The Congenital and Limb-Girdle Muscular Dystrophies

Kirschner, Janbernd; Bönnemann, Carsten G.

doi:10.1001/archneur.61.2.189

Cited by 58 publications

(3 citation statements)

References 109 publications

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“…Dystroglycanopathies cause neocortical dysplasia and variable pontocerebellar hypoplasia and microcephaly or hydrocephalus (Table 3) [64,65]. An X-linked brain malformation phenotype with a moderately simplified gyral pattern and mild cortical dysplasia, only visible on autopsy is due to mutations in the calcium/calmodulin dependent serine protein kinase gene ( CASK ).…”

Section: Reviewmentioning

confidence: 99%

Classification, diagnosis and potential mechanisms in Pontocerebellar Hypoplasia

Namavar

Barth

Poll-Thé

et al. 2011

Orphanet J Rare Dis

161

127

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Pontocerebellar Hypoplasia (PCH) is group of very rare, inherited progressive neurodegenerative disorders with prenatal onset. Up to now seven different subtypes have been reported (PCH1-7). The incidence of each subtype is unknown. All subtypes share common characteristics, including hypoplasia/atrophy of cerebellum and pons, progressive microcephaly, and variable cerebral involvement. Patients have severe cognitive and motor handicaps and seizures are often reported. Treatment is only symptomatic and prognosis is poor, as most patients die during infancy or childhood. The genetic basis of different subtypes has been elucidated, which makes prenatal testing possible in families with mutations. Mutations in three tRNA splicing endonuclease subunit genes were found to be responsible for PCH2, PCH4 and PCH5. Mutations in the nuclear encoded mitochondrial arginyl- tRNA synthetase gene underlie PCH6. The tRNA splicing endonuclease, the mitochondrial arginyl- tRNA synthetase and the vaccinia related kinase1 are mutated in the minority of PCH1 cases. These genes are involved in essential processes in protein synthesis in general and tRNA processing in particular. In this review we describe the neuroradiological, neuropathological, clinical and genetic features of the different PCH subtypes and we report on in vitro and in vivo studies on the tRNA splicing endonuclease and mitochondrial arginyl-tRNA synthetase and discuss their relation to pontocerebellar hypoplasia.

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Section: Reviewmentioning

confidence: 99%

Classification, diagnosis and potential mechanisms in Pontocerebellar Hypoplasia

Namavar

Barth

Poll-Thé

et al. 2011

Orphanet J Rare Dis

161

127

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“…The M-line anchors parts of the contractile sarcomere (myosin and titn) and contains proteins such as myomesin and obscurin. Titin is the most extensively studied of the M-line proteins and mutations in titin’s C-terminus lead to limb girdle muscular dystrophies, tibial and Salih congenital muscular dystrophies [9,24,25]. Although a mutation in the dimerization domain of myomesin 1 leads to hypertrophic cardiomyopathy in humans, no other mutations have been described in M-line proteins, including myomesin 2 and 3 [26].…”

Section: Introductionmentioning

confidence: 99%

Myomesin is part of an integrity pathway that responds to sarcomere damage and disease

et al. 2019

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The structure and function of the sarcomere of striated muscle is well studied but the steps of sarcomere assembly and maintenance remain under-characterized. With the aid of chaperones and factors of the protein quality control system, muscle proteins can be folded and assembled into the contractile apparatus of the sarcomere. When sarcomere assembly is incomplete or the sarcomere becomes damaged, suites of chaperones and maintenance factors respond to repair the sarcomere. Here we show evidence of the importance of the M-line proteins, specifically myomesin, in the monitoring of sarcomere assembly and integrity in previously characterized zebrafish muscle mutants. We show that myomesin is one of the last proteins to be incorporated into the assembling sarcomere, and that in skeletal muscle, its incorporation requires connections with both titin and myosin. In diseased zebrafish sarcomeres, myomesin1a shows an early increase of gene expression, hours before chaperones respond to damaged muscle. We found that myomesin expression is also more specific to sarcomere damage than muscle creatine kinase, and our results and others support the use of myomesin assays as an early, specific, method of detecting muscle damage.

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“…M UTATIONS ON THE GENES that encode sarcolemmal proteins (sarcoglycans, dysferlin, and caveolin-3) may cause diverse muscular disorders (Cohn and Campbell, 2000;Kirschner and Bonnemann, 2004). Mutations on dysferlin (DYSF) are related to at least three known different pathologic phenotypes of muscular dystrophy called dysferlinopathies (Liu et al, 1998;Nguyen et al, 2005) that includes pathologic phenotypes as the autosomal type B recessive limb-girdle muscular dystrophy (LGMD2B), which affects proximal limbs; Miyoshi myopathy (MM), which is characterized by affections on distal lower limb muscles (Liu et al, 1998;Bushby, 1999;Illa et al, 2001), and the distal anterior compartment myopathy (DMAT).…”

Section: Introductionmentioning

confidence: 99%

Dysferlin Homozygous Mutation G1418D Causes Limb-Girdle Type 2B in a Mexican Family

et al. 2007

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Dysferlin protein (DYSF) is a ferlin family member found in sarcolemma and is involved in membrane repair, muscle differentiation, membrane fusion, etc. The deficiency of DYSF due to mutations is associated with different pathologic phenotypes including the autosomal recessive limb-girdle type 2B phenotype (LGMD2B), a distal anterior compartment myopathy (DMAT), and the Miyoshi myopathy (MM). In this study, we determined a missense mutation c.4253G>A on the DYSF gene in a Mexican family from an endogamic population. This mutation was assumed to be the cause of dystrophy because only homozygous individuals of the family manifest a clinical phenotype. Structural implications caused by G/D substitution at amino acid position 1418 are discussed in terms of potential importance of the dysferlin neighboring sequence.

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The Congenital and Limb-Girdle Muscular Dystrophies

Cited by 58 publications

References 109 publications

Classification, diagnosis and potential mechanisms in Pontocerebellar Hypoplasia

Classification, diagnosis and potential mechanisms in Pontocerebellar Hypoplasia

Myomesin is part of an integrity pathway that responds to sarcomere damage and disease

Dysferlin Homozygous Mutation G1418D Causes Limb-Girdle Type 2B in a Mexican Family

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