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Serum CK levels are markedly elevated In contrast to the dystrophinopathies, there are no signi cant intellectual impairments or cardiac abnormalities in the sarcoglycanopathies
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Histopathology
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Muscle biopsies demonstrate normal dystrophin; however, each of the sarcoglycans are absent or diminished on the sarcolemma, regardless of the primary sarcoglycan mutation
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LGMD 2H Clinical Features
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This genetically distinct LGMD was initially reported in families of Manitoba Hutterite origin29,132 Age of onset of weakness ranges from 8 to 27 years The myopathy is slowly progressive, and most affected individuals are still ambulatory, without assistance in the fourth decade of life
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LGMDs 2C, 2D, 2E, and 2F are caused by mutations in the -, -, -, and -sarcoglycan genes, respectively6,102,116, 117,119 125 The clinical phenotypes appear to correlate with the expression of the sarcoglycans The proteins of the sarcoglycan complex appear to function as a unit Mutations involving any of the sarcoglycans result in destabilization of the entire complex and reduced expression of the other proteins As apparent with the dystrophinopathies, the clinical severity of the sarcoglycanopathies may correlate with the type of mutation (ie, whether the reading frame is preserved) and subsequent level of functional protein expression
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Serum CKs are elevated vefold to 50-fold There may be nonspeci c EKG changes
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Histopathology CONGENITAL FIBROSIS OF THE EXTRAOCULAR MUSCLES
Mutations in the sarcospan gene located on chromosome 12p112 are associated with congenital brosis of the extraocular muscles, a rare form of muscular dystrophy126 Muscle biopsies demonstrate typical dystrophic features In addition, many bers (mostly type 2) contain small vacuoles that immunostain for sarcoplasmic reticulumassociated ATPase These vacuoles abut T-tubules and appear to be membrane bound and appeared on EM
Molecular Genetics and Pathogenesis LGMD 2G Clinical Features
This myopathy is associated with prominent early weakness of the quadriceps and anterior tibial muscle groups and has mean age of onset of muscle weakness of 125 years127,128 Cases resembling Miyoshi myopathy (LGMD 2B) with calf weakness have also been described129 LGMD 2H and sarcotubular myopathy (discussed in 25 with the Congenital Myopathies) are now known to be allelic disorders caused by mutations in the gene that encodes for E3-ubiquitine ligase (also known as TRIM 32) located on chromosome 9q31 q33 was recently reported29 TRIM 32 may function by ubiquinating proteins that need degradation by proteosomes The mechanism by which this leads to muscle destruction is unclear, but one might speculate on the possible toxic accumulation of aged or otherwise abnormal proteins not cleared by proteasomes
Laboratory Features
Serum CKs are elevated threefold to 17-fold
SECTION II
SPECIFIC DISORDERS
LGMD 2I Clinical Features
LGMD 2I was initially described in a large consanguineous Tunisian family with 13 affected members133 However, it subsequently has been demonstrated worldwide and is the most common form of LGMD in England, the Netherlands, and northern Europe The onset can range from infancy (MDC type 1C) to the fourth decade of life30,31 The pattern of weakness and course is variable Some individuals have more hip-girdle involvement, while others are weaker in the proximal arms and neck exors Calves are often hypertrophic Importantly, approximately one-half of patients develop a dilated cardiomyopathy and ventilatory muscle weakness134 136
Histopathology
Nonspeci c dystrophic features are evident on muscle biopsy Of note, immunohistochemistry demonstrates normal dystrophin and sarcoglycan staining However, -dystroglycan and occasional merosin are reduced or absent on immunostaining (Fig 24 12)
Molecular Genetics and Pathogenesis
The LGMD 2I is caused by mutations in the gene that encodes for FKRP located on chromosome 19q133 Mutations in this gene are also responsible for MDC type 1C; FKRP is a glycosyltransferase and its de ciency is associated with abnormal glycosylation of alphadystroglycan, which apparently disrupts the dystrophin glycoprotein complex Abnormalities in glycosylation of -dystroglycan is recurring theme in the MDCs, as this is also causative mechanism in Fukuyama disease, MEB, WWS, and LARGE-related CMD (MDC 1D) There is a correlation between a reduction in alpha-dystroglycan, the mutation, and the clinical phenotype in MDC 1C and LGMD 2I32
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