Evidence map›Paper›PMID 17056255›Full record

ArticleNeuromuscular disorders : NMD2006

AbetaPP-overexpression and proteasome inhibition increase alphaB-crystallin in cultured human muscle: relevance to inclusion-body myositis.

Slawomir Wojcik, W King Engel, Janis McFerrin, Orlando Paciello, Valerie Askanas

Open access · greenAbstract read
In one paragraph

Article in Neuromuscular disorders : NMD, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

14 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Risk factors and disease mechanisms in myositis.Nature reviews. Rheumatology · 2018
    Review
  3. Inclusion body myositis.Neurologic clinics · 2014
    Review
  4. Article
  5. Article
  6. Inclusion body myositis.Current neurology and neuroscience reports · 2013
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Immunization with amyloid-beta attenuates inclusion body myositis-like myopathology and motor impairment in a transgenic mouse model.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009
    Article
  12. Review
  13. Review
  14. Article
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

5 authors at 2 institutions in 1 country.

Slawomir WojcikUSC Neuromuscular Center, Department of Neurology, University of Southern California Keck School of Medicine, Good Samaritan Hospital, Los Angeles, CA 90017-1912, USA.
W King Engel
Janis McFerrin
Orlando Paciello
Valerie Askanas
University of Southern California · USGood Samaritan Hospital · US

Funding

ALZHEIMER-LIKE PATHOLOGY IN INCLUSION BODY MYOPATHYR37AG016768 · NIA · UNIVERSITY OF SOUTHERN CALIFORNIA · PI ASKANAS, VALERIE · 1999 to 2005
$1.9M
NIA NIH HHS AG16768NIA NIH HHS R37 AG016768NIA NIH HHS R37 AG016768-07
6 · The paper itself

Abstract

Amyloid-beta precursor protein (AbetaPP) and its fragment amyloid-beta (Abeta) are increased in s-IBM muscle fibers and appear to play an important role in the pathogenic cascade. alphaB-Crystallin (alphaBC) was shown immunohistochemically to be accumulated in s-IBM muscle fibers, but the stressor(s) influencing alphaBC accumulation was not identified. We now demonstrate, using our experimental IBM model based on genetic overexpression of AbetaPP into cultured normal human muscle fibers, that: (1) AbetaPP overexpression increased alphaBC 3.7-fold (p=0.025); (2) additional inhibition of proteasome with epoxomicin increased alphaBC 7-fold (p=0.002); and (3) alphaBC physically associated with AbetaPP and Abeta oligomers. We also show that in biopsied s-IBM muscle fibers, alphaBC was similarly increased 3-fold (p=0.025) and physically associated with AbetaPP and Abeta oligomers. We propose that increased AbetaPP is a stressor increasing alphaBC expression in s-IBM muscle fibers. Determining the consequences of alphaBC association with Abeta oligomers could have clinical therapeutic relevance.

Indexed as

alpha-Crystallin B ChainAmyloid beta-PeptidesAmyloid beta-Protein PrecursorCells, CulturedGene Expression RegulationHumansInclusion BodiesMuscle, SkeletalMyositis, Inclusion BodyOligopeptidesProteasome Endopeptidase ComplexProteasome InhibitorsStress, PhysiologicalUp-Regulationalpha-Crystallin B ChainAmyloid beta-PeptidesAmyloid beta-Protein PrecursorepoxomicinOligopeptidesProteasome Endopeptidase ComplexProteasome Inhibitors

Identifiers

PMID17056255
PMCPMC1976411
OpenAlexW2029232434

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.