G2Cdb::Human Disease report

Disease id
D00000255
Name
Myosin storage myopathy
Nervous system disease
no

Genes (1)

Gene Name/Description Mutations Found Literature Mutations Type Genetic association?
G00002430 MYH6
myosin, heavy chain 6, cardiac muscle, alpha
Y (15136674) Single nucleotide polymorphism (SNP) Y
G00002430 MYH6
myosin, heavy chain 6, cardiac muscle, alpha
Y (15699387) Single nucleotide polymorphism (SNP) Y
G00002430 MYH6
myosin, heavy chain 6, cardiac muscle, alpha
Y (16684601) Single nucleotide polymorphism (SNP) Y
G00002430 MYH6
myosin, heavy chain 6, cardiac muscle, alpha
Y (17118657) Single nucleotide polymorphism (SNP) Y
G00002430 MYH6
myosin, heavy chain 6, cardiac muscle, alpha
Y (17336526) Single nucleotide polymorphism (SNP) Y

References

  • MYH7 gene mutation in myosin storage myopathy and scapulo-peroneal myopathy.

    Pegoraro E, Gavassini BF, Borsato C, Melacini P, Vianello A, Stramare R, Cenacchi G and Angelini C

    Department of Neurosciences, University of Padova, Italy. elena.pegoraro@unipd.it

    In order to characterize, at the clinical, molecular and imaging level, myopathies due to MYH7 gene mutations, MYH7 gene analysis was conducted by RT-PCR/SSCP/sequencing in two patients diagnosed with myosin storage myopathy and 17 patients diagnosed with scapulo-peroneal myopathy of unknown etiology. MYH7 gene studies revealed the 5533C>T mutation (Arg1845Trp) in both myosin storage myopathy and in 2 of the 17 scapulo-peroneal patients studied. 5533C>T segregation analysis in the mutation carrier families identified 11 additional patients. The clinical spectrum in our cohort of patients included asymptomatic hyperCKemia, scapulo-peroneal myopathy and proximal and distal myopathy with muscle hypertrophy. 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. Muscle biopsy revealed hyaline bodies in only half of biopsied patients (2/4). In conclusion, phenotypic and histopathological variability may underlie MYH7 gene mutation and the absence of hyaline bodies in muscle biopsies does not rule out MYH7 gene mutations.

    Funded by: Telethon: GTF02009

    Neuromuscular disorders : NMD 2007;17;4;321-9

  • Myosin storage (hyaline body) myopathy: a case report.

    Shingde MV, Spring PJ, Maxwell A, Wills EJ, Harper CG, Dye DE, Laing NG and North KN

    Department of Pathology, University of Sydney, Australia. meena.shingde@email.cs.nsw.gov.au

    Myosin storage myopathy/hyaline body myopathy is a rare congenital myopathy, with less than 30 cases reported in the literature. It is characterised by the presence of subsarcolemmal hyaline bodies in type 1 muscle fibres and predominantly proximal muscle weakness. Recently, a single mutation (Arg1845Trp) in the slow/beta-cardiac myosin heavy chain gene (MYH7) was identified in four unrelated probands from Sweden and Belgium. The clinical severity and age of onset was variable, despite the same disease-causing mutation and similar histological findings. Here, we report the clinical and morphological findings of two brothers of English/Scottish background with the Arg1845Trp mutation in MYH7. This case report adds to the clinical description of this rare disorder and confirms that Arg1845Trp is a common mutation associated with this phenotype, at least in the White European population.

    Neuromuscular disorders : NMD 2006;16;12;882-6

  • Novel slow-skeletal myosin (MYH7) mutation in the original myosin storage myopathy kindred.

    Dye DE, Azzarelli B, Goebel HH and Laing NG

    Molecular Neurogenetics Laboratory, Centre for Medical Research, West Australian Institute for Medical Research, University of Western Australia M519, 'B' Block, Queen Elizabeth II Medical Centre, Nedlands, WA 6009, Australia.

    Myosin storage myopathy (OMIM 608358), a congenital myopathy characterised by subsarcolemmal, hyaline-like accumulations of myosin in Type I muscle fibres, was first described by Cancilla and Colleagues in 1971 [Neurology 1971;21:579-585] in two siblings as 'familial myopathy with probable lysis of myofibrils in type I muscle fibres'. Two mutations in the slow skeletal myosin heavy chain gene (MYH7) have recently been associated with the disease in other families. We have identified a novel heterozygous Leu1793Pro mutation in MYH7 in DNA from paraffin sections of one of the original siblings. This historical molecular analysis confirms the original cases had myosin storage myopathy.

