A miopatia de Cap é uma doença muscular congênita muito rara, ou seja, a pessoa já nasce com ela. Ela se manifesta com fraqueza nos músculos do rosto e nos que controlam a respiração. Além disso, está associada a deformidades (alterações na forma) na cabeça, no rosto e no tórax (peito). Também causa fraqueza nos músculos dos braços e das pernas, tanto os que ficam mais próximos do corpo quanto os que ficam mais distantes. Os sintomas aparecem ao nascer ou durante a infância. A fraqueza muscular progride lentamente, mas pode levar a um quadro clínico grave e, em alguns casos, ser fatal.
Introdução
O que você precisa saber de cara
A miopatia de Cap é uma doença muscular congênita muito rara, ou seja, a pessoa já nasce com ela. Ela se manifesta com fraqueza nos músculos do rosto e nos que controlam a respiração. Além disso, está associada a deformidades (alterações na forma) na cabeça, no rosto e no tórax (peito). Também causa fraqueza nos músculos dos braços e das pernas, tanto os que ficam mais próximos do corpo quanto os que ficam mais distantes. Os sintomas aparecem ao nascer ou durante a infância. A fraqueza muscular progride lentamente, mas pode levar a um quadro clínico grave e, em alguns casos, ser fatal.
Escala de raridade
<1/50kMuito rara
1/20kRara
1/10kPouco freq.
1/5kIncomum
1/2k
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Sinais e sintomas
O que aparece no corpo e com que frequência cada sintoma acontece
Partes do corpo afetadas
+ 11 sintomas em outras categorias
Características mais comuns
Os sintomas variam de pessoa para pessoa. Abaixo estão as 30 características clínicas mais associadas, ordenadas por frequência.
Linha do tempo da pesquisa
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Genética e causas
O que está alterado no DNA e como passa nas famílias
Genes associados
3 genes identificados com associação a esta condição. Padrão de herança: Autosomal dominant.
Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments
Cytoplasm, cytoskeleton
Congenital myopathy 4A, autosomal dominant
A muscular disorder characterized by onset of muscle weakness in infancy or childhood. Most affected individuals show mildly delayed motor development, hypotonia, generalized muscle weakness, and weakness of the proximal limb muscles and neck muscles, resulting in difficulty running and easy fatigability. Many patients have respiratory insufficiency with reduced vital capacity. Skeletal muscle biopsy shows nemaline rod inclusions, subsarcolemmal 'cap' structures, and fiber-type disproportion.
Component of the sarcomere that tethers together nebulin (skeletal muscle) and nebulette (cardiac muscle) to alpha-actinin, at the Z lines
CytoplasmNucleusCytoplasm, myofibril, sarcomereCytoplasm, myofibril, sarcomere, Z line
Congenital myopathy 24
An autosomal recessive muscular disorder characterized by slowly progressive muscle weakness and atrophy, mainly affecting the lower limbs and neck. Some patients may have mild cardiac or respiratory involvement, but they do not have respiratory failure. Muscle biopsy shows nemaline bodies.
Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. The non-muscle isoform may have a role in agonist-mediated receptor internalization
Cytoplasm, cytoskeleton
Congenital myopathy 23
An autosomal dominant muscular disorder characterized clinically by hypotonia and muscle weakness, and a static or slowly progressive clinical course. Disease onset ranges from birth to childhood. Histologic examination of muscle fibers shows various anomalies including fiber type disproportion, an irregular myofibrillar network, abnormal thread-like or rod-shaped structures, and cap-like structures which are well demarcated and peripherally located under the sarcolemma with abnormal accumulation of sarcomeric proteins.
Variantes genéticas (ClinVar)
497 variantes patogênicas registradas no ClinVar.
Classificação de variantes (ClinVar)
Distribuição de 2 variantes classificadas pelo ClinVar.
Vias biológicas (Reactome)
4 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 de Cap
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Dados de DATASUS/CNES, SBGM, ABNeuro e Ministério da Saúde. Sempre confirme a disponibilidade diretamente com o estabelecimento.
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Publicações mais relevantes
Novel autosomal dominant TPM3 mutation causes a combined congenital fibre type disproportion-cap disease histological pattern.
