É uma doença muscular de origem genética que causa fraqueza, principalmente nas partes mais distantes do corpo, como as mãos e os pés. É herdada de apenas um dos pais e afeta igualmente homens e mulheres.
Introdução
O que você precisa saber de cara
É uma doença muscular de origem genética que causa fraqueza, principalmente nas partes mais distantes do corpo, como as mãos e os pés. É herdada de apenas um dos pais e afeta igualmente homens e mulheres.
Encontrou um erro ou informação desatualizada? Sugira uma correção →
Entender a doença
Do básico ao detalhe, leia no seu ritmo
Preparando trilha educativa...
Sinais e sintomas
O que aparece no corpo e com que frequência cada sintoma acontece
Partes do corpo afetadas
+ 60 sintomas em outras categorias
Características mais comuns
Os sintomas variam de pessoa para pessoa. Abaixo estão as 174 características clínicas mais associadas, ordenadas por frequência.
Linha do tempo da pesquisa
Encontrou um erro ou informação desatualizada? Sugira uma correção →
Genética e causas
O que está alterado no DNA e como passa nas famílias
Genes associados
12 genes identificados com associação a esta condição.
May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. May also regulate voltage-gated potassium channels. Plays a role in the sarcolemma repair mechanism of both skeletal muscle and cardiomyocytes that permits rapid resealing of membranes disrupted by mechanical stress (By similarity). Mediates the recruitment of CAVIN2 and CAVIN3 proteins to the caveolae (PubMed:19262564)
Golgi apparatus membraneCell membraneMembrane, caveolaCell membrane, sarcolemma
HyperCKmia
Characterized by persistent elevated levels of serum creatine kinase without muscle weakness.
Necessary for the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis. Involved in the formation of the transitional endoplasmic reticulum (tER). The transfer of membranes from the endoplasmic reticulum to the Golgi apparatus occurs via 50-70 nm transition vesicles which derive from part-rough, part-smooth transitional elements of the endoplasmic reticulum (tER). Vesicle budding from the tER is an ATP-dependent process. The ternary complex containing UFD1, VCP and
Cytoplasm, cytosolEndoplasmic reticulumNucleusCytoplasm, Stress granule
Inclusion body myopathy with early-onset Paget disease with or without frontotemporal dementia 1
An autosomal dominant disease characterized by disabling muscle weakness clinically resembling to limb girdle muscular dystrophy, osteolytic bone lesions consistent with Paget disease, and premature frontotemporal dementia. Clinical features show incomplete penetrance.
Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for mitotic progression and cytokinesis. The BCR(KLHL9-KLHL13) E3 ubiquitin ligase complex mediates the ubiquitination of AURKB and controls the dynamic behavior of AURKB on mitotic chromosomes and thereby coordinates faithful mitotic progression and completion of cytokinesis
May play a role in transcription or may interact with other nuclear matrix proteins to form the internal fibrogranular network. In association with the SFPQ-NONO heteromer may play a role in nuclear retention of defective RNAs. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:2871272
Nucleus matrix
Amyotrophic lateral sclerosis 21
A neurodegenerative disorder affecting upper and lower motor neurons, resulting in muscle weakness and respiratory failure. Some patients may develop myopathic features or dementia.
Molecular adapter required for selective macroautophagy (aggrephagy) by acting as a bridge between polyubiquitinated proteins and autophagosomes (PubMed:15340068, PubMed:15953362, PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22017874, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:33509017, PubMed:34471133, PubMed:34893540, PubMed:35831301, PubMed:37306101, PubMed:37802024). Promotes the recruitment of ubiquitinated cargo
Cytoplasmic vesicle, autophagosomePreautophagosomal structureCytoplasm, cytosolNucleus, PML bodyLate endosomeLysosomeNucleusEndoplasmic reticulumCytoplasm, myofibril, sarcomere
Paget disease of bone 3
A disorder of bone remodeling characterized by increased bone turnover affecting one or more sites throughout the skeleton, primarily the axial skeleton. Osteoclastic overactivity followed by compensatory osteoblastic activity leads to a structurally disorganized mosaic of bone (woven bone), which is mechanically weaker, larger, less compact, more vascular, and more susceptible to fracture than normal adult lamellar bone.
Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and modulation of splice site selection (PubMed:17371836). Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (PubMed:20010808). Binds to the IRES and thereby inhibits the translation of the apoptosis protease activating
NucleusCytoplasm
Inclusion body myopathy with early-onset Paget disease with or without frontotemporal dementia 3
An autosomal dominant disease characterized by disabling muscle weakness clinically resembling to limb girdle muscular dystrophy, osteolytic bone lesions consistent with Paget disease, and premature frontotemporal dementia. Clinical features show incomplete penetrance.
RNA-binding protein involved in the regulation of alternative pre-RNA splicing and mRNA translation by binding to uridine-rich (U-rich) RNA sequences (PubMed:11106748, PubMed:12486009, PubMed:17488725, PubMed:8576255). Binds to U-rich sequences immediately downstream from a 5' splice sites in a uridine-rich small nuclear ribonucleoprotein (U snRNP)-dependent fashion, thereby modulating alternative pre-RNA splicing (PubMed:11106748, PubMed:8576255). Preferably binds to the U-rich IAS1 sequence in
NucleusCytoplasmCytoplasm, Stress granule
Welander distal myopathy
An autosomal dominant disorder characterized by adult onset of distal muscle weakness predominantly affecting the distal long extensors of the hands, with slow progression to involve all small hand muscles and the lower legs. Skeletal muscle biopsy shows myopathic changes and prominent rimmed vacuoles. Rare homozygous patients showed earlier onset, faster progression, and proximal muscle involvement.
Muscle-specific filamin, which plays a central role in sarcomere assembly and organization (PubMed:34405687). Critical for normal myogenesis, it probably functions as a large actin-cross-linking protein with structural functions at the Z lines in muscle cells. May be involved in reorganizing the actin cytoskeleton in response to signaling events (By similarity)
CytoplasmMembraneCytoplasm, cytoskeletonCytoplasm, myofibril, sarcomere, Z line
Myopathy, myofibrillar, 5
A form of myofibrillar myopathy, a group of chronic neuromuscular disorders characterized at ultrastructural level by disintegration of the sarcomeric Z disk and myofibrils, and replacement of the normal myofibrillar markings by small dense granules, or larger hyaline masses, or amorphous material. MFM5 is characterized by onset in adulthood, clinical features of a limb-girdle myopathy, and focal myofibrillar destruction.
Component of a complex of multiple actin cross-linking proteins. Involved in the control of myofibril assembly and stability at the Z lines in muscle cells
Cell membrane, sarcolemmaCytoplasm, cytoskeletonCytoplasm, myofibril, sarcomere, Z line
Myopathy, myofibrillar, 3
A form of myofibrillar myopathy, a group of chronic neuromuscular disorders characterized at ultrastructural level by disintegration of the sarcomeric Z disk and myofibrils, and replacement of the normal myofibrillar markings by small dense granules, or larger hyaline masses, or amorphous material. MFM3 is characterized by progressive skeletal muscle weakness greater distally than proximally, tight heel cords, hyporeflexia, cardiomyopathy and peripheral neuropathy in some patients. Affected muscle exhibits disorganization and streaming of the Z-line, presence of large hyaline structures, excessive accumulation of myotilin and other ectopically expressed proteins and prominent congophilic deposits.
Key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of the cross-links are the main determinants of sarcomere extensibility properties of muscle. In non-muscle cells, seems to play a role in chromosome condensation and chromosome segregation during mitosis. Might link the lamina network to ch
CytoplasmNucleus
Myopathy, myofibrillar, 9, with early respiratory failure
An autosomal dominant myopathy characterized by adulthood onset of weakness in proximal, distal, axial and respiratory muscles. Pelvic girdle weakness, foot drop and neck weakness are the main symptoms at onset, but ultimately the weakness usually involves the proximal compartment of both upper and lower limbs. Additional features include variable degrees of Achilles tendon contractures, spinal rigidity and muscle hypertrophy. Respiratory involvement often leads to requirement for non-invasive ventilation support.
May function as an adapter in striated muscle to couple protein kinase C-mediated signaling via its LIM domains to the cytoskeleton
Cytoplasm, perinuclear regionCell projection, pseudopodiumCytoplasm, cytoskeletonCytoplasm, myofibril, sarcomere, Z line
Cardiomyopathy, dilated, 1C, with or without left ventricular non-compaction
A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. Cardiomyopathy dilated type 1C is associated with left ventricular non-compaction in some patients. Left ventricular non-compaction is characterized by numerous prominent trabeculations and deep intertrabecular recesses in hypertrophied and hypokinetic segments of the left ventricle.
May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. In lens epithelial cells, stabilizes the ATP6V1A protein, preventing its degradation by the proteasome (By similarity)
CytoplasmNucleusSecretedLysosome
Myopathy, myofibrillar, 2A, adult-onset
A form of myofibrillar myopathy, a group of chronic neuromuscular disorders characterized at ultrastructural level by disintegration of the sarcomeric Z disk and myofibrils, and replacement of the normal myofibrillar markings by small dense granules, or larger hyaline masses, or amorphous material. MFM2A is an autosomal dominant form characterized by weakness of the proximal and distal limb muscles, weakness of the neck, velopharynx and trunk muscles, respiratory insufficiency, hypertrophic cardiomyopathy, and cataract.
Medicamentos aprovados (FDA)
1 medicamento encontrado nos registros da FDA americana.
Variantes genéticas (ClinVar)
432 variantes patogênicas registradas no ClinVar.
Vias biológicas (Reactome)
42 vias biológicas associadas aos genes desta condição.
Diagnóstico
Os sinais que médicos procuram e os exames que confirmam
Tratamento e manejo
Remédios, cuidados de apoio e o que precisa acompanhar
Onde tratar no SUS
Hospitais de referência no Brasil e o protocolo oficial do SUS (PCDT)
🇧🇷 Atendimento SUS — Miopatia distal autossômica dominante
Selecione um estado ou use sua localização para ver resultados.
Dados de DATASUS/CNES, SBGM, ABNeuro e Ministério da Saúde. Sempre confirme a disponibilidade diretamente com o estabelecimento.
Pesquisa ativa
Ensaios clínicos abertos e novidades científicas recentes
Ensaios em destaque
Pesquisa e ensaios clínicos
0 ensaios clínicos encontrados.
Publicações mais relevantes
Autosomal dominant distal myopathy due to p.Ser85Cys mutation in the MATR3 gene: Novel case series and literature review.
Matrin-3 autosomal dominant myopathy, most commonly caused by a Ser85Cys (S85C) missense mutation, is a rare distal myopathy, presenting a heterogeneous phenotype. We report the clinical, physiological, radiological, and histological features of the first Portuguese patients diagnosed with p.Ser85Cys MATR3-related myopathy using a specific gene panel dedicated to "distal myopathies". Additionally, a narrative review of the literature was performed to contextualize our findings within the broader landscape of MATR3-related pathologies. Our case series describes the clinical findings of three patients diagnosed and followed in our center. The first patient was a 57-year-old male presenting with lower limb weakness, followed by loss of muscle force for fine motor gestures in the distal upper limb. Neurological examination revealed important muscle atrophy of the distal limbs and symmetrical motor deficit. The second patient, the brother of the aforementioned subject, was a 54-year-old male with similar symptoms associated with dysphagia and dysphonia. The third patient was a 58-year-old female, unrelated to the previous patients, presenting with distal weakness in the upper limbs and severe Achillean contractures. All three patients were investigated using needle electromyography and whole-body magnetic resonance imaging that disclosed a fatty infiltration pattern in the gastrocnemius, soleus, and tibialis anterior muscles. A muscle biopsy was performed solely for one patient and revealed rimmed vacuoles, consistent with previous reports. Genetic analysis found the same mutation in all three cases: c.254C>G, p.Ser85Cys in the MATR3 gene. The literature review included nine articles reporting families diagnosed with the p.Ser85Cys mutation in the MATR3 gene, and the main phenotypes associated with this genetic variant. Despite being a rare myopathy, with only a few cases reported, MATR3 gene mutations should be considered in patients with distal myopathy and rimmed vacuoles on muscle biopsy.
