Evidence map›Paper›PMID 18787103›Full record

ArticleThe American journal of pathology2008

Accumulation of citrullinated proteins by up-regulated peptidylarginine deiminase 2 in brains of scrapie-infected mice: a possible role in pathogenesis.

Byungki Jang, Eunah Kim, Jin-Kyu Choi, Jae-Kwang Jin, Jae-Il Kim, Akihito Ishigami, Naoki Maruyama, Richard I Carp, Yong-Sun Kim, Eun-Kyoung Choi

Open access · bronzeAbstract read
In one paragraph

Article in The American journal of pathology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

30 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
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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

10 authors at 4 institutions in 4 countries.

Byungki JangIlsong Institute of Life Science, Hallym University, Anyang, Republic of Korea.
Eunah Kim
Jin-Kyu Choi
Jae-Kwang Jin
Jae-Il Kim
Akihito Ishigami
Naoki Maruyama
Richard I Carp
Yong-Sun Kim
Eun-Kyoung Choi
Hallym University · KRTokyo Metropolitan Institute of Gerontology · JPCollege of Staten Island · USNew York State Office for People With Developmental Disabilities · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peptidylarginine deiminases (PADs), which are a group of posttranslational modification enzymes, are involved in protein citrullination (deimination) by the conversion of peptidylarginine to peptidylcitrulline in a calcium concentration-dependent manner. Among the PADs, PAD2 is widely distributed in various tissues and is the only type that is expressed in brain. To elucidate the involvement of protein citrullination by PAD2 in the pathogenesis of brain-specific prion diseases, we examined the profiles of citrullinated proteins using the brains of scrapie-infected mice as a prion disease model. We found that, compared with controls, increased levels of citrullinated proteins of various molecular weights were detected in different brain sections of scrapie-infected mice. In support of this data, expression levels of PAD2 protein as well as its enzyme activity were significantly increased in brain sections of scrapie-infected mice, including hippocampus, brain stem, and striatum. Additionally, the expression levels of PAD2 mRNA were increased during scrapie infection. Moreover, PAD2 immunoreactivity was increased in scrapie-infected brains, with staining detected primarily in reactive astrocytes. Using two-dimensional electrophoresis and matrix-assisted laser desorption/ionization-time of flight mass spectrometry, various citrullinated proteins were identified in the brains of scrapie-infected mice, including glial fibrillary acidic protein, myelin basic protein, enolases, and aldolases. This study suggests that accumulated citrullinated proteins and abnormal activation of PAD2 may function in the pathogenesis of prion diseases and serve as potential therapeutic targets.

Indexed as

AnimalsAstrocytesBrainCitrullineElectrophoresis, Gel, Two-DimensionalFluorescent Antibody TechniqueFructose-Bisphosphate AldolaseGlial Fibrillary Acidic ProteinHydrolasesImmunohistochemistryMiceMