-β. However, no direct interactions were found between DYSF and HLA-A by co-immunoprecipitation. Conclusion Our study revealed the dysregulated proteins involved in common and specific biological processes in DM/PM patient samples. DYSF is upregulated and exhibits a potential role along with that of HLA-A and MCP-1 in inflammatory cell infiltration and muscle damage during the development of DM/PM.

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Michel Espinoza-Fonseca, L. "Pathogenic mutation R959W alters recognition dynamics of dysferlin inner DysF domain." Molecular BioSystems 12, no. 3 (2016): 973–81. http://dx.doi.org/10.1039/c5mb00772k.

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We have used atomistic simulations to demonstrate that the pathogenic mutation R959W alters recognition dynamics of dysferlin inner DysF domain. Based on these simulations, we propose a novel role for the inner DysF domain in muscle membrane repair through recruitment of dysferlin to plasma membrane.

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Mezzani, Alessandro, Ugo Corrà, Cristina Andriani, Andrea Giordano, Roberto Colombo, and Pantaleo Giannuzzi. "Anaerobic and aerobic relative contribution to total energy release during supramaximal effort in patients with left ventricular dysfunction." Journal of Applied Physiology 104, no. 1 (January 2008): 97–102. http://dx.doi.org/10.1152/japplphysiol.00608.2007.

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Energetic metabolism during effort is impaired in patients with left ventricular dysfunction (Dysf), but data have been lacking up to now on the relative anaerobic vs. aerobic contribution to total energy release during supramaximal effort. Recently, the maximal accumulated oxygen deficit (MAOD) has been shown to be measurable in Dysf patients, making it possible to evaluate the anaerobic/aerobic interaction under conditions of maximal stress of both anaerobic and aerobic metabolic pathways in this population. Nineteen Dysf patients and 17 normal patients (N) underwent one ramp cardiopulmonary, three moderate-intensity constant-power, and three supramaximal constant-power (1- to 2-min, 2- to 3-min, and 3- to 4-min duration) exercise tests. MAOD was the difference between accumulated O2demand (accO2dem; estimated from the moderate-intensity O2uptake/watt relationship) and uptake during supramaximal tests. Percent anaerobic (%Anaer) and aerobic (%Aer) energetic release were [(MAOD/accO2dem)·100] and 100 − %Anaer, respectively. MAOD did not vary between 1–2, 2–3, and 3–4 min supramaximal tests, whereas accO2dem increased significantly with and was linearly related to test duration in both Dysf and N. Consequently, %Anaer and %Aer decreased and increased, respectively, with increasing test duration but did not differ between Dysf and N in 1–2 min, 2–3 min, and 3–4 min tests. Our study demonstrates a similar relative anaerobic vs. aerobic contribution to total energy release during supramaximal effort in Dysf and N. This finding indicates that energetic metabolism during supramaximal exercise is exercise tolerance independent and that relative anaerobic vs. aerobic contribution in this effort domain remains the same within the physiology- or pathology-induced limits to individual peak exercise performance.

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Ganchinho Lucas, Sandra, Inês Vieira Santos, Filipe Jorge Pencas Alfaiate, and Ireneia Lino. "A new dysferlin gene mutation in a Portuguese family with Miyoshi myopathy." BMJ Case Reports 14, no. 7 (July 2021): e242341. http://dx.doi.org/10.1136/bcr-2021-242341.

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Dysferlinopathies are autosomal recessive muscular dystrophies caused by mutations in the dysferlin gene (DYSF). A 33-year-old man was born to a non-consanguineous couple. At the age of 25 he stared to feel weakness of the distal lower limbs and also experienced episodes of rhabdomyolysis. Electromyography showed a myopathic pattern, and muscle biopsy revealed dystrophic changes with absence of dysferlin. Genetic analysis was positive for a mutation in the c3367_3368del DYSF gene (p.Lys1123GLUFS*2). After 8 years of disease evolution the symptomatology worsened. This is the first report of this mutation of the DYSF gene identified in a non-consanguineous Portuguese family, studied over 8 years. We believe the mutation is responsible for the Miyoshi myopathy. Disease progression cannot be predicted in either the patient or carrier family because there are no similar cases previously described in the literature.

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Bryant, Grace, Steven A. Moore, James S. Nix, Grace Rice, Murat Gokden, and Aravindhan Veerapandiyan. "Miyoshi Muscular Dystrophy Due to Novel Splice Site Variants in DYSF Gene." Child Neurology Open 9 (January 2022): 2329048X2211402. http://dx.doi.org/10.1177/2329048x221140298.

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Dysferlinopathies are a group of phenotypically heterogeneous disorders caused by pathogenic variants in the DYSF (DYStrophy-associated Fer-1-like) gene encoding dysferlin. The phenotypic spectrum includes Miyoshi muscular dystrophy (MMD), limb-girdle muscular dystrophy type R2, distal myopathy with anterior tibial onset, and isolated hyperCKemia. MMD is characterized by muscle weakness and atrophy predominantly affecting the calf muscles with symptoms onset between 14 and 40 years of age. There is no clear phenotype – genotype correlation for dysferlinopathy. We describe a 15-year-old girl who presented with a phenotype consistent with MMD. However, she was initially treated for presumed polymyositis without improvement. Subsequent genetic testing revealed two novel variants in DYSF: c.3225dup (p.Gly1076Trpfs*38) in exon 30 and c.3349-2A > G (Splice acceptor) in intron 30. No dysferlin was detected in a muscle biopsy using immunostains and western blots, a result consistent with dysferlinopathy that supports the pathogenicity of the DYSF variants.

