his.sePublications
Change search
Refine search result
1 - 4 of 4
CiteExportLink to result list
Permanent link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Rows per page
  • 5
  • 10
  • 20
  • 50
  • 100
  • 250
Sort
  • Standard (Relevance)
  • Author A-Ö
  • Author Ö-A
  • Title A-Ö
  • Title Ö-A
  • Publication type A-Ö
  • Publication type Ö-A
  • Issued (Oldest first)
  • Issued (Newest first)
  • Created (Oldest first)
  • Created (Newest first)
  • Last updated (Oldest first)
  • Last updated (Newest first)
  • Disputation date (earliest first)
  • Disputation date (latest first)
  • Standard (Relevance)
  • Author A-Ö
  • Author Ö-A
  • Title A-Ö
  • Title Ö-A
  • Publication type A-Ö
  • Publication type Ö-A
  • Issued (Oldest first)
  • Issued (Newest first)
  • Created (Oldest first)
  • Created (Newest first)
  • Last updated (Oldest first)
  • Last updated (Newest first)
  • Disputation date (earliest first)
  • Disputation date (latest first)
Select
The maximal number of hits you can export is 250. When you want to export more records please use the Create feeds function.
  • 1.
    Kariminejad, Ariana
    et al.
    Kariminejad-Najmabadi Pathology and Genetics Center, Tehran, Iran.
    Dahl-Halvarsson, Martin
    Department of Pathology, University of Gothenburg, Sahlgrenska University Hospital, Sweden.
    Ravenscroft, Gianina
    Centre for Medical Research, The University of Western Australia and the Harry Perkins Institute for Medical Research, Nedlands, Western Australia, Australia.
    Afroozan, Fariba
    Kariminejad-Najmabadi Pathology and Genetics Center, Tehran, Iran.
    Keshavarz, Elham
    Department of Radiology, Mahdieh Hospital, Shahid Beheshti University of Medical Science, Tehran, Iran.
    Goullée, Hayley
    Centre for Medical Research, The University of Western Australia and the Harry Perkins Institute for Medical Research, Nedlands, Western Australia, Australia.
    Davis, Mark R.
    Department of Diagnostic Genomics, Pathwest, QEII Medical Centre, Nedlands, Western Australia, Australia.
    Faraji Zonooz, Mehrshid
    Kariminejad-Najmabadi Pathology and Genetics Center, Tehran, Iran.
    Najmabadi, Hossein
    Kariminejad-Najmabadi Pathology and Genetics Center, Tehran, Iran.
    Laing, Nigel G.
    Centre for Medical Research, The University of Western Australia and the Harry Perkins Institute for Medical Research, Nedlands, Western Australia, Australia.
    Tajsharghi, Homa
    University of Skövde, School of Health and Education. University of Skövde, Health and Education. Centre for Medical Research, The University of Western Australia and the Harry Perkins Institute for Medical Research, Nedlands, Western Australia, Australia.
    TOR1A variants cause a severe arthrogryposis with developmental delay, strabismus and tremor2017In: Brain, ISSN 0006-8950, E-ISSN 1460-2156, Vol. 140, no 11, p. 2851-2859Article in journal (Refereed)
    Abstract [en]

    Autosomal dominant torsion dystonia-1 is a disease with incomplete penetrance most often caused by an in-frame GAG deletion (p.Glu303del) in the endoplasmic reticulum luminal protein torsinA encoded by TOR1A.

    We report an association of the homozygous dominant disease-causing TOR1A p.Glu303del mutation, and a novel homozygous missense variant (p.Gly318Ser) with a severe arthrogryposis phenotype with developmental delay, strabismus and tremor in three unrelated Iranian families. All parents who were carriers of the TOR1A variant showed no evidence of neurological symptoms or signs, indicating decreased penetrance similar to families with autosomal dominant torsion dystonia-1. The results from cell assays demonstrate that the p.Gly318Ser substitution causes a redistribution of torsinA from the endoplasmic reticulum to the nuclear envelope, similar to the hallmark of the p.Glu303del mutation.

    Our study highlights that TOR1A mutations should be considered in patients with severe arthrogryposis and further expands the phenotypic spectrum associated with TOR1A mutations. 

  • 2.
    Lossos, Alexander
    et al.
    Department of Neurology, Hebrew University-Hadassah Medical Centre, Jerusalem, Israel.
    Oldfors, Anders
    Department of Pathology, University of Gothenburg, Sahlgrenska Hospital, Gothenburg, Sweden.
    Fellig, Yakov
    Department of Pathology, Hebrew University-Hadassah Medical Centre, Jerusalem, Israel.
    Meiner, Vardiella
    Department of Genetics, Hebrew University-Hadassah Medical Centre, Jerusalem, Israel.
    Argov, Zohar
    Department of Neurology, Hebrew University-Hadassah Medical Centre, Jerusalem, Israel.
    Tajsharghi, Homa
    Department of Pathology, University of Gothenburg, Sahlgrenska Hospital, Gothenburg, Sweden.
    MYH2 mutation in recessive myopathy with external ophthalmoplegia linked to chromosome 17p13.1-p122013In: Brain, ISSN 0006-8950, E-ISSN 1460-2156, Vol. 136, no 7, article id e238Article in journal (Refereed)
  • 3.
    Ohlsson, Monica
    et al.
    Department of Pathology, University of Gothenburg, Sahlgrenska University Hospital, Gothenburg, Sweden.
    Hedberg, Carola
    Department of Pathology, University of Gothenburg, Sahlgrenska University Hospital, Gothenburg, Sweden.
    Brådvik, Björn
    Department of Clinical Sciences, Division of Neurology, Lund University, Lund, Sweden.
    Lindberg, Christopher
    Department of Neurology, University of Gothenburg, Sahlgrenska University Hospital, Gothenburg, Sweden.
    Tajsharghi, Homa
    Department of Pathology, University of Gothenburg, Sahlgrenska University Hospital, Gothenburg, Sweden.
    Danielsson, Olof
    Division of Neurology, Department of Clinical and Experimental Medicine, University Hospital Linköping, Linköping, Sweden.
    Melberg, Atle
    Department of Neuroscience, Neurology, Uppsala University, Uppsala University Hospital, Uppsala, Sweden.
    Udd, Bjarne
    Neuromuscular Centre, Tampere University and Hospital, Tampere, Finland / Department of Neurology, Vasa Central Hospital, Vasa, Finland / Folkhälsan Genetic Institute, Department of Medical Genetics, Helsinki University, Helsinki, Finland.
    Martinsson, Tommy
    Department of Clinical Genetics, University of Gothenburg, Sahlgrenska University Hospital, Gothenburg, Sweden.
    Oldfors, Anders
    Department of Pathology, University of Gothenburg, Sahlgrenska University Hospital, Gothenburg, Sweden.
    Hereditary myopathy with early respiratory failure associated with a mutation in A-band titin2012In: Brain, ISSN 0006-8950, E-ISSN 1460-2156, Vol. 135, no 6, p. 1682-1694Article in journal (Refereed)
    Abstract [en]

    Hereditary myopathy with early respiratory failure and extensive myofibrillar lesions has been described in sporadic and familial cases and linked to various chromosomal regions. The mutated gene is unknown in most cases. We studied eight individuals, from three apparently unrelated families, with clinical and pathological features of hereditary myopathy with early respiratory failure. The investigations included clinical examination, muscle histopathology and genetic analysis by whole exome sequencing and single nucleotide polymorphism arrays. All patients had adult onset muscle weakness in the pelvic girdle, neck flexors, respiratory and trunk muscles, and the majority had prominent calf hypertrophy. Examination of pulmonary function showed decreased vital capacity. No signs of cardiac muscle involvement were found. Muscle histopathological features included marked muscle fibre size variation, fibre splitting, numerous internal nuclei and fatty infiltration. Frequent groups of fibres showed eosinophilic inclusions and deposits. At the ultrastructural level, there were extensive myofibrillar lesions with marked Z-disc alterations. Whole exome sequencing in four individuals from one family revealed a missense mutation, g.274375T>C; p.Cys30071Arg, in the titin gene (TTN). The mutation, which changes a highly conserved residue in the myosin binding A-band titin, was demonstrated to segregate with the disease in all three families. High density single nucleotide polymorphism arrays covering the entire genome demonstrated sharing of a 6.99 Mb haplotype, located in chromosome region 2q31 including TTN, indicating common ancestry. Our results demonstrate a novel and the first disease-causing mutation in A-band titin associated with hereditary myopathy with early respiratory failure. The typical histopathological features with prominent myofibrillar lesions and inclusions in muscle and respiratory failure early in the clinical course should be incentives for analysis of TTN mutations.

  • 4.
    Tajsharghi, Homa
    et al.
    Department of Pathology, Institute of Biomedicine, University of Gothenburg, Sahlgrenska Hospital, Gothenburg, Sweden.
    Hilton-Jones, David
    Department of Neurology, West Wing, John Racliffe Hospital, Oxford, UK.
    Raheem, Olayinka
    Neuromuscular Centre, Tampere University and Hospital, Tampere, Finland.
    Saukkonen, Anna Maija
    Department of Neurology, Central Hospital of Northern Karelia, Joensuu, Finland.
    Oldfors, Anders
    Department of Pathology, Institute of Biomedicine, University of Gothenburg, Sahlgrenska Hospital, Gothenburg, Sweden.
    Udd, Bjarne
    Neuromuscular Centre, Tampere University and Hospital, Tampere, Finland / Department of Neurology, Vasa Central Hospital, Vasa, Finland / Folkhälsan Genetic Institute, Department of Medical Genetics, Helsinki University, Helsinki, Finland.
    Human disease caused by loss of fast IIa myosin heavy chain due to recessive MYH2 mutations2010In: Brain, ISSN 0006-8950, E-ISSN 1460-2156, Vol. 133, no 5, p. 1451-1459Article in journal (Refereed)
    Abstract [en]

    Striated muscle myosin heavy chain is a molecular motor protein that converts chemical energy into mechanical force. It is a major determinant of the physiological properties of each of the three muscle fibre types that make up the skeletal muscles. Heterozygous dominant missense mutations in myosin heavy chain genes cause various types of cardiomyopathy and skeletal myopathy, but the effects of myosin heavy chain null mutations in humans have not previously been reported. We have identified the first patients lacking fast type 2A muscle fibres, caused by total absence of fast myosin heavy chain IIa protein due to truncating mutations of the corresponding gene MYH2. Five adult patients, two males and three females, from three unrelated families in UK and Finland were clinically assessed and muscle biopsy was performed in one patient from each family. MYH2 was sequenced and the expression of the corresponding transcripts and protein was analysed in muscle tissue. The patients had early-onset symptoms characterized by mild generalized muscle weakness, extraocular muscle involvement and relatively favourable prognosis. Muscle biopsy revealed myopathic changes including variability of fibre size, internalized nuclei, and increased interstitial connective and adipose tissue. No muscle fibres expressing type IIa myosin heavy chain were identified and the MYH2 transcripts were markedly reduced. All patients were compound heterozygous for truncating mutations in MYH2. The parents were unaffected, consistent with recessive mutations. Our findings show that null mutations in the fast myosin heavy chain IIa gene cause early onset myopathy and demonstrate that this isoform is necessary for normal muscle development and function. The relatively mild phenotype is interesting in relation to the more severe phenotypes generally seen in relation to recessive null mutations in sarcomeric proteins.

1 - 4 of 4
CiteExportLink to result list
Permanent link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf