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  • 1.
    Darin, Niklas
    et al.
    Department of Pediatrics, Sahlgrenska University Hospital, Göteborg, Sweden / Department of Pediatrics, Queen Silvia Children's Hospital, Göteborg, Sweden.
    Tajsharghi, Homa
    Department of Pathology, Sahlgrenska University Hospital, Göteborg, Sweden.
    Östman-Smith, I.
    Department of Pediatrics, Sahlgrenska University Hospital, Göteborg, Sweden.
    Gilljam, T.
    Department of Pediatrics, Sahlgrenska University Hospital, Göteborg, Sweden.
    Oldfors, Anders
    Department of Pathology, Sahlgrenska University Hospital, Göteborg, Sweden.
    New skeletal myopathy and cardiomyopathy associated with a missense mutation in MYH72007In: Neurology, ISSN 0028-3878, E-ISSN 1526-632X, Vol. 68, no 23, p. 2041-2042Article in journal (Refereed)
  • 2.
    Kimber, Eva
    et al.
    Department of Neuropediatrics, Uppsala University Children's Hospital, Uppsala, Sweden / .
    Tajsharghi, Homa
    Department of Pathology, Sahlgrenska University Hospital, Sweden.
    Kroksmark, A.-K.
    Queen Silvia Children's Hospital, Sahlgrenska Academy, University of Göteborg, Göteborg, Sweden.
    Oldfors, Anders
    Department of Pathology, Sahlgrenska University Hospital, Sweden.
    Tulinius, M.
    Queen Silvia Children's Hospital, Sahlgrenska Academy, University of Göteborg, Göteborg, Sweden.
    A mutation in the fast skeletal muscle troponin I gene causes myopathy and distal arthrogryposis.2006In: Neurology, ISSN 0028-3878, E-ISSN 1526-632X, Vol. 67, no 4, p. 597-601Article in journal (Refereed)
    Abstract [en]

    OBJECTIVE: To describe a three-generation family with distal arthrogryposis associated with myopathy and caused by a mutation in the gene encoding for sarcomeric thin filament protein troponin I, TNNI2.

    METHODS: The authors performed clinical investigations and reviewed medical records. Muscle biopsy specimens were obtained for morphologic analysis. Genomic DNA was extracted from blood and analyzed for mutations in TNNI2.

    RESULTS: The five affected individuals had predominantly distal congenital joint contractures, mild facial involvement (mild micrognathia, narrow palpebral fissures), and no detectable muscle weakness. The four affected adults had slightly increased levels of creatine kinase in blood, and muscle biopsy specimens showed findings of myopathy with changes restricted to type 2 fibers. These included variability of muscle fiber size, internalized nuclei, and increased interstitial connective tissue. Analysis of TNNI2 encoding the troponin I isoform expressed in type 2 muscle fibers disclosed a heterozygous three-base in-frame deletion, 2,918-2,920del, skipping the highly conserved lysine at position 176. The mutation was present in all 5 affected individuals but was not identified in any of the 11 unaffected family members.

    CONCLUSION: Distal arthrogryposis type 1 is genetically heterogeneous, and myopathy due to sarcomeric protein dysfunction may be one underlying cause of the disease.

  • 3.
    Ohlsson, M.
    et al.
    Department of Pathology, Sahlgrenska University Hospital, Göteborg, Sweden.
    Quijano-Roy, S.
    AP-HP, Service de Pédiatrie, Centre National de Référence des Maladies Neuromusculaires GNMH, Garches, France.
    Darin, N.
    Department of Pediatrics, Sahlgrenska University Hospital, Göteborg, Sweden.
    Brochier, G.
    Institut de Myologie, Groupe Hospitalier Pitie-Salpêtrière, Paris, France.
    Lacène, E.
    Institut de Myologie, Groupe Hospitalier Pitie-Salpêtrière, Paris, France.
    Avila-Smirnow, D.
    AP-HP, Service de Pédiatrie, Centre National de Référence des Maladies Neuromusculaires GNMH, Garches, France.
    Fardeau, M.
    Institut de Myologie, Groupe Hospitalier Pitie-Salpêtrière, Paris, France.
    Oldfors, Anders
    Department of Pathology, Sahlgrenska University Hospital, Göteborg, Sweden.
    Tajsharghi, Homa
    Department of Pathology, Sahlgrenska University Hospital, Göteborg, Sweden.
    New morphologic and genetic findings in cap disease associated with beta-tropomyosin (TPM2) mutations2008In: Neurology, ISSN 0028-3878, E-ISSN 1526-632X, Vol. 71, no 23, p. 1896-1901Article in journal (Refereed)
    Abstract [en]

    OBJECTIVE: Mutations in the beta-tropomyosin gene (TPM2) are a rare cause of congenital myopathies with features of nemaline myopathy and cap disease and may also cause distal arthrogryposis syndromes without major muscle pathology. We describe the muscle biopsy findings in three patients with cap disease and novel heterozygous mutations in TPM2.

    METHODS: Three unrelated patients with congenital myopathy were investigated by muscle biopsy and genetic analysis.

    RESULTS: All three patients had early-onset muscle weakness of variable severity and distribution. Muscle biopsy demonstrated in all three patients near uniformity of type 1 fibers and an unusual irregular and coarse-meshed intermyofibrillar network. By electron microscopy, the myofibrils were broad and partly split, and the Z lines appeared jagged. In one of the patients caps structures were identified only by electron microscopy, and in one patient they were identified only in a second biopsy at adulthood. Three novel, de novo, heterozygous mutations in TPM2 were identified: a three-base pair deletion in-frame (p.Lys49del), a three-base pair duplication in-frame (p.Gly52dup), and a missense mutation (p.Asn202Lys).

    CONCLUSIONS: Mutations in TPM2 seem to be a frequent cause of cap disease. Because cap structures may be sparse, other prominent features, such as a coarse-meshed intermyofibrillar network and jagged Z lines, may be clues to correct diagnosis and also indicate that the pathogenesis involves defective assembly of myofilaments.

  • 4.
    Oldfors, Anders
    et al.
    Göteborg, Sweden.
    Tajsharghi, Homa
    Göteborg, Sweden.
    Thornell, L. E.
    Mutation of the slow myosin heavy chain rod domain underlies hyaline body myopathy2005In: Neurology, ISSN 0028-3878, E-ISSN 1526-632X, Vol. 64, no 3, p. 580-581Article in journal (Refereed)
  • 5.
    Tajsharghi, Homa
    et al.
    Department of Pathology, Sahlgrenska University Hospital, Göteborg, Sweden.
    Kimber, Eva
    Department of Neuropediatrics, Uppsala University Children's Hospital, Uppsala, Sweden.
    Holmgren, D.
    Division of Pediatric Cardiology, Sahlgrenska University Hospital, Göteborg, Sweden.
    Tulinius, M.
    Department of Pediatrics, Sahlgrenska University Hospital, Göteborg, Sweden.
    Oldfors, Anders
    Department of Pathology, Sahlgrenska University Hospital, Göteborg, Sweden.
    Distal arthrogryposis and muscle weakness associated with a beta-tropomyosin mutation2007In: Neurology, ISSN 0028-3878, E-ISSN 1526-632X, Vol. 68, no 10, p. 772-775Article in journal (Refereed)
    Abstract [en]

    Tropomyosin (TM), a sarcomeric thin-filament protein, plays an essential part in muscle contraction by regulating actin-myosin interaction. We describe two patients, a woman and her daughter, with muscle weakness and distal arthrogryposis (DA) type 2B, caused by a heterozygous missense mutation, R133W, in TPM2, the gene encoding beta-TM. Our results demonstrate the involvement of muscle dysfunction in the pathogenesis of DA and the fact that DA2B may be caused by mutations in TPM2.

  • 6.
    Tajsharghi, Homa
    et al.
    Department of Pathology, Sahlgrenska University Hospital, Göteborg, Sweden.
    Oldfors, Anders
    Department of Pathology, Sahlgrenska University Hospital, Göteborg, Sweden.
    Macleod, Dominic P.
    Department of Respiratory Medicine, Royal London Hospital, United Kingdom.
    Swash, Michael
    Department of Neurology, Royal London Hospital, United Kingdom.
    Homozygous mutation in MYH7 in myosin storage myopathy and cardiomyopathy2007In: Neurology, ISSN 0028-3878, E-ISSN 1526-632X, Vol. 68, no 12, p. 962-Article in journal (Refereed)
  • 7.
    Tajsharghi, Homa
    et al.
    Department of Pathology, Sahlgrenska University Hospital, Göteborg, Sweden.
    Thornell, L.-E.
    Department of Anatomy, Umeå University, Umeå, Sweden.
    Darin, Niklas
    Department of Pediatrics, Sahlgrenska University Hospital, Gothenburg, Sweden.
    Martinsson, T.
    Department of Clinical Genetics, Sahlgrenska University Hospital, Gothenburg, Sweden.
    Kyllerman, M.
    Department of Pediatrics, Sahlgrenska University Hospital, Gothenburg, Sweden.
    Wahlström, J.
    Department of Clinical Genetics, Sahlgrenska University Hospital, Gothenburg, Sweden.
    Oldfors, Anders
    Department of Pathology, Sahlgrenska University Hospital, Göteborg, Sweden.
    Myosin heavy chain IIa gene mutation E706K is pathogenic and its expression increases with age2002In: Neurology, ISSN 0028-3878, E-ISSN 1526-632X, Vol. 58, no 5, p. 780-786Article in journal (Refereed)
    Abstract [en]

    BACKGROUND: The authors recently described a new autosomal dominant myopathy (OMIM 605637 inclusion body myopathy 3) associated with a missense mutation in the myosin heavy chain (MyHC) IIa gene (MyHC IIa, Human Gene Map [HGM] locus MYH2). Young patients showed minor changes in their muscle biopsies, although dystrophic alterations and rimmed vacuoles with 15- to 20-nm tubulofilaments identical to those in sporadic inclusion body myositis (s-IBM) were observed in some of the adult (especially older) patients. The current study was undertaken to investigate the relation between expression of the mutant MyHC IIa and pathologic changes in muscle.

    METHODS: The expression of MyHC IIa in nine muscle specimens from six individuals carrying the mutation was analyzed by immunohistochemistry, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and a new reverse transcriptase--PCR method to measure the relative abundance of the various MyHC transcripts.

    RESULTS: Young patients with muscle weakness and minor pathologic changes in muscle expressed MyHC IIa at undetectable levels. MyHC IIa was expressed at high levels in adults with a progressive clinical course and dystrophic muscle changes. In these cases, a large number of muscle fibers were hybrids with expression of more than one MyHC isoform. Both MyHC IIa alleles were equally expressed. The relative level of MyHC IIa transcripts exceeded that of the corresponding protein, indicating an increased turnover of mutated protein. MyHC IIa expression was a consistent finding in muscle fibers with rimmed vacuoles.

    CONCLUSIONS: The clear correlation between pathologic changes and expression of MyHC IIa indicates that defects in MyHC may lead not only to muscle weakness but also to muscle degeneration. The consistent expression of MyHC IIa in muscle fibers with rimmed vacuoles indicates that the breakdown of sarcomeric proteins is a key element in the pathogenesis of rimmed vacuoles of s-IBM type.

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