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Kocherova, I., E. Pachera, D. Nurzynska, F. DI Meglio, O. Distler, P. Blyszczuk, and G. Kania. "POS0486 IDENTIFICATION OF NEW CANDIDATE TARGETS INVOLVED IN ACTIVATION OF CARDIAC FIBROBLASTS UNDER IMMUNOFIBROTIC CONDITIONS." Annals of the Rheumatic Diseases 81, Suppl 1 (May 23, 2022): 498.1–498. http://dx.doi.org/10.1136/annrheumdis-2022-eular.4399.

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BackgroundInflammatory dilated cardiomyopathy (iDCM) often leads to heart failure (HF), which is the main cause of mortality in patients with systemic diseases. Fibroblast activation, driven by the activator protein 1 family member Fos-related antigen 2 (FOSL2), represents a critical step in cardiac fibrogenesis. The existing antifibrotic therapies, based on known fibrotic markers, failed to demonstrate efficacy against myocardial fibrosis.ObjectivesTo identify new candidate targets implicated in cardiac fibrogenesis under immunofibrotic conditions.MethodsCardiac fibroblasts were isolated from the left atria of patients (n=5) undergoing heart transplantation due to HF associated with iDCM and from unaffected hearts of brain-dead donors (UDs, n=5). Protein identification and quantification was performed using liquid chromatography tandem-mass spectrometry (LC–MS/MS). The data were analysed with MaxQuant v1.6.2.3 software. Bulk RNA sequencing (RNA-seq) was conducted using the Illumina HiSeq platform. Differentially expressed genes were identified using DESeq2. Additionally, we analysed publicly available single-cell (sc) RNA sequencing datasets (GSE109816, GSE121893) [1] on adult hearts from HF patients (n=6) and UDs (n=14) using Seurat package (V.2.3.4). Specific gene knockdown was achieved by siRNA transfection of human foetal cardiac fibroblasts (HCFs, Sigma), untreated or stimulated with TGF-β for 48-72h. The profibrotic marker expression was assessed using RT-qPCR and Western Blot. Cell viability was measured using PrestoBlue HS reagent (Invitrogen), and ATP production was quantified with CellTiter-Glo assay (Promega) in untreated and TGF-β-stimulated HCFs 48h after transfection.ResultsThe LC–MS/MS analysis revealed 14 differentially expressed proteins (absolute log2FC>1, adj. p<0.05) in the HF group compared to UDs. The most upregulated protein in HF fibroblasts was dysferlin (DYSF, log2FC=5.78, adj. p<0.004), which is known to play a role in the sarcolemma repair of both skeletal muscle fibres and cardiomyocytes. Bulk RNA-seq analysis identified a total of 67 significantly differentially expressed genes (absolute log2FC>1, adj. p<0.05). The comparative analysis of bulk RNA-seq results and publicly available scRNA-seq datasets revealed two commonly upregulated genes in HF fibroblasts or their subclusters, encoding transcription factor FOXF1 (log2FC=3.51, adj.p<0.05) and matrix remodelling-associated protein MXRA5 (log2FC=2.91, adj. p<0.05).Further in vitro studies on HCFs (n=4) showed that TGF-β upregulated DYSF (p<0.001) and MXRA5 (p<0.01) but downregulated FOXF1 (p<0.05). DYSF silencing in HCFs (n=4) upregulated MXRA5 after 48h of TGF-β stimulation (p<0.05), downregulated ACTA2 (48h and 72h of TGF-β stimulation, p<0.05), and upregulated FOSL2 protein levels in untreated HCFs and 72h after TGF-β stimulation (n=3, p<0.05). MXRA5 knockdown (n=8) resulted in the upregulation of DYSF (p<0.05), ACTA2 (p<0.05) and COL1A1 (p<0.001) in untreated HCFs, and also upregulated DYSF (p<0.01) and COL1A1 (p<0.05) after 48h of TGF-β stimulation. FOXF1 silencing in HCFs (n=8) followed by 48h of TGF-β stimulation downregulated MXRA5 (p<0.01) and ACTA2 (p=0.06), and upregulated DYSF (p<0.001) and COL1A1 (p=0.05). Candidate targets knockdown reduced cell viability in untreated (n=4, DYSF: p<0.01, MXRA5: p<0.001, FOXF1: p<0.01) and TGF-β stimulated (n=4, DYSF: p<0.05, MXRA5: p<0.05, FOXF1: p<0.01) HCFs. ATP levels were decreased in TGF-β-stimulated HCFs after DYSF silencing (n=6, p=0.05).ConclusionBased on transcriptomics, proteomics and in vitro analysis of human cardiac fibroblasts, we identified DYSF, MXRA5 and FOXF1 as candidate targets implicated in profibrotic phenotype development, including profibrotic transcription factor FOSL2 regulation. These newly proposed candidates may serve as potential therapeutic targets for the treatment of cardiac fibrosis.References[1]Wang, L. et al. Nat. Cell Biol. 2020.Disclosure of InterestsIevgeniia Kocherova: None declared, Elena Pachera: None declared, Daria Nurzynska: None declared, Franca Di Meglio: None declared, Oliver Distler Speakers bureau: Bayer, Boehringer Ingelheim, Janssen, Medscape, Consultant of: Abbvie, Acceleron, Alcimed, Amgen, AnaMar, Arxx, AstraZeneca, Baecon, Blade, Bayer, Boehringer Ingelheim, Corbus, CSL Behring, 4P Science, Galapagos, Glenmark, Horizon, Inventiva, Kymera, Lupin, Miltenyi Biotec, Mitsubishi Tanabe, MSD, Novartis, Prometheus, Roivant, Sanofi and Topadur, Grant/research support from: Kymera, Mitsubishi Tanabe, Boehringer Ingelheim, Przemyslaw Blyszczuk: None declared, Gabriela Kania: None declared.

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Rubi, Lena, Vaibhavkumar S. Gawali, Helmut Kubista, Hannes Todt, Karlheinz Hilber, and Xaver Koenig. "Proper Voltage-Dependent Ion Channel Function in Dysferlin-Deficient Cardiomyocytes." Cellular Physiology and Biochemistry 36, no. 3 (2015): 1049–58. http://dx.doi.org/10.1159/000430278.

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Background/Aims: Dysferlin plays a decisive role in calcium-dependent membrane repair in myocytes. Mutations in the encoding DYSF gene cause a number of myopathies, e.g. limb-girdle muscular dystrophy type 2B (LGMD2B). Besides skeletal muscle degenerative processes, dysferlin deficiency is also associated with cardiac complications. Thus, both LGMD2B patients and dysferlin-deficient mice develop a dilated cardiomyopathy. We and others have recently reported that dystrophin-deficient ventricular cardiomyocytes from mouse models of Duchenne muscular dystrophy show significant abnormalities in voltage-dependent ion channels, which may contribute to the pathophysiology in dystrophic cardiomyopathy. The aim of the present study was to investigate if dysferlin, like dystrophin, is a regulator of cardiac ion channels. Methods and Results: By using the whole cell patch-clamp technique, we compared the properties of voltage-dependent calcium and sodium channels, as well as action potentials in ventricular cardiomyocytes isolated from the hearts of normal and dysferlin-deficient (dysf) mice. In contrast to dystrophin deficiency, the lack of dysferlin did not impair the ion channel properties and left action potential parameters unaltered. In connection with normal ECGs in dysf mice these results suggest that dysferlin deficiency does not perturb cardiac electrophysiology. Conclusion: Our study demonstrates that dysferlin does not regulate cardiac voltage-dependent ion channels, and implies that abnormalities in cardiac ion channels are not a universal characteristic of all muscular dystrophy types.

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Malcher, Jakub, Leonie Heidt, Aurélie Goyenvalle, Helena Escobar, Andreas Marg, Cyriaque Beley, Rachid Benchaouir, et al. "Exon Skipping in a Dysf-Missense Mutant Mouse Model." Molecular Therapy - Nucleic Acids 13 (December 2018): 198–207. http://dx.doi.org/10.1016/j.omtn.2018.08.013.

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Sula, Altin, Ambrose R. Cole, Corin Yeats, Christine Orengo, and Nicholas H. Keep. "Crystal structures of the human Dysferlin inner DysF domain." BMC Structural Biology 14, no. 1 (2014): 3. http://dx.doi.org/10.1186/1472-6807-14-3.

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Liewluck, Teerin, Sunsanee Pongpakdee, Rawiphan Witoonpanich, Tumtip Sangruchi, Theeraphong Pho-iam, Chanin Limwongse, Wanna Thongnoppakhun, et al. "Novel DYSF mutations in Thai patients with distal myopathy." Clinical Neurology and Neurosurgery 111, no. 7 (September 2009): 613–18. http://dx.doi.org/10.1016/j.clineuro.2009.05.001.

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Wang, Yuning, Roya Tadayon, Liliana Santamaria, Pascal Mercier, Chantal J. Forristal, and Gary S. Shaw. "Calcium binds and rigidifies the dysferlin C2A domain in a tightly coupled manner." Biochemical Journal 478, no. 1 (January 15, 2021): 197–215. http://dx.doi.org/10.1042/bcj20200773.

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The membrane protein dysferlin (DYSF) is important for calcium-activated plasma membrane repair, especially in muscle fibre cells. Nearly 600 mutations in the DYSF gene have been identified that are causative for rare genetic forms of muscular dystrophy. The dysferlin protein consists of seven C2 domains (C2A–C2G, 13%–33% identity) used to recruit calcium ions and traffic accessory proteins and vesicles to injured membrane sites needed to reseal a wound. Amongst these, the C2A is the most prominent facilitating the calcium-sensitive interaction with membrane surfaces. In this work, we determined the calcium-free and calcium-bound structures of the dysferlin C2A domain using NMR spectroscopy and X-ray crystallography. We show that binding two calcium ions to this domain reduces the flexibility of the Ca2+-binding loops in the structure. Furthermore, calcium titration and mutagenesis experiments reveal the tight coupling of these calcium-binding sites whereby the elimination of one site abolishes calcium binding to its partner site. We propose that the electrostatic potential distributed by the flexible, negatively charged calcium-binding loops in the dysferlin C2A domain control first contact with calcium that promotes subsequent binding. Based on these results, we hypothesize that dysferlin uses a ‘calcium-catching’ mechanism to respond to calcium influx during membrane repair.

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Spadafora, Patrizia, Antonio Qualtieri, Francesca Cavalcanti, Gemma Di Palma, Olivier Gallo, Selene De Benedittis, Annamaria Cerantonio, and Luigi Citrigno. "A Novel Homozygous Variant in DYSF Gene Is Associated with Autosomal Recessive Limb Girdle Muscular Dystrophy R2/2B." International Journal of Molecular Sciences 23, no. 16 (August 11, 2022): 8932. http://dx.doi.org/10.3390/ijms23168932.

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Mutations in the DYSF gene, encoding dysferlin, are responsible for Limb Girdle Muscular Dystrophy type R2/2B (LGMDR2/2B), Miyoshi myopathy (MM), and Distal Myopathy with Anterior Tibialis onset (MDAT). The size of the gene and the reported inter and intra familial phenotypic variability make early diagnosis difficult. Genetic analysis was conducted using Next Gene Sequencing (NGS), with a panel of 40 Muscular Dystrophies associated genes we designed. In the present study, we report a new missense variant c.5033G>A, p.Cys1678Tyr (NM_003494) in the exon 45 of DYSF gene related to Limb Girdle Muscular Dystrophy type R2/2B in a 57-year-old patient affected with LGMD from a consanguineous family of south Italy. Both healthy parents carried this variant in heterozygosity. Genetic analysis extended to two moderately affected sisters of the proband, showed the presence of the variant c.5033G>A in both in homozygosity. These data indicate a probable pathological role of the variant c.5033G>A never reported before in the onset of LGMDR2/2B, pointing at the NGS as powerful tool for identifying LGMD subtypes. Moreover, the collection and the networking of genetic data will increase power of genetic-molecular investigation, the management of at-risk individuals, the development of new therapeutic targets and a personalized medicine.