Dominant Distal Myopathy 3 (MPD3) Caused by a Deletion in the HNRNPA1 Gene.
To determine the genetic cause of the disease in the previously reported family with adult-onset autosomal dominant distal myopathy (myopathy, distal, 3; MPD3). Continued clinical evaluation including muscle MRI and muscle pathology. A linkage analysis with single nucleotide polymorphism arrays and genome sequencing were used to identify the genetic defect, which was verified by Sanger sequencing. RNA sequencing was used to investigate the transcriptional effects of the identified genetic defect. Small hand muscles (intrinsic, thenar, and hypothenar) were first involved with spread to the lower legs and later proximal muscles. Dystrophic changes with rimmed vacuoles and cytoplasmic inclusions were observed in muscle biopsies at advanced stage. A single nucleotide polymorphism array confirmed the previous microsatellite-based linkage to 8p22-q11 and 12q13-q22. Genome sequencing of three affected family members combined with structural variant calling revealed a small heterozygous deletion of 160 base pairs spanning the second last exon 10 of the heterogeneous nuclear ribonucleoprotein A1 (HNRNPA1) gene, which is in the linked region on chromosome 12. Segregation of the mutation with the disease was confirmed by Sanger sequencing. RNA sequencing showed that the mutant allele produces a shorter mutant mRNA transcript compared with the wild-type allele. Immunofluorescence studies on muscle biopsies revealed small p62 and larger TDP-43 inclusions. A small exon 10 deletion in the gene HNRNPA1 was identified as the cause of MPD3 in this family. The new HNRNPA1-related phenotype, upper limb presenting distal myopathy, was thus confirmed, and the family displays the complexities of gene identification.
Actininopathy: A new muscular dystrophy caused by ACTN2 dominant mutations.
To clinically and pathologically characterize a cohort of patients presenting with a novel form of distal myopathy and to identify the genetic cause of this new muscular dystrophy. We studied 4 families (3 from Spain and 1 from Sweden) suffering from an autosomal dominant distal myopathy. Affected members showed adult onset asymmetric distal muscle weakness with initial involvement of ankle dorsiflexion later progressing also to proximal limb muscles. In all 3 Spanish families, we identified a unique missense variant in the ACTN2 gene cosegregating with the disease. The affected members of the Swedish family carry a different ACTN2 missense variant. ACTN2 encodes for alpha actinin2, which is highly expressed in the sarcomeric Z-disk with a major structural and functional role. Actininopathy is thus a new genetically determined distal myopathy. ANN NEUROL 2019;85:899-906.
A novel mutation in TTN gene in a Saudi patient with bilateral facial weakness and scapular winging.
Titin (TTN) is a large gene with 363 exons that encodes a large abundant protein (longest known polypeptide in nature) that is expressed in cardiac and skeletal muscles. TTN has an important role in the sarcomere organization, assembly of muscles, transmission of the force at the Z-line, passive myocyte stiffness, and resting tension maintenance in the I-band region. Mutation in extreme C terminus of TTN, situated at the end of M-band of the TTN in chromosome 2q31, results in tibial muscular dystrophy (TMD), also called Udd Distal Myopathy, which is an autosomal dominant distal myopathy. In this article, we report a novel mutation in TTN gene in a Saudi patient with bilateral facial weakness and scapular winging. This report adds to the literature a heterozygous missense variant c.85652C>G, p.(Pro28551Arg) in TTN gene, which may be related to genes that cause the disease, but more case validation is needed. The novel mutation described in the present study widened the genetic spectrum of TTN-associated diseases, which may benefit studies addressing this disease in the future.
Autosomal dominant distal myopathy with nemaline rods due to p.Glu197Asp mutation in ACTA1.
In a previous report of a new phenotype with predominant scapulo-humeral-peroneal-distal myopathy associated with the Glu197Asp mutation in ACTA1, muscle biopsies did not show nemaline rods, nor could nemaline rods formation be demonstrated in an exhaustive functional in vivo or in vitro study. However, muscle biopsy in members of our family, carrying a similar clinical phenotype of some members of the original family and the same ACTA1 mutation, revealed the presence of numerous nemaline rods, suggesting that there must be other factors that explain the absence of nemaline rods.
Publicações recentes
Autosomal dominant distal myopathy due to p.Ser85Cys mutation in the MATR3 gene: Novel case series and literature review.
Dominant Distal Myopathy 3 (MPD3) Caused by a Deletion in the HNRNPA1 Gene.
A novel mutation in TTN gene in a Saudi patient with bilateral facial weakness and scapular winging.
Actininopathy: A new muscular dystrophy caused by ACTN2 dominant mutations.
Autosomal dominant distal myopathy with nemaline rods due to p.Glu197Asp mutation in ACTA1.
📚 EuropePMC16 artigos no totalmostrando 9
Autosomal dominant distal myopathy due to p.Ser85Cys mutation in the MATR3 gene: Novel case series and literature review.
Revue neurologiqueDominant Distal Myopathy 3 (MPD3) Caused by a Deletion in the HNRNPA1 Gene.
Neurology. GeneticsA novel mutation in TTN gene in a Saudi patient with bilateral facial weakness and scapular winging.
Intractable & rare diseases researchActininopathy: A new muscular dystrophy caused by ACTN2 dominant mutations.
Annals of neurologyAutosomal dominant distal myopathy with nemaline rods due to p.Glu197Asp mutation in ACTA1.
Neuromuscular disorders : NMDAutosomal dominant distal myopathy due to a novel ACTA1 mutation.
Neuromuscular disorders : NMDTransgenic mice overexpressing the ALS-linked protein Matrin 3 develop a profound muscle phenotype.
Acta neuropathologica communicationsMyoimaging in the NGS era: the discovery of a novel mutation in MYH7 in a family with distal myopathy and core-like features--a case report.
BMC medical geneticsSQSTM1 splice site mutation in distal myopathy with rimmed vacuoles.
NeurologyAssociações
Organizações que acompanham esta doença — pra ter apoio e orientação
Ainda não temos associações cadastradas para Miopatia distal autossômica dominante.
É de uma associação que acompanha esta doença? Fale com a gente →
Comunidades
Grupos ativos de quem convive com esta doença aqui no Raras
Ainda não existe comunidade no Raras para Miopatia distal autossômica dominante
Pacientes, familiares e cuidadores se organizam em comunidades pra compartilhar experiências, fazer perguntas e se apoiar. Você pode ser o primeiro.
Tire suas dúvidas
Perguntas, dicas e experiências compartilhadas aqui na página
Participe da discussão
Faça login para postar dúvidas, compartilhar experiências e interagir com especialistas.
Fazer loginDoenças relacionadas
Doenças com sintomas parecidos — ajudam quem ainda está buscando diagnóstico
Referências e fontes
Bases de dados externas citadas neste artigo
Publicações científicas
Artigos indexados no PubMed ligados a esta doença no grafo RarasNet — título, periódico e PMID direto da fonte, sem intermediação de IA.
- Autosomal dominant distal myopathy due to p.Ser85Cys mutation in the MATR3 gene: Novel case series and literature review.
- Dominant Distal Myopathy 3 (MPD3) Caused by a Deletion in the HNRNPA1 Gene.
- Actininopathy: A new muscular dystrophy caused by ACTN2 dominant mutations.
- A novel mutation in TTN gene in a Saudi patient with bilateral facial weakness and scapular winging.
- Autosomal dominant distal myopathy with nemaline rods due to p.Glu197Asp mutation in ACTA1.
Bases de dados e fontes oficiais
Identificadores e referências canônicas usadas para montar este verbete.
- ORPHA:206650(Orphanet)
- MONDO:0016108(MONDO)
- GARD:20361(GARD (NIH))
- Variantes catalogadas(ClinVar)
- Busca completa no PubMed(PubMed)
- Q55785936(Wikidata)
Dados compilados pelo RarasNet a partir de fontes abertas (Orphanet, OMIM, MONDO, PubMed/EuropePMC, ClinicalTrials.gov, DATASUS, PCDT/MS). Este conteúdo é informativo e não substitui avaliação médica.
Conteúdo mantido por Agente Raras · Médicos e pesquisadores podem colaborar