    Neuromuscular disorders : NMD 2006;16;6;357-60

  • Myosin storage myopathy: slow skeletal myosin (MYH7) mutation in two isolated cases.

    Laing NG, Ceuterick-de Groote C, Dye DE, Liyanage K, Duff RM, Dubois B, Robberecht W, Sciot R, Martin JJ and Goebel HH

    Centre for Neuromuscular and Neurologic Disorders, Australian Neuromuscular Research Institute and Centre for Medical Research, University of Western Australia, QEII Medical Centre, Nedlands, Australia. nlaing@cyllene.uwa.edu.au

    Myosin storage myopathy is a congenital myopathy characterized by subsarcolemmal hyaline bodies in type 1 muscle fibers, which are ATPase positive and thus contain myosin. Mutations recently were identified in the type 1 muscle fiber myosin gene (MYH7) in Swedish and Saudi families with myosin storage myopathy. The authors have identified the arginine 1845 tryptophan mutation found in the Swedish families in two isolated Belgian cases, indicating a critical role for myosin residue arginine 1845.

    Neurology 2005;64;3;527-9

  • Mutation of the slow myosin heavy chain rod domain underlies hyaline body myopathy.

    Bohlega S, Abu-Amero SN, Wakil SM, Carroll P, Al-Amr R, Lach B, Al-Sayed Y, Cupler EJ and Meyer BF

    Department of Neurosciences, King Faisal Specialist Hospital and Research Centre, Riyadh, Saudi Arabia.

    Objective: To identify the gene and specific mutation underlying hyaline body myopathy in the family studied.

    Methods: A microsatellite-based whole genome scan was performed. Linkage analysis assumed autosomal dominant inheritance and equal allele frequencies. A candidate gene approach within the linked interval and direct sequencing were used for mutation detection.

    Results: Initial analysis indicated a maximum lod score of 3.01 at D14S1280. High-density mapping surrounding the linked locus was performed. Multipoint analysis showed that the linked region with a maximum lod score of 3.01 extended from D14S742 to D14S608 with a peak non-parametric linkage (NPL) score of 3.75 at D14S608. The myosin heavy chain genes MYH6 and MYH7 map to the region between D14S742 and D14S1280. Sequence analysis of the coding regions of MYH7 revealed an A-->T transversion at nucleotide position 25596 (M57965) resulting in a histidine-to-leucine amino acid change at residue 1904 (H1904L).

    Conclusion: Pathogenicity of the MYH7 H1904L mutation most likely results from disruption of myosin heavy chain assembly or stability of the sarcomeric protein. The MYH7 tail domain mutation results in an inclusion body myopathy with an apparent absence of hypertrophic cardiomyopathy usually associated with mutations of this gene.

    Neurology 2004;62;9;1518-21

Literature (5)

Pubmed - human_disease

  • MYH7 gene mutation in myosin storage myopathy and scapulo-peroneal myopathy.

    Pegoraro E, Gavassini BF, Borsato C, Melacini P, Vianello A, Stramare R, Cenacchi G and Angelini C

    Department of Neurosciences, University of Padova, Italy. elena.pegoraro@unipd.it

    In order to characterize, at the clinical, molecular and imaging level, myopathies due to MYH7 gene mutations, MYH7 gene analysis was conducted by RT-PCR/SSCP/sequencing in two patients diagnosed with myosin storage myopathy and 17 patients diagnosed with scapulo-peroneal myopathy of unknown etiology. MYH7 gene studies revealed the 5533C>T mutation (Arg1845Trp) in both myosin storage myopathy and in 2 of the 17 scapulo-peroneal patients studied. 5533C>T segregation analysis in the mutation carrier families identified 11 additional patients. The clinical spectrum in our cohort of patients included asymptomatic hyperCKemia, scapulo-peroneal myopathy and proximal and distal myopathy with muscle hypertrophy. 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. Muscle biopsy revealed hyaline bodies in only half of biopsied patients (2/4). In conclusion, phenotypic and histopathological variability may underlie MYH7 gene mutation and the absence of hyaline bodies in muscle biopsies does not rule out MYH7 gene mutations.

    Funded by: Telethon: GTF02009

    Neuromuscular disorders : NMD 2007;17;4;321-9

  • Myosin storage (hyaline body) myopathy: a case report.