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Park, Joonhong, Young Jae Moon, and Dal Sik Kim. "Miyoshi Muscular Dystrophy Type 1 with Mutated DYSF Gene Misdiagnosed as Becker Muscular Dystrophy: A Case Report and Literature Review." Genes 14, no. 1 (January 12, 2023): 200. http://dx.doi.org/10.3390/genes14010200.

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Dysferlinopathy covers a spectrum of muscle disorder categorized by two major phenotypes, namely Miyoshi muscular dystrophy type 1 (MMD1, OMIM #254130) and limb-girdle muscular dystrophy autosomal recessive 2 (LGMDR2, OMIM #253601), and two minor symptoms, including asymptomatic hyperCKemia and distal myopathy with anterior tibial onset (DMAT, OMIM #606768). We report the first Korean MMD1 misdiagnosed as Becker muscular dystrophy (BMD), which was caused by a combination of compound heterozygous c.663 + 1G > C and p.Trp992Arg of the DYSF gene. A 70-year-old male previously diagnosed with BMD was admitted for genetic counseling. Since he was clinically suspected to have dysferlinopathy but not BMD, targeted panel sequencing was performed to discover the potential hereditary cause of the suspected muscular dystrophy in the proband. Consequently, two pathogenic single nucleotide variants of the DYSF gene, c.663 + 1G > C (rs398123800) and p.Trp992Arg (rs750028300), associated with dysferlinopathy were identified. These variants were previously reported with variant allele frequencies of 0.000455 (c.663 + 1G > C) and 0.000455 (c.2974T > C; p.Trp992Arg) in the Korean population. This report emphasizes the need for common variant screening in the diagnostic algorithms of certain muscle disorders or gene panels with potential pathogenic effects and high rates of recurrent variants.

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Barzilai-Tutsch, Hila, Olga Genin, Mark Pines, and Orna Halevy. "Early pathological signs in young dysf mice are improved by halofuginone." Neuromuscular Disorders 30, no. 6 (June 2020): 472–82. http://dx.doi.org/10.1016/j.nmd.2020.04.001.

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Zhao, Zhe, Jing Hu, Yusuke Sakiyama, Yuji Okamoto, Itsuro Higuchi, Na Li, Hongrui Shen, and Hiroshi Takashima. "DYSF mutation analysis in a group of Chinese patients with dysferlinopathy." Clinical Neurology and Neurosurgery 115, no. 8 (August 2013): 1234–37. http://dx.doi.org/10.1016/j.clineuro.2012.11.010.

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Schoewel, V., S. Adams, C. Herrmann, U. Zacharias, M. Boschmann, I. Richard, and S. Spuler. "P2.55 Mstn/Dysf double knockout mice gain muscle mass but no strength." Neuromuscular Disorders 21, no. 9-10 (October 2011): 676–77. http://dx.doi.org/10.1016/j.nmd.2011.06.877.

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Bardakov, S. N., A. М. Emelin, S. S. Nikitin, A. N. Khelkovskaya-Sergeeva, I. S. Limaev, A. F. Murtazina, V. A. Tsargush, et al. "Reasons for misdiagnosis of polymyositis in patients with dysferlinopathy: a clinical case." Neuromuscular Diseases 12, no. 4 (December 13, 2022): 73–87. http://dx.doi.org/10.17650/2222-8721-2022-12-4-73-87.

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Differential diagnosis of inflammatory myopathies with hereditary muscular dystrophies accompanied by a secondary inflammatory process is a time‑consuming clinical and pathomorphological task. In particular, false diagnosis of polymyositis in patients with dysferlinopathy reaches 25 % of cases.A 40‑year‑old female patient with a limb‑girdle phenotype of dysferlinopathy, initially diagnosed as polymyositis, is presented. The reasons that led to the erroneous diagnosis were: sporadic case; subacute onset; proximal muscle weakness; myalgia, which stopped on the glucocorticosteroid therapy; high levels of creatine phosphokinase (up to 17 times); the presence of lymphocytic‑macrophage infiltrate in the muscle biopsy and the absence of magnetic resonance imaging data in primary examination of the patient.The refractoriness of clinical and laboratory signs to complex immunosuppressive therapy was the reason for revising the muscle biopsy with typing of the inflammatory infiltrate. The predominantly unexpressed perivascular infiltrate was characterized by the predominance of macrophages and, to a lesser extent, CD4+, which indicated the secondary nature of the inflammation in the muscle observed in some hereditary muscular dystrophies. When conducting an immunohistochemical reaction, the absence of the dysferlin protein in the sarcoplasmic membrane was revealed.Whole‑exome sequencing (NGS) revealed a mutation in exon 39 of the DYSF gene (p.Gln1428Ter) in the heterozygous state, which leads to the appearance of a stop codon and premature termination of protein translation. MLPA method registered 3 copies of exons 18, 19, 20, 22, 24 of the DYSF gene.Thus, this clinical example reflects the main methodological errors and possible effects of immunosuppressive therapy in patients with dysferlinopathy.

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Li, Quanzhen, Hui Luo, Honglin Zhu, Chengsong Zhu, Li Wang, Huali Zhang, and Xiaoxia Zuo. "A combined genome-wide DNA methylation and mRNA expression analysis identified aberrant gene regulatory pathways in inflammatory myositis." Journal of Immunology 198, no. 1_Supplement (May 1, 2017): 210.12. http://dx.doi.org/10.4049/jimmunol.198.supp.210.12.

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Abstract Inflammatory myositis (IM) is an immune-mediated inflammatory process primarily involving skeletal muscle and the etiology is still poorly understood. Clinical and molecular evidence indicated that the epigenetic regulation on mRNA transcription of immune cells may drive the pathogenic processing. In this study, we performed genome-scale DNA methylation and mRNA transcription profiling using Illumina HumanMethy450 and HumanHT-12 Beadchips on PBMC of 24 IM patients and matched normal controls (NC). We identified 617 genes showing altered DNA methylation between IM and NC. By integrating DNA methylation and mRNA expression data, we found 108 hypomethylated genes showing concurrent up-regulation and 43 hypermethylated genes showing decreased expression. Integrated pathway analysis indicated that these genes are involved in Th1/Th2 cell activation, arginine degradation, chemotaxis of neutrophils, granulocyte adhesion, cytotoxic T cell-mediated apoptosis, etc. Comparison of DNA methylation profile between dermatomyositis (DM) and polymyositis (PM) identified 66 altered genes which were shared in both DM and PM, 51 genes altered only in PM and 32 genes only DM. The genes which showed most significant hypomethylation and up-regulated are DYSF, IL1R2, OLFM4, ARG1, PDE6H, PPARG, MYB, and the most hypermethylated and down-regulated genes include CXCR6, ABLIM1, LAX1, PRKCH, CD3G and SLFN5. DYSF is a gene encoding dysferlin protein which may involve in the pathogenesis of myositis by interfering membrane repair in muscular dystrophy. Our analysis lays the groundwork for further molecular studies of IM by identifying novel epigenetically dysregulated genes potentially involved in the immune activation and muscular dystrophy.

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Peng, Li-Sha, Zeng-Ming Li, Ge Chen, Fa-Ying Liu, Yong Luo, Jiu-Bai Guo, Guo-Dong Gao, et al. "Frequent DYSF rare variants/mutations in 152 Han Chinese samples with ovarian endometriosis." Archives of Gynecology and Obstetrics 304, no. 3 (May 13, 2021): 671–77. http://dx.doi.org/10.1007/s00404-021-06094-8.

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ten Dam, Leroy, Anneke J. van der Kooi, Fleur Rövekamp, Wim H. J. P. Linssen, and Marianne de Visser. "Comparing clinical data and muscle imaging of DYSF and ANO5 related muscular dystrophies." Neuromuscular Disorders 24, no. 12 (December 2014): 1097–102. http://dx.doi.org/10.1016/j.nmd.2014.07.004.

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Astorga, C., C. Basualto-Alarcon, P. Caviedes, J. Bevilacqua, and J. Cárdenas. "P.173Ketogenic diet ameliorates dysferlinopathy phenotype in Dysf-/-mice by promoting mitochondrial function." Neuromuscular Disorders 29 (October 2019): S99. http://dx.doi.org/10.1016/j.nmd.2019.06.228.

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Sivasamy, Manoj, Shreenidhi R., Nishaanth M. K., Jagadeesan M., Prasanna Karthik S., and Kevin Fernandez. "A case of dysferlinopathy (Miyoshi distal myopathy limb-girdle muscular dystrophy type 2b phenotype) from a tertiary care hospital." International Journal of Advances in Medicine 10, no. 2 (January 23, 2023): 161–63. http://dx.doi.org/10.18203/2349-3933.ijam20230067.

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Limb girdle muscular dystrophy type 2B (LGMD2B) and Miyoshi myopathy are caused by similar mutations in the dysferlin gene. The phenotype of these allelic disease variants can vary considerably. We report a young male with severe and rapidly progressing muscle disorder with increased creatine phosphokinase (CPK) and confirmatory muscle biopsy findings. Genetic testing was done. A homozygous nonsense variation in exon 23 of the DYSF gene, which was consistent with the patient’s clinical reports of dysferlinopathy. Clinical phenomenology and preferential muscle involvement lead one to the gold standard genetic testing in heritable myopathies, which was well established in this report.

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Ullah, Muhammad, Arsalan Ahmad, Milena Žarković, Syed Shah, Abdul Nasir, Saqib Mahmood, Wasim Ahmad, Christian Hübner, and Muhammad Hassan. "Novel duplication mutation of the DYSF gene in a Pakistani family with Miyoshi Myopathy." Saudi Medical Journal 38, no. 12 (December 3, 2017): 1190–95. http://dx.doi.org/10.15537/smj.2017.12.18456.

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Ullah, Muhammad, Arsalan Ahmad, Milena Žarković, Syed Shah, Abdul Nasir, Saqib Mahmood, Wasim Ahmad, Christian Hübner, and Muhammad Hassan. "Novel duplication mutation of the DYSF gene in a Pakistani family with Miyoshi Myopathy." Saudi Medical Journal 38, no. 12 (December 3, 2017): 1190–95. http://dx.doi.org/10.15537/smj.2017.12.20989.

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Vafiadaki, Elizabeth, Andre Reis, Sharon Keers, Ruth Harrison, Louise V. B. Anderson, Thomas Raffelsberger, Silva Ivanova, et al. "Cloning of the mouse dysferlin gene and genomic characterization of the SJL-Dysf mutation." Neuroreport 12, no. 3 (March 2001): 625–29. http://dx.doi.org/10.1097/00001756-200103050-00039.

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ten Dam, L., A. J. van der Kooi, F. Rövekamp, W. H. Linssen, and M. de Visser. "P.5.2 A comparison of muscle imaging in DYSF and ANO5 related muscular dystrophies." Neuromuscular Disorders 23, no. 9-10 (October 2013): 764. http://dx.doi.org/10.1016/j.nmd.2013.06.454.

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Gáti, István, Olof Danielsson, Cecilia Gunnarsson, Magnus Vrethem, Bo Häggqvist, Bengt-Arne Fredriksson, and Anne-Marie Landtblom. "Bent Spine Syndrome: A Phenotype of Dysferlinopathy or a Symptomatic DYSF Gene Mutation Carrier." European Neurology 67, no. 5 (2012): 300–302. http://dx.doi.org/10.1159/000336265.

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Charnay, Théo, Véronique Blanck, Mathieu Cerino, Marc Bartoli, Florence Riccardi, Nathalie Bonello-Palot, Christophe Pécheux, et al. "Retrospective analysis and reclassification of DYSF variants in a large French series of dysferlinopathy patients." Genetics in Medicine 23, no. 8 (April 29, 2021): 1574–77. http://dx.doi.org/10.1038/s41436-021-01164-3.

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Lee, Joshua J. A., Rika Maruyama, William Duddy, Hidetoshi Sakurai, and Toshifumi Yokota. "Identification of Novel Antisense-Mediated Exon Skipping Targets in DYSF for Therapeutic Treatment of Dysferlinopathy." Molecular Therapy - Nucleic Acids 13 (December 2018): 596–604. http://dx.doi.org/10.1016/j.omtn.2018.10.004.

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30

Ha, Mihyang, Hoim Jeong, Jong Seong Roh, Beomgu Lee, Myoung-Eun Han, Sae-Ock Oh, Dong Hyun Sohn, and Yun Hak Kim. "DYSF expression in clear cell renal cell carcinoma: A retrospective study of 2 independent cohorts." Urologic Oncology: Seminars and Original Investigations 37, no. 10 (October 2019): 735–41. http://dx.doi.org/10.1016/j.urolonc.2019.07.007.

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31

Tang, Jin, Xueqin Song, Guang Ji, Hongran Wu, Shuyan Sun, Shan Lu, Yuan Li, Chi Zhang, and Huiqing Zhang. "A novel mutation in the DYSF gene in a patient with a presumed inflammatory myopathy." Neuropathology 38, no. 4 (May 25, 2018): 433–37. http://dx.doi.org/10.1111/neup.12474.

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32

Lee, Sook Joung, Eunseok Choi, Soyoung Shin, and Joonhong Park. "Genetically confirmed limb-girdle muscular dystrophy type 2B with DYSF mutation using gene panel sequencing." Medicine 99, no. 28 (July 10, 2020): e20810. http://dx.doi.org/10.1097/md.0000000000020810.

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Okubo, Mariko, Aritoshi Iida, Shinichiro Hayashi, Madoka Mori-Yoshimura, Yasushi Oya, Akihiro Watanabe, Hajime Arahata, Rasha El Sherif, Satoru Noguchi, and Ichizo Nishino. "Three novel recessive DYSF mutations identified in three patients with muscular dystrophy, limb-girdle, type 2B." Journal of the Neurological Sciences 395 (December 2018): 169–71. http://dx.doi.org/10.1016/j.jns.2018.10.015.

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34

Bulankina, Anna V., and Sven Thoms. "Functions of Vertebrate Ferlins." Cells 9, no. 3 (February 25, 2020): 534. http://dx.doi.org/10.3390/cells9030534.

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Ferlins are multiple-C2-domain proteins involved in Ca2+-triggered membrane dynamics within the secretory, endocytic and lysosomal pathways. In bony vertebrates there are six ferlin genes encoding, in humans, dysferlin, otoferlin, myoferlin, Fer1L5 and 6 and the long noncoding RNA Fer1L4. Mutations in DYSF (dysferlin) can cause a range of muscle diseases with various clinical manifestations collectively known as dysferlinopathies, including limb-girdle muscular dystrophy type 2B (LGMD2B) and Miyoshi myopathy. A mutation in MYOF (myoferlin) was linked to a muscular dystrophy accompanied by cardiomyopathy. Mutations in OTOF (otoferlin) can be the cause of nonsyndromic deafness DFNB9. Dysregulated expression of any human ferlin may be associated with development of cancer. This review provides a detailed description of functions of the vertebrate ferlins with a focus on muscle ferlins and discusses the mechanisms leading to disease development.

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Huang, Qianwen, Noman Qureshi, Simin Lin, and Shaoyin Duan. "Experimental Verification of Gene Expression Related to Lung Cancer in Nasal Epitthelia." ITM Web of Conferences 26 (2019): 02004. http://dx.doi.org/10.1051/itmconf/20192602004.

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Genes expression related to lung cancer are observed in nasal epitthelia, to identify their similarities and differences and provide the basis for possible application. There are three groups:non-lung cancer group (NLC), lung cancer group (LC) and postoperative lung cancer group (PLC).The genes expression in nasal epitthelia were observed by PCR, including the HCK, NCF1, TLR8, EMR3, CSF2RB, DYSF, SPEF2, ANKFN1, HYDIN, DNAH5, C12orf55 and CCDC113. Their expression levels were obtained and statistically compared. Results showed that all the related genes in LC and PLC groups were highly expressed. There are significant difference in HCK, NCF1, TLR8, EMR3, CSF2RB and C12orf55 gene expression between the LC or PLC and NLC, and in EMR3 and C12orf55 between LC and PLC. Conclusions are HCK, NCF1, TLR8, EMR3, CSF2RB, C12orf55 can be used for lung cancer screening, while EMR3 and C12orf55 for the review of post-operative lung cancer.

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36

Chekmareva, I. A., R. V. Deev, O. N. Chernova, I. U. Bikhteev, and A. M. Emelin. "Cells corresponding to telocites have been detected in pathologically altered skeletal muscle." Genes & Cells 17, no. 1 (March 15, 2022): 38–41. http://dx.doi.org/10.23868/202205007.

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A relatively recently described population of cells, apparently belonging to the tissue system of the internal environment, are the telocytes. Their peculiarities are not only the co-expression of CD117- and CD34-molecules, but also thin, indistinguishable processes at the light-optical level, whose length can be many times greater than the diameter of the cell body. In this regard, transmission electron microscopy remains the method of choice for their detection in tissues. Telocytes were found in the myocardium, connective tissue of the gallbladder, in gastrointestinal tract, in the stroma of the exocrine glands, the placenta, some vessels. However, data on the detection of telocytes in striated skeletal muscle tissue are either absent or still rare. This brief report demonstrates cells that, by their ultrastructural characteristics, can be identified as telocytes in the endomysium of gastrocnemius muscle in Bla/J mice (mutation in the dysferlin gene, DYSF).