Tropomyosin 3 (TPM3) gene mutations associate with autosomal dominant and recessive nemaline myopathy 1 (NEM1), congenital fiber type disproportion myopathy (CFTD) and cap myopathy (CAPM1), and a combination of caps and nemaline bodies. We report on a 47-year-old man with polyglobulia, restricted vital capacity and mild apnea hypopnea syndrome, requiring noninvasive ventilation. Physical assessment revealed bilateral ptosis and facial paresis, with high arched palate and retrognathia; global hypotonia and diffuse axial weakness, including neck and upper and lower limb girdle and foot dorsiflexion weakness. Whole body MRI showed a diffuse fatty replacement with an unspecific pattern. A 122 gene NGS neuromuscular disorders panel revealed the heterozygous VUS c.709G>A (p.Glu237Lys) on exon 8 of TMP3. A deltoid muscle biopsy showed a novel histological pattern combining fiber type disproportion and caps. Our findings support the pathogenicity of the novel TPM3 variant and widen the phenotypic gamut of TMP3-related congenital myopathy.
A pathogenic mechanism associated with myopathies and structural birth defects involves TPM2-directed myogenesis.
Nemaline myopathy (NM) is the most common congenital myopathy, characterized by extreme weakness of the respiratory, limb, and facial muscles. Pathogenic variants in Tropomyosin 2 (TPM2), which encodes a skeletal muscle-specific actin binding protein essential for sarcomere function, cause a spectrum of musculoskeletal disorders that include NM as well as cap myopathy, congenital fiber type disproportion, and distal arthrogryposis (DA). The in vivo pathomechanisms underlying TPM2-related disorders are unknown, so we expressed a series of dominant, pathogenic TPM2 variants in Drosophila embryos and found 4 variants significantly affected muscle development and muscle function. Transient overexpression of the 4 variants also disrupted the morphogenesis of mouse myotubes in vitro and negatively affected zebrafish muscle development in vivo. We used transient overexpression assays in zebrafish to characterize 2 potentially novel TPM2 variants and 1 recurring variant that we identified in patients with DA (V129A, E139K, A155T, respectively) and found these variants caused musculoskeletal defects similar to those of known pathogenic variants. The consistency of musculoskeletal phenotypes in our assays correlated with the severity of clinical phenotypes observed in our patients with DA, suggesting disrupted myogenesis is a potentially novel pathomechanism of TPM2 disorders and that our myogenic assays can predict the clinical severity of TPM2 variants.
Nemaline Rod/Cap Myopathy Due to Novel Homozygous MYPN Mutations: The First Report from South Asia and Comprehensive Literature Review.
Pathogenic variants in the myopalladin gene (MYPN) are known to cause mildly progressive nemaline/cap myopathy. Only nine cases have been reported in the English literature. A detailed evaluation was conducted of the clinical, muscle magnetic resonance imaging (MRI), and genetic findings of two unrelated adults with MYPN-related cap myopathy. Genetic analysis was performed using whole-exome sequencing. MRI was performed on a 1.5-T device in patient 1. Two unrelated adults born to consanguineous parents, a 28-year-old male and a 23-year-old female, were diagnosed with pathogenic variants in MYPN that cause cap myopathy. Both patients presented with early-onset, insidiously progressive, and minimally disabling proximodistal weakness with mild ptosis, facial weakness, and bulbar symptoms. Patient 1 had a prominent foot drop from the onset. Both patients were followed up at age 30 years, at which point serum creatine kinase concentrations were minimally elevated. There were no cardiac symptoms; electrocardiograms and two-dimensional echocardiograms were normal in both patients. Muscle MRI revealed preferential involvement of the glutei, posterior thigh muscles, and anterior leg muscles. Whole-exome sequencing revealed significant homozygous splice-site variants in both of the probands, affecting intron 10 of MYPN: c.1973+1G>C (patient 1) and c.1974-2A>C (patient 2). This study elaborates on two patients with homozygous MYPN pathogenic variants, presenting as slowly progressive congenital myopathy. These patients are only the tenth and eleventh cases reported in the English literature, and the first from South Asia. The clinical phenotype reiterates the mild form of nemaline rod/cap myopathy. A comprehensive literature review is presented.
Whole genome sequencing reveals biallelic PLA2G6 mutations in siblings with cerebellar atrophy and cap myopathy.
The R168G heterozygous mutation of tropomyosin 3 (TPM3) was identified in three family members and has manifestations ranging from asymptotic to serve scoliosis and respiratory complications.
According to existing reports, mutations in the slow tropomyosin gene (TPM3) may lead to congenital fiber-type disproportion (CFTD), nemaline myopathy (NM) and cap myopathy (CD). They are all congenital myopathies and are associated with clinical, pathological and genetic heterogeneity. A ten-year-old girl with scoliosis was unable to wean from mechanical ventilation after total intravenous anesthesia. The girl has scoliosis, respiratory insufficiency, motion delay and muscle weakness; her younger brother has a similar physiology but does not have scoliosis or respiratory insufficiency, and her parents are healthy. We conducted genetic testing and found a c.502C > G (p.R168G) heterozygous mutation in the family. This mutation originated from the father and was autosomal dominant. Muscle biopsy results indicated that no special structures were present, and the type I fiber ratio was not notably high compared to previous reports. Although the family members have the same mutations, their clinical manifestations are quite different.
Publicações recentes
Novel autosomal dominant TPM3 mutation causes a combined congenital fibre type disproportion-cap disease histological pattern.
A pathogenic mechanism associated with myopathies and structural birth defects involves TPM2-directed myogenesis.
Nemaline Rod/Cap Myopathy Due to Novel Homozygous MYPN Mutations: The First Report from South Asia and Comprehensive Literature Review.
Whole genome sequencing reveals biallelic PLA2G6 mutations in siblings with cerebellar atrophy and cap myopathy.
Respiratory Failure as the Presenting Symptom in a Sporadic Case of Cap Myopathy.
📚 EuropePMC13 artigos no totalmostrando 14
Novel autosomal dominant TPM3 mutation causes a combined congenital fibre type disproportion-cap disease histological pattern.
Neuromuscular disorders : NMDA pathogenic mechanism associated with myopathies and structural birth defects involves TPM2-directed myogenesis.
JCI insightNemaline Rod/Cap Myopathy Due to Novel Homozygous MYPN Mutations: The First Report from South Asia and Comprehensive Literature Review.
Journal of clinical neurology (Seoul, Korea)Whole genome sequencing reveals biallelic PLA2G6 mutations in siblings with cerebellar atrophy and cap myopathy.
Clinical geneticsRespiratory Failure as the Presenting Symptom in a Sporadic Case of Cap Myopathy.
Journal of neuropathology and experimental neurologyThe R168G heterozygous mutation of tropomyosin 3 (TPM3) was identified in three family members and has manifestations ranging from asymptotic to serve scoliosis and respiratory complications.
Genes & diseasesMyopalladin promotes muscle growth through modulation of the serum response factor pathway.
Journal of cachexia, sarcopenia and muscleCongenital myopathy with hanging big toe due to homozygous myopalladin (MYPN) mutation.
Skeletal muscleDominantly inherited distal nemaline/cap myopathy caused by a large deletion in the nebulin gene.
Neuromuscular disorders : NMDThe Primary Causes of Muscle Dysfunction Associated with the Point Mutations in Tpm3.12; Conformational Analysis of Mutant Proteins as a Tool for Classification of Myopathies.
International journal of molecular sciencesThe reason for the low Ca2+-sensitivity of thin filaments associated with the Glu41Lys mutation in the TPM2 gene is "freezing" of tropomyosin near the outer domain of actin and inhibition of actin monomer switching off during the ATPase cycle.
Biochemical and biophysical research communicationsMolecular mechanisms of dysfunction of muscle fibres associated with Glu139 deletion in TPM2 gene.
Scientific reportsRecessive MYPN mutations cause cap myopathy with occasional nemaline rods.
Annals of neurologySevere congenital actin related myopathy with myofibrillar myopathy features.
Neuromuscular disorders : NMDAssociações
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Comunidades
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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.
- Novel autosomal dominant TPM3 mutation causes a combined congenital fibre type disproportion-cap disease histological pattern.
- A pathogenic mechanism associated with myopathies and structural birth defects involves TPM2-directed myogenesis.
- Nemaline Rod/Cap Myopathy Due to Novel Homozygous MYPN Mutations: The First Report from South Asia and Comprehensive Literature Review.
- Whole genome sequencing reveals biallelic PLA2G6 mutations in siblings with cerebellar atrophy and cap myopathy.
- The R168G heterozygous mutation of tropomyosin 3 (TPM3) was identified in three family members and has manifestations ranging from asymptotic to serve scoliosis and respiratory complications.
- Respiratory Failure as the Presenting Symptom in a Sporadic Case of Cap Myopathy.
Bases de dados e fontes oficiais
Identificadores e referências canônicas usadas para montar este verbete.
- ORPHA:171881(Orphanet)
- MONDO:0015753(MONDO)
- GARD:11915(GARD (NIH))
- Variantes catalogadas(ClinVar)
- Busca completa no PubMed(PubMed)
- Q56013758(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.
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