    Shingde MV, Spring PJ, Maxwell A, Wills EJ, Harper CG, Dye DE, Laing NG and North KN

    Department of Pathology, University of Sydney, Australia. meena.shingde@email.cs.nsw.gov.au

    Myosin storage myopathy/hyaline body myopathy is a rare congenital myopathy, with less than 30 cases reported in the literature. It is characterised by the presence of subsarcolemmal hyaline bodies in type 1 muscle fibres and predominantly proximal muscle weakness. Recently, a single mutation (Arg1845Trp) in the slow/beta-cardiac myosin heavy chain gene (MYH7) was identified in four unrelated probands from Sweden and Belgium. The clinical severity and age of onset was variable, despite the same disease-causing mutation and similar histological findings. Here, we report the clinical and morphological findings of two brothers of English/Scottish background with the Arg1845Trp mutation in MYH7. This case report adds to the clinical description of this rare disorder and confirms that Arg1845Trp is a common mutation associated with this phenotype, at least in the White European population.

    Neuromuscular disorders : NMD 2006;16;12;882-6

  • Novel slow-skeletal myosin (MYH7) mutation in the original myosin storage myopathy kindred.

    Dye DE, Azzarelli B, Goebel HH and Laing NG

    Molecular Neurogenetics Laboratory, Centre for Medical Research, West Australian Institute for Medical Research, University of Western Australia M519, 'B' Block, Queen Elizabeth II Medical Centre, Nedlands, WA 6009, Australia.

    Myosin storage myopathy (OMIM 608358), a congenital myopathy characterised by subsarcolemmal, hyaline-like accumulations of myosin in Type I muscle fibres, was first described by Cancilla and Colleagues in 1971 [Neurology 1971;21:579-585] in two siblings as 'familial myopathy with probable lysis of myofibrils in type I muscle fibres'. Two mutations in the slow skeletal myosin heavy chain gene (MYH7) have recently been associated with the disease in other families. We have identified a novel heterozygous Leu1793Pro mutation in MYH7 in DNA from paraffin sections of one of the original siblings. This historical molecular analysis confirms the original cases had myosin storage myopathy.

    Neuromuscular disorders : NMD 2006;16;6;357-60

  • Myosin storage myopathy: slow skeletal myosin (MYH7) mutation in two isolated cases.

    Laing NG, Ceuterick-de Groote C, Dye DE, Liyanage K, Duff RM, Dubois B, Robberecht W, Sciot R, Martin JJ and Goebel HH

    Centre for Neuromuscular and Neurologic Disorders, Australian Neuromuscular Research Institute and Centre for Medical Research, University of Western Australia, QEII Medical Centre, Nedlands, Australia. nlaing@cyllene.uwa.edu.au

    Myosin storage myopathy is a congenital myopathy characterized by subsarcolemmal hyaline bodies in type 1 muscle fibers, which are ATPase positive and thus contain myosin. Mutations recently were identified in the type 1 muscle fiber myosin gene (MYH7) in Swedish and Saudi families with myosin storage myopathy. The authors have identified the arginine 1845 tryptophan mutation found in the Swedish families in two isolated Belgian cases, indicating a critical role for myosin residue arginine 1845.

    Neurology 2005;64;3;527-9

  • Mutation of the slow myosin heavy chain rod domain underlies hyaline body myopathy.

    Bohlega S, Abu-Amero SN, Wakil SM, Carroll P, Al-Amr R, Lach B, Al-Sayed Y, Cupler EJ and Meyer BF

    Department of Neurosciences, King Faisal Specialist Hospital and Research Centre, Riyadh, Saudi Arabia.

    Objective: To identify the gene and specific mutation underlying hyaline body myopathy in the family studied.

    Methods: A microsatellite-based whole genome scan was performed. Linkage analysis assumed autosomal dominant inheritance and equal allele frequencies. A candidate gene approach within the linked interval and direct sequencing were used for mutation detection.

    Results: Initial analysis indicated a maximum lod score of 3.01 at D14S1280. High-density mapping surrounding the linked locus was performed. Multipoint analysis showed that the linked region with a maximum lod score of 3.01 extended from D14S742 to D14S608 with a peak non-parametric linkage (NPL) score of 3.75 at D14S608. The myosin heavy chain genes MYH6 and MYH7 map to the region between D14S742 and D14S1280. Sequence analysis of the coding regions of MYH7 revealed an A-->T transversion at nucleotide position 25596 (M57965) resulting in a histidine-to-leucine amino acid change at residue 1904 (H1904L).

    Conclusion: Pathogenicity of the MYH7 H1904L mutation most likely results from disruption of myosin heavy chain assembly or stability of the sarcomeric protein. The MYH7 tail domain mutation results in an inclusion body myopathy with an apparent absence of hypertrophic cardiomyopathy usually associated with mutations of this gene.

    Neurology 2004;62;9;1518-21

© G2C 2014. The Genes to Cognition Programme received funding from The Wellcome Trust and the EU FP7 Framework Programmes:
EUROSPIN (FP7-HEALTH-241498), SynSys (FP7-HEALTH-242167) and GENCODYS (FP7-HEALTH-241995).

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