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Bittner, Reginald E., Louise V. B. Anderson, Elke Burkhardt, Rumaisa Bashir, Elizabeth Vafiadaki, Silva Ivanova, Thomas Raffelsberger, et al. "Dysferlin deletion in SJL mice (SJL-Dysf) defines a natural model for limb girdle muscular dystrophy 2B." Nature Genetics 23, no. 2 (October 1999): 141–42. http://dx.doi.org/10.1038/13770.

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38

Krahn, M., R. Bernard, K. Nguyen, V. Labelle, G. Bassez, D. Figarella-Branger, J. Pouget, et al. "G.P.4.01 Mutational spectrum of the DYSF gene based on a large cohort of dysferlin deficient patients." Neuromuscular Disorders 17, no. 9-10 (October 2007): 787. http://dx.doi.org/10.1016/j.nmd.2007.06.093.

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39

Asadi, Shahin. "Assessment of Genetic Mutations DMD, DYSF, EMD, LMNA, DUX4, DMPK, ZNF9, PABPN1 Genes Induction Duchenne Muscular Dystrophy." SOJ Immunology 5, no. 2 (October 12, 2017): 1–8. http://dx.doi.org/10.15226/2372-0948/5/2/00161.

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40

Vilchez, Juan J., Pia Gallano, Eduard Gallardo, Adriana Lasa, Ricardo Rojas-García, Alba Freixas, Noemí De Luna, et al. "Identification of a Novel Founder Mutation in the DYSF Gene Causing Clinical Variability in the Spanish Population." Archives of Neurology 62, no. 8 (August 1, 2005): 1256. http://dx.doi.org/10.1001/archneur.62.8.1256.

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41

Kim, Du Hwan, Dae-Hyun Jang, and Ja-Hyun Jang. "Incidental Severe Fatty Degeneration of the Erector Spinae in a Patient with L5–S1 Disc Extrusion Diagnosed with Limb-Girdle Muscular Dystrophy R2 Dysferin-Related." Diagnostics 10, no. 8 (July 29, 2020): 530. http://dx.doi.org/10.3390/diagnostics10080530.

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Limb-girdle muscular dystrophy type R2 dysferin-related (LGMD R2 dysferin-related), a phenotype of dysferlinopathy, usually begins with pelvic girdle weakness. A 35-year-old male presented with right leg pain for 2 weeks without a previous history of limb weakness. Magnetic resonance imaging of the lumbar spine showed disc extrusion at L5–S1 and incidental severe fatty degeneration of the lumbar erector spinae. Physical examination demonstrated no definite limb weakness. Serum creatine kinase levels were elevated. Genetic testing using a targeted gene-sequencing panel identified compound heterozygous variants NM_003494.3(DYSF) c.[1284+2T>C]; [5303G>A]. Computed tomography revealed fatty degeneration of lower-limb muscles, which was mild in the adductor muscles and severe in the gluteus minimus. Immunohistochemistry staining of the vastus lateralis showed under-expression of dysferlin. This patient was diagnosed with LGMD R2 dysferin-related. Thus, unusual fatty degeneration of the lumbar paraspinalis can be a manifestation of dysferlinopathy.

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42

Tarnopolsky, Mark A., Erin Hatcher, and Rachel Shupak. "Genetic Myopathies Initially Diagnosed and Treated as Inflammatory Myopathy." Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques 43, no. 3 (February 25, 2016): 381–84. http://dx.doi.org/10.1017/cjn.2015.386.

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AbstractObjectives: Differentiating genetic myopathies from inflammatory myopathies can be challenging because of multiple overlapping clinical features. Examples are presented to highlight important clinical features that assist in the differentiation between the two. Methods: Clinical features including age at onset, history, pattern of weakness, serum creatine kinase activity, electromyography findings, and muscle biopsies are reported in six patients initially thought to have an inflammatory myopathy in whom the final diagnosis was a genetic myopathy. Results: All six patients met Bohan and Peter criteria for at least probable idiopathic polymyositis and were subsequently found to have a genetic myopathy (4 DYSF, RYR1, and GNE). The key distinguishing clinical were minimal to no response to immunosuppression and atypical involvement of distal muscles in the majority of cases. Conclusions: Patients diagnosed with inflammatory myopathies should be reevaluated for the possibility of a genetic myopathy if they fail to respond to a course of disease-modifying agents and/or there is atypical distal muscle involvement.

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43

Korokin, M. V., E. V. Kuzubova, A. I. Radchenko, R. V. Deev, I. A. Yakovlev, A. V. Deikin, N. S. Zhunusov, et al. "В6.А-DYSFPRMD/GENEJ MICE AS A GENETIC MODEL OF DYSFERLINOPATHY." Pharmacy & Pharmacology 10, no. 5 (December 16, 2022): 483–96. http://dx.doi.org/10.19163/2307-9266-2022-10-5-483-496.

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The aim of the work was behavioral and pathomorphological phenotyping of the mice knockout for the DYSF gene, which plays an important role in the development and progression of dysferlinopathy.Materials and methods. A B6.A-Dysfprmd/GeneJ (Bla/J) mice subline was used in the work. During the study, a muscle activity was determined basing on the following tests: “Inverted grid”, “Grip strength”, “Wire Hanging”, “Weight-loaded swimming”, Vertical Pole”. Histological and immunofluorescent examinations of skeletal muscles (m. gastrocnemius, m. tibialis) were performed. The presence and distribution of the dysferlin protein was assessed, and general histological changes in the skeletal muscle characteristics of mice at the age of 12 and 24 weeks, were described. A morphometric analysis with the determination of the following parameters was performed: the proportion of necrotic muscle fibers; the proportion of fibers with centrally located nuclei; the mean muscle fiber diameter.Results. The “Grip strength” test and the “Weight-loaded swimming” test revealed a decrease in the strength of the forelimbs and endurance in the studied mice of the Bla/J subline compared to the control line. The safety of physical performance was checked using the “Wire Hanging” test and the “Vertical Pole” test, which showed a statistically significant difference between the studied mice and control. The coordination of movements and muscle strength of the limbs examined in the “Inverted Grid” test did not change in these age marks. Decreased grip strength of the forelimbs, decreased physical endurance with age, reflects the progression of the underlying muscular disease. Histological methods in the skeletal muscles revealed signs of a myopathic damage pattern: necrotic muscle fibers, moderate lympho-macrophage infiltration, an increase in the proportion of fibers with centrally located nuclei, and an increase in the average fiber diameter compared to the control. The dysferlin protein was not found out in the muscle tissues.Conclusion. Taking into account the results of the tests performed, it was shown that the absence of Dysf-/- gene expressionin Bla/J subline mice led to muscular dystrophy with the onset of the development of phenotypic disease manifestations at the age of 12 weeks and their peak at 24 weeks. Histopathological phenotypic manifestations of the disease are generally nonspecific and corresponded to the data of intravital pathoanatomical examination in diferlinopathy patients. The mice of the studied subline Bla/J are a representative model of dysferlinopathy and can be used to evaluate new therapeutic agents for the treatment of this disease.

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Folland, C., R. Johnsen, A. Botero Gomez, D. Trajanoski, M. Davis, U. Moore, V. Straub, et al. "O.11 Identification of a novel heterozygous DYSF variant in a large family with a dominantly-inherited dysferlinopathy." Neuromuscular Disorders 32 (October 2022): S94—S95. http://dx.doi.org/10.1016/j.nmd.2022.07.219.

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Ceyhan-Birsoy, Ozge, Beril Talim, Lindsay C. Swanson, Mert Karakaya, Michelle A. Graff, Alan H. Beggs, and Haluk Topaloglu. "Whole Exome Sequencing Reveals DYSF, FKTN, and ISPD Mutations in Congenital Muscular Dystrophy Without Brain or Eye Involvement." Journal of Neuromuscular Diseases 2, no. 1 (2015): 87–92. http://dx.doi.org/10.3233/jnd-140038.

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46

Santos, R., J. Oliveira, E. Vieira, T. Coelho, A. Carneiro Leite, T. Evangelista, A. Fortuna, A. Geraldo, N. Luís, and A. Guimarães. "G.P.4.02 Founder effect of a new DYSF exon 48-skipping mutation detected in seven Portuguese dysferlinopathy patients." Neuromuscular Disorders 17, no. 9-10 (October 2007): 788. http://dx.doi.org/10.1016/j.nmd.2007.06.094.

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47

Patel, Pryank, Richard Harris, Stella M. Geddes, Eugen-Matthias Strehle, James D. Watson, Rumaisa Bashir, Katharine Bushby, Paul C. Driscoll, and Nicholas H. Keep. "Solution Structure of the Inner DysF Domain of Myoferlin and Implications for Limb Girdle Muscular Dystrophy Type 2B." Journal of Molecular Biology 379, no. 5 (June 2008): 981–90. http://dx.doi.org/10.1016/j.jmb.2008.04.046.

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48

Li, Qiao, Cheng Tan, Jiajun Chen, and Lei Zhang. "Next-generation sequencing identified a novel DYSF variant in a patient with limb-girdle muscular dystrophy type 2B." Medicine 99, no. 41 (October 9, 2020): e22615. http://dx.doi.org/10.1097/md.0000000000022615.

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49

Wu, Fei, Rinse de Boer, Arjen M. Krikken, Arman Akşit, Nicola Bordin, Damien P. Devos, and Ida J. van der Klei. "Pex24 and Pex32 are required to tether peroxisomes to the ER for organelle biogenesis, positioning and segregation in yeast." Journal of Cell Science 133, no. 16 (July 14, 2020): jcs246983. http://dx.doi.org/10.1242/jcs.246983.

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ABSTRACTThe yeast Hansenula polymorpha contains four members of the Pex23 family of peroxins, which characteristically contain a DysF domain. Here we show that all four H. polymorpha Pex23 family proteins localize to the endoplasmic reticulum (ER). Pex24 and Pex32, but not Pex23 and Pex29, predominantly accumulate at peroxisome–ER contacts. Upon deletion of PEX24 or PEX32 – and to a much lesser extent, of PEX23 or PEX29 – peroxisome–ER contacts are lost, concomitant with defects in peroxisomal matrix protein import, membrane growth, and organelle proliferation, positioning and segregation. These defects are suppressed by the introduction of an artificial peroxisome–ER tether, indicating that Pex24 and Pex32 contribute to tethering of peroxisomes to the ER. Accumulation of Pex32 at these contact sites is lost in cells lacking the peroxisomal membrane protein Pex11, in conjunction with disruption of the contacts. This indicates that Pex11 contributes to Pex32-dependent peroxisome–ER contact formation. The absence of Pex32 has no major effect on pre-peroxisomal vesicles that occur in pex3 atg1 deletion cells.

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Cho, Hyun-Jung, Duck Hyun Sung, Eun-Jin Kim, Chul Ho Yoon, Chang-Seok Ki, and Jong-Won Kim. "Clinical and Genetic Analysis of Korean Patients with Miyoshi Myopathy: Identification of Three Novel Mutations in the DYSF Gene." Journal of Korean Medical Science 21, no. 4 (2006): 724. http://dx.doi.org/10.3346/jkms.2006.21.4.724.

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