Evidence map›Paper›PMID 19181672›Full record

ArticleBrain : a journal of neurology2009

Clinical, histological and genetic characterization of reducing body myopathy caused by mutations in FHL1.

Joachim Schessl, Ana L Taratuto, Caroline Sewry, Roberta Battini, Steven S Chin, Baijayanta Maiti, Alberto L Dubrovsky, Marcela G Erro, Graciela Espada, Monica Robertella and 13 more

Open access · bronzeAbstract read
In one paragraph

Article in Brain : a journal of neurology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed, 1 pooled it
4.5field-weighted citation impact, top 5% 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

43 citing papers in PubMed, 1 synthesis or guideline pooled it, 100 citations in OpenAlex.

  1. Guideline
  2. Trial
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. The FHL1 myopathy spectrum revisited: a literature review and report of two new patients.Acta myologica : myopathies and cardiomyopathies : official journal of the Mediterranean Society of Myology · 2024
    Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Differential diagnosis of vacuolar myopathies in the NGS era.Brain pathology (Zurich, Switzerland) · 2020
    Article
  15. Article
  16. Article
  17. Article
  18. Myofibrillar myopathy in the genomic context.Journal of applied genetics · 2018
    Review
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

23 authors at 2 institutions in 7 countries.

Joachim SchesslDivision of Neurology, The Children's Hospital of Philadelphia, Pennsylvania Muscle Institute, University of Pennsylvania School of Medicine, Philadelphia, PA, USA.
Ana L Taratuto
Caroline Sewry
Roberta Battini
Steven S Chin
Baijayanta Maiti
Alberto L Dubrovsky
Marcela G Erro
Graciela Espada
Monica Robertella
Maria Saccoliti
Patricia Olmos
Leslie R Bridges
Peter Standring
Ying Hu
Yaqun Zou
Kathryn J Swoboda
Mena Scavina
Hans-Hilmar Goebel
Christina A Mitchell
Kevin M Flanigan
Francesco Muntoni
Carsten G Bönnemann
Children's Hospital of Philadelphia · USAlfred I. duPont Hospital for Children · US

Funding

The Molecular Basis of CMD Types Ullrich and BethlemR01AR051999 · NIAMS · UNIVERSITY OF PENNSYLVANIA · PI BONNEMANN, CARSTEN G · 2005 to 2009
$1.7M
Medical Research Council G0601943NIAMS NIH HHS R01 AR051999NIAMS NIH HHS R01AR051999
6 · The paper itself

Abstract

We recently identified the X-chromosomal four and a half LIM domain gene FHL1 as the causative gene for reducing body myopathy, a disorder characterized by progressive weakness and intracytoplasmic aggregates in muscle that exert reducing activity on menadione nitro-blue-tetrazolium (NBT). The mutations detected in FHL1 affected highly conserved zinc coordinating residues within the second LIM domain and lead to the formation of aggregates when transfected into cells. Our aim was to define the clinical and morphological phenotype of this myopathy and to assess the mutational spectrum of FHL1 mutations in reducing body myopathy in a larger cohort of patients. Patients were ascertained via the detection of reducing bodies in muscle biopsy sections stained with menadione-NBT followed by clinical, histological, ultrastructural and molecular genetic analysis. A total of 11 patients from nine families were included in this study, including seven sporadic patients with early childhood onset disease and four familial cases with later onset. Weakness in all patients was progressive, sometimes rapidly so. Respiratory failure was common and scoliosis and spinal rigidity were significant in some of the patients. Analysis of muscle biopsies confirmed the presence of aggregates of FHL1 positive material in all biopsies. In two patients in whom sequential biopsies were available the aggregate load in muscle sections appeared to increase over time. Ultrastructural analysis revealed that cytoplasmic bodies were regularly seen in conjunction with the reducing bodies. The mutations detected were exclusive to the second LIM domain of FHL1 and were found in both sporadic as well as familial cases of reducing body myopathy. Six of the nine mutations affected the crucial zinc coordinating residue histidine 123. All mutations in this residue were de novo and were associated with a severe clinical course, in particular in one male patient (H123Q). Mutations in the zinc coordinating residue cysteine 153 were associated with a milder phenotype and were seen in the familial cases in which the boys were still more severely affected compared to their mothers. We expect the mild end of the spectrum to significantly expand in the future. On the severe end of the spectrum we define reducing body myopathy as a progressive disease with early, but not necessarily congenital onset, distinguishing this condition from the classic essentially non-progressive congenital myopathies.

Indexed as

Mutation, MissenseAdultChildChild, PreschoolFemaleGenetic Diseases, X-LinkedGenetic Predisposition to DiseaseHumansInfantIntracellular Signaling Peptides and ProteinsLIM Domain ProteinsMaleMicroscopy, ImmunoelectronMuscle ProteinsMuscle, SkeletalMuscular DiseasesFHL1 protein, humanIntracellular Signaling Peptides and ProteinsLIM Domain ProteinsMuscle Proteins

Identifiers

PMID19181672
PMCPMC2724920
OpenAlexW2161471585

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.