Evidence map›Paper›PMID 32779703›Full record

ArticleBrain : a journal of neurology2020

Loss of supervillin causes myopathy with myofibrillar disorganization and autophagic vacuoles.

Carola Hedberg-Oldfors, Robert Meyer, Kay Nolte, Yassir Abdul Rahim, Christopher Lindberg, Kristjan Karason, Inger Johanne Thuestad, Kittichate Visuttijai, Mats Geijer, Matthias Begemann and 14 more

Erratum issuedOpen access · hybridAbstract readCase Reports
In one paragraph

Article in Brain : a journal of neurology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 21 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed, 2 pooled it
2.2field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed, 2 syntheses or guidelines pooled it, 30 citations in OpenAlex.

  1. Pooled it
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  13. Protein Aggregates and Aggrephagy in Myopathies.International journal of molecular sciences · 2023
    Review
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  16. Morphological and Molecular Responses ofInternational journal of molecular sciences · 2022
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

24 authors at 7 institutions in 4 countries.

Carola Hedberg-OldforsDepartment of Pathology and Genetics, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
Robert MeyerInstitute of Human Genetics, Medical Faculty, RWTH Aachen University, Aachen, Germany.
Kay NolteInstitute of Neuropathology, Medical Faculty, RWTH Aachen University, Aachen, Germany.
Yassir Abdul RahimDepartment of Pathology and Genetics, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
Christopher LindbergDepartment of Neurology, Neuromuscular Centre, Sahlgrenska University Hospital, Gothenburg, Sweden.
Kristjan KarasonDepartment of Cardiology and Transplant Institute, Sahlgrenska University Hospital, Gothenburg, Sweden.
Inger Johanne ThuestadDepartment of Pediatrics, Skane University Hospital, Malmo, Sweden.
Kittichate VisuttijaiDepartment of Pathology and Genetics, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
Mats GeijerDepartment of Radiology, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
Matthias BegemannInstitute of Human Genetics, Medical Faculty, RWTH Aachen University, Aachen, Germany.
Florian KraftInstitute of Human Genetics, Medical Faculty, RWTH Aachen University, Aachen, Germany.
Eva LausbergInstitute of Human Genetics, Medical Faculty, RWTH Aachen University, Aachen, Germany.
Lea HitpassDepartment of Diagnostic and Interventional Radiology, Medical Faculty, RWTH Aachen University, Aachen, Germany.
Rebekka GötzlDepartment of Plastic Surgery, Hand and Burn Surgery, Medical Faculty, RWTH Aachen University, Aachen, Germany.
Elizabeth J LunaDivision of Cell Biology and Imaging, Department of Radiology, University of Massachusetts Medical School, Worcester, USA.
Hanns LochmüllerChildren's Hospital of Eastern Ontario Research Institute, Division of Neurology, Department of Medicine, The Ottawa Hospital, Ottawa, Canada.
Steffen KoschmiederDepartment of Hematology, Oncology, Hemostaseology and Stem Cell Transplantation, Medical Faculty, RWTH Aachen University, Aachen, Germany.
Michael GramlichDepartment of Invasive Electrophysiology, Medical Faculty, RWTH Aachen University, Aachen, Germany.
Burkhard GessDepartment of Neurology, Medical Faculty, RWTH Aachen University, Aachen, Germany.
Miriam ElbrachtInstitute of Human Genetics, Medical Faculty, RWTH Aachen University, Aachen, Germany.
Joachim WeisInstitute of Neuropathology, Medical Faculty, RWTH Aachen University, Aachen, Germany.
Ingo KurthInstitute of Human Genetics, Medical Faculty, RWTH Aachen University, Aachen, Germany.
Anders OldforsDepartment of Pathology and Genetics, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
Cordula KnoppInstitute of Human Genetics, Medical Faculty, RWTH Aachen University, Aachen, Germany.
RWTH Aachen University · DEUniversity of Gothenburg · SESahlgrenska University Hospital · SELund University · SESkåne University Hospital · SEUniversity of Massachusetts Chan Medical School · USUniversity of Ottawa · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The muscle specific isoform of the supervillin protein (SV2), encoded by the SVIL gene, is a large sarcolemmal myosin II- and F-actin-binding protein. Supervillin (SV2) binds and co-localizes with costameric dystrophin and binds nebulin, potentially attaching the sarcolemma to myofibrillar Z-lines. Despite its important role in muscle cell physiology suggested by various in vitro studies, there are so far no reports of any human disease caused by SVIL mutations. We here report four patients from two unrelated, consanguineous families with a childhood/adolescence onset of a myopathy associated with homozygous loss-of-function mutations in SVIL. Wide neck, anteverted shoulders and prominent trapezius muscles together with variable contractures were characteristic features. All patients showed increased levels of serum creatine kinase but no or minor muscle weakness. Mild cardiac manifestations were observed. Muscle biopsies showed complete loss of large supervillin isoforms in muscle fibres by western blot and immunohistochemical analyses. Light and electron microscopic investigations revealed a structural myopathy with numerous lobulated muscle fibres and considerable myofibrillar alterations with a coarse and irregular intermyofibrillar network. Autophagic vacuoles, as well as frequent and extensive deposits of lipoproteins, including immature lipofuscin, were observed. Several sarcolemma-associated proteins, including dystrophin and sarcoglycans, were partially mis-localized. The results demonstrate the importance of the supervillin (SV2) protein for the structural integrity of muscle fibres in humans and show that recessive loss-of-function mutations in SVIL cause a distinctive and novel myopathy.

Indexed as

AdolescentAge of OnsetAutophagyChildFemaleHumansLoss of Function MutationMaleMembrane ProteinsMicrofilament ProteinsMuscle, SkeletalMuscular DiseasesPedigreeVacuolesMembrane ProteinsMicrofilament ProteinsSVIL protein, humancardiac diseasecostameric proteinmyopathysupervillinSVIL

Identifiers

PMID32779703
PMCPMC7447519
OpenAlexW3048723714

What OpenQuestion holds

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LicenceCC BY-NC
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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.