Alternative titles; symbols
SNOMEDCT: 129620000; ICD10CM: G71.09; ORPHA: 53698, 636965; DO: 0111269;
| Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
Gene/Locus |
Gene/Locus MIM number |
|---|---|---|---|---|---|---|
| 14q11.2 | Congenital myopathy 7A, myosin storage, autosomal dominant | 608358 | Autosomal dominant | 3 | MYH7 | 160760 |
A number sign (#) is used with this entry because of evidence that autosomal dominant myosin storage congenital myopathy-7A (CMYO7A) is caused by heterozygous mutation in the MYH7 gene (160760) on chromosome 14q11.
Biallelic mutation in the MYH7 gene causes autosomal recessive myosin storage congenital myopathy-7B (CMYO7B; 255160).
Autosomal dominant myosin storage congenital myopathy-7A (CMYO7A) is a skeletal muscle disorder with wide phenotypic variability. The age at symptom onset can range from early childhood to late adulthood. Affected individuals have proximal muscle weakness affecting the upper and lower limbs and distal muscle weakness of the lower limbs, resulting in gait difficulties and scapular winging (scapuloperoneal myopathy). Additional features may include thin habitus, high-arched palate, foot drop, pes cavus, calf pseudohypertrophy, and decreased reflexes. The severity is also variable: some patients develop respiratory insufficiency, joint contractures, and scoliosis in the first decades, whereas others are clinically unaffected, but show subtle signs of the disorder on examination. Serum creatine kinase may be normal or elevated. The disease is usually slowly progressive and most patients remain ambulatory. Skeletal muscle biopsy can show different abnormalities, including hyaline bodies, type 1 fiber predominance, congenital fiber-type disproportion (CFTD), and nonspecific myopathic changes with myofibrillar disarray. Intrafamilial variability is common (Dye et al., 2006; Pegoraro et al., 2007; review by Tajsharghi and Oldfors, 2013).
For a discussion of genetic heterogeneity of congenital myopathy, see CMYO1A (117000).
Cancilla et al. (1971) described a brother and sister with a congenital myopathy in which they noted probable lysis of type I myofibrils. A fine granular material that stained intensely with the myosin ATPase reaction had accumulated within the fibers. Dye et al. (2006) stated that the disease progressed over the years in the patients reported by Cancilla et al. (1971). The sister developed joint contractures of her limbs, severe scoliosis, and required ventilatory assistance. She died at age 25 years from bronchopneumonia after exploratory abdominal surgery for appendicitis. Her younger brother had scoliosis with fusion rod and tracheotomy at the age of 30 years. In 1 of the affected sibs originally reported by Cancilla et al. (1971), Dye et al. (2006) identified a heterozygous mutation in the MYH7 gene (L1793P; 160760.0037), confirming that the disease in that family was autosomal dominant myosin storage myopathy.
Ceuterick et al. (1993) reported a 10-year-old Belgian boy with nonprogressive myopathy. Muscle biopsy showed hyaline bodies in type I fibers that stained with the myosin ATPase reaction at pH 4.2 and with polyclonal antiskeletal myosin. Immunoreactive deposits to antidesmin were observed at the border of some hyaline bodies. Ultrastructurally, the hyaline bodies were not surrounded by a limiting membrane and were only localized in subsarcolemmal areas. Periodic acid Schiff (PAS) staining for polysaccharides was negative. Laing et al. (2005) reported follow-up of this patient, who was 21 years of age and worked as an electrician. He had a nonprogressive limb-girdle myopathy since childhood, but did not show muscle weakness. Physical examination showed a thin man with high-arched palate, kyphosis, mild scapular winging, and enlarged calves. An unrelated 57-year-old Belgian woman presented at age 53 with proximal muscle weakness affecting the upper and lower limbs. She had scapular winging, hyperlordosis with a waddling gait, and weak reflexes. Neither patient had a family history of a similar disorder. Genetic analysis identified a heterozygous mutation in the MYH7 gene (R1845W; 160760.0028) in both patients.
Fananapazir et al. (1993) demonstrated that many patients with hypertrophic cardiomyopathy (CMH1; 192600) due to mutation in the MYH7 gene have histologic changes on soleus muscle biopsy consistent with central core disease. A few of the patients with CMH1 they reported had 'significant muscle weakness.' Two adults and 3 children from a family with the L908V mutation (160760.0010) in the MYH7 gene were observed to have pathologic changes in the soleus muscle with no cardiac hypertrophy as defined by echocardiogram. The histologic hallmark was the absence of mitochondria in the center of many type I fibers as revealed by light microscopic examination of NADH-stained fresh-frozen skeletal muscle sections. McKenna (1993), who stated that he had never seen clinical evidence of skeletal myopathy in CMH1, doubted the significance of the findings.
Barohn et al. (1994) reported 2 patients with sporadic hyaline body myopathy since infancy: a 40-year-old male and a 3-year-old female. Both had numerous subsarcolemmal glassy, hyaline bodies in 20 to 30% of type I muscle fibers. The hyaline bodies stained negative for PAS and oxidative enzymes, contained amorphous granular material, but were not contained within a membrane.
Masuzugawa et al. (1997) reported a family in which 7 members over 4 generations developed slowly progressive scapuloperoneal muscle weakness and atrophy with an age at onset ranging from the first to fifth decade. Muscle biopsy of 2 patients showed subsarcolemmal hyaline bodies in approximately 20% of type I fibers. The hyaline bodies showed myofibrillar ATPase activity and stained intensely with antibodies to slow myosin heavy chain. Ultrastructurally, the hyaline bodies consisted of granules in linear array, filaments, or amorphous materials.
Bohlega et al. (2003) reported a Saudi Arabian kindred in which 11 members, including a mother, her father, and 8 of her 13 children, were affected with hyaline body myopathy inherited in an autosomal dominant pattern. The phenotype was clinically heterogeneous. Most patients had symptom onset by 2 years of age with proximal muscle weakness of the lower limbs resulting in difficulty walking; 1 patient had onset at age 12 years. The 47-year-old mother had onset at age 42 years and showed a rapidly progressive course with loss of ambulation at age 45. Some patients had proximal muscle weakness of the upper limbs, resulting in scapular winging, and some had distal muscle weakness of the lower limbs, causing foot drop. More variable features included positive Gowers sign, thin habitus with decreased subcutaneous fat, pectus excavatum, high-arched palate, scoliosis, calf pseudohypertrophy, and restrictive lung disease. Besides the mother, only 1 patient lost ambulation, at age 18. Serum creatine kinase was elevated in all patients. Bohlega et al. (2003) noted 2 disease patterns: a nonprogressive minimal generalized muscle wasting and weakness since childhood, and a relentlessly progressive weakness starting at age 2 years with proximal arm and hand weakness, scapular winging, and severe functional impairment. Muscle biopsies showed subsarcolemmal hyaline bodies in type I fibers that were positive for ATPase and heavy chain slow myosin. Ultrastructurally, the hyaline bodies were granular and filamentous or amorphous, surrounded by disorganized sarcomeres. There were also many signs of myopathy, including fiber-type grouping, angulated fibers, fiber necrosis, fibrosis, and central nucleation. In affected members of the family reported by Bohlega et al. (2003), Bohlega et al. (2004) identified a heterozygous mutation in the MYH7 gene (H1904L; 160760.0031).
Tajsharghi et al. (2003) reported a patient with slowly progressive muscle weakness since childhood, when his gait was affected by hip weakness, but he was able to climb stairs and even run. He also had shoulder girdle weakness, bilateral winging of the scapulae, and pseudohypertrophy of the calves. By age 71 years, he was severely weak in the proximal muscles and moderately weak in the distal muscles. Lung vital capacity was 57% of normal, serum creatine kinase was elevated, and EMG findings were consistent with a myopathy. There were no signs of cardiomyopathy clinically or by imaging, although he did have atrial fibrillation. His mother had had similar symptoms, with hip and shoulder girdle weakness, as well as atrial fibrillation. One of 3 children (a daughter) of the proband was also affected. Tajsharghi et al. (2003) also reported an unrelated 33-year-old woman with a similar phenotype, including waddling gait, winging of the scapulae, pseudohypertrophy of the calves, and normal cardiac findings. None of her family members was affected. Muscle biopsy in the proband of the first family showed type 1 fiber predominance and increased interstitial fat and connective tissue. Inclusion bodies consisting of the beta cardiac myosin heavy chain were present in the majority of type 1 fibers, but not in type 2 fibers. The authors termed the disorder 'myosin storage myopathy.' In affected members of a family and in an unrelated patient with CMYO7A, Tajsharghi et al. (2003) identified a heterozygous mutation in the MYH7 gene (R1845W; 160760.0028).
Sobrido et al. (2005) reported a large Spanish family with a congenital myopathy inherited in an autosomal dominant pattern. Seven of 25 examined family members were affected. Onset of slowly progressive muscle weakness was in early childhood, manifest by clumsiness and difficulty running, climbing stairs, and getting up from the floor. As adults, all retained independent ambulation but demonstrated waddling gait, proximal upper and lower extremity weakness and atrophy, weakness of foot dorsiflexors, and hypo- or areflexia. Notably, none of the affected individuals had neonatal respiratory or sucking difficulties. MRI studies showed loss of volume and fatty infiltration of proximal muscles; EMG showed myopathic changes. Skeletal muscle biopsies of 2 affected individuals showed characteristic findings of CFTD without dystrophic changes. No mutations were identified in the coding sequence of the ACTA1 gene (102610). Ortolano et al. (2011) reported follow-up of the family reported by Sobrido et al. (2005), noting that there were 12 affected members spanning 5 generations. The patients had an early-onset, slowly progressive predominantly proximal myopathy with mild distal involvement and no signs of cardiomyopathy. Skeletal muscle samples were available from 3 patients (at ages 25, 43, and 62). All showed features of CFTD, and the oldest patient demonstrated subsarcolemmal hyaline accumulation in type 1 muscle fibers, suggesting that the pathologic findings can change over time. Genetic analysis of this family identified a heterozygous mutation in the MYH7 gene (160760.0048).
Pegoraro et al. (2007) reported a large multigenerational family (family A) in which 9 individuals had variable manifestations of CMYO7A associated with a heterozygous missense mutation in the MYH7 gene (R1845W; 160760.0028). The proband was a 66-year-old man with a history of progressive weakness since childhood, delayed motor development, and clumsiness. At age 62, he had proximal muscle weakness and atrophy of the upper and lower limbs, a waddling gait, foot drop, pes cavus, scapular winging, and weakness of the anterior compartment of the distal leg. Muscle biopsy showed nonspecific myopathic changes, and he was diagnosed with scapuloperoneal myopathy. His 35-year-old niece had slowly progressive muscle weakness in the upper limbs since 7 to 8 years of age. As an adult, she had proximal muscle weakness of the upper and lower limbs, distal lower limb weakness, a waddling gait, foot drop, scapular winging, pes cavus, and quadriceps and calf hypertrophy. Muscle biopsy showed type 1 fiber predominance and hyaline bodies in type 1 fibers. Serum creatine kinase was elevated in both patients. Other family members with the mutation showed weakness of the upper and/or lower limbs with a variable age at onset ranging from childhood to adulthood. Many had scapular winging and pes cavus. Muscle MRI identified a unique pattern in the posterior compartment of the thigh, characterized by early involvement of the biceps femoris and semimembranosus, with relative sparing of the semitendinosus; distal leg muscles and upper limb muscles were also affected. Disease progression was slow, and all remained ambulatory. Four mutation carriers were asymptomatic at ages 29 to 43 years, but examination showed subtle features of the disease, including hyperCKemia. Pegoraro et al. (2007) also identified 2 members of another family (family B) with adult-onset of proximal and distal muscle weakness affecting the upper and lower limbs consistent with scapuloperoneal myopathy; hyaline bodies were found in the muscle biopsy of one. Genetic analysis in family B showed a heterozygous R1845W mutation in the MYH7 gene. The findings indicated that the absence of hyaline bodies in muscle biopsies does not rule out MYH7 gene mutations.
In a mother with myosin storage myopathy, who later developed hypertrophic cardiomyopathy (CMH1; 192600), and in her daughter, who had early-symptomatic left ventricular noncompaction (LVNC5; 613426), Uro-Coste et al. (2009) identified heterozygosity for a missense mutation in the MYH7 gene (L1793P; 160760.0037) The mother presented at age 30 years with proximal muscle weakness, which progressed to the point of her being wheelchair-bound by 48 years of age. At age 51, she was diagnosed with CMH. Skeletal muscle biopsy at age 53 showed subsarcolemmal accumulation of hyaline material in type 1 fibers. Her 24-year-old daughter presented with heart failure at 3 months of age and was diagnosed with early-onset cardiomyopathy. Angiography revealed a less-contractile, irregular 'spongiotic' wall in the inferior left ventricle, and echocardiography confirmed the diagnosis of LVNC. The daughter did not complain of muscle weakness, but clinical examination revealed bilateral wasting of the distal leg anterior compartment and she had some difficulty with heel-walking.
The transmission pattern of CMYO7A in the kindred reported by Bohlega et al. (2003) was consistent with autosomal dominant inheritance.
In a review, Tajsharghi and Oldfors (2013) noted that mutations in CMYO7A and CMYO7B are usually found in the distal rod region of the MYH7 gene.
In affected members of a family and in an unrelated patient with CMYO7A, Tajsharghi et al. (2003) identified a heterozygous mutation in the MYH7 gene (R1845W; 160760.0028).
In affected members of a Saudi Arabian family with autosomal dominant CMYO7A Bohlega et al. (2003), Bohlega et al. (2004) identified a heterozygous mutation in the MYH7 gene (H1904L; 160760.0031).
In a Belgian patient with myosin storage myopathy, originally reported by Ceuterick et al. (1993), Laing et al. (2005) identified a heterozygous mutation in the MYH7 gene (R1845W; 160760.0028).
In 1 of the affected sibs with congenital myopathy originally reported by Cancilla et al. (1971), Dye et al. (2006) identified a heterozygous mutation in the MYH7 gene (L1793P; 160760.0037), confirming that the disease in that family was autosomal dominant myosin storage myopathy. Dye et al. (2006) noted that contact with the family had been lost and DNA studies were performed on archival postmortem sections from the affected sister who died at age 25 years. The sibs presumably had the disease because of gonadal mosaicism in 1 of the unaffected parents, although this could not be confirmed.
In a large multigenerational family (family A) in which 9 individuals had variable manifestations of CMYO7A, Pegoraro et al. (2007) identified a heterozygous missense mutation in the MYH7 gene (R1845W; 160760.0028). Two affected members of another family (family B) carried the same heterozygous mutation.
In 12 affected members of a 5-generation Spanish family previously reported by Sobrido et al. (2005) with CMYO7A, Ortolano et al. (2011) identified a heterozygous mutation in the C-terminal region of the MYH7 gene (160760.0048). The mutation, which was found by a combination of linkage analysis and candidate gene sequencing, segregated with the disorder in the family. It was not present in 202 population controls. Two skeletal muscle samples studied had normal expression of type I and II myosin heavy chains, but only a younger patient showed decreased MYH7 transcript levels compared to controls.
Goebel and Warlo (2001) suggested that hyaline body myopathy may be related to a surplus of proteins present in a granular or filamentous form.
Armel and Leinwand (2009) analyzed the functional effects of 4 different MYH7 mutations in the rod or tail domain that were found to be responsible for myosin storage myopathy: R1845W (160760.0028), H1901L (160760.0031), E1886K (160760.0035), and L1793P (160760.0037). None of the mutations altered the secondary structure of the protein, but L1793P and H1901L showed decreased thermodynamic stability. All mutations decreased the extent of self-assembly of the light meromyosin rod (less than 50 to 60%) compared to the wildtype protein. R1845W and H1901L showed formation of more stable and larger filaments, whereas L1793P and E1886K showed more rapid filament degradation. Armel and Leinwand (2009) noted that the assembly of muscle filaments is a multistep process that involves both the proper folding of alpha-helices into coiled-coils, and the assembly of these coiled-coils, in proper register, into filaments, and concluded that defects in any one of these steps can result in improper filament formation leading to muscle disease.
Scapuloperoneal syndrome was initially described by Jules Broussard (1886) as 'une forme hereditaire d'atrophie musculaire progressive' beginning in the lower legs and affecting the shoulder region earlier and more severely than distal arm.
Thomas et al. (1975) described 6 cases of adult-onset scapuloperoneal myopathy. Four were apparently sporadic. The other 2 cases occurred in mother and daughter. Progression was relatively slow. Electromyography and muscle biopsy showed myopathic changes in all. Facial involvement occurred in some. The authors considered that the disorder resembled that described by Ricker and Mertens (1968) and Serratrice et al. (1969). The latter group observed 9 cases in which autosomal dominant inheritance was suggested.
Sahgal and Sahgal (1977) reported a patient with sporadic nonprogressive congenital myopathy with weakness and atrophy of the scapuloperoneal muscles. Muscle biopsy showed preferential atrophy of type I muscle fibers and subsarcolemmal bodies composed of an acid protein with ATPase activity.
Goebel et al. (1981) reported a 15-year-old girl with proximal muscle weakness since infancy. Milder distal muscle weakness was also present. Quadriceps muscle biopsy showed a predominance of type I muscle fibers with 'cytoplasmic bodies.' There was no family history.
Tawil et al. (1995) described 4 individuals in 2 generations, 1 female and 3 males, affected with a scapuloperoneal myopathy. There was male-to-male transmission. Electromyography demonstrated small polyphasic units, and muscle biopsy demonstrated necrotic and regenerating fibers as well as an increase in endomesial connective tissue, demonstrating this to be a myopathy. Although the index case fulfilled the diagnostic criteria for facioscapulohumeral dystrophy (158900), none of the other 3 affected individuals demonstrated facial weakness. Furthermore, linkage to markers on 4q35 was excluded, demonstrating this to be a distinct genetic entity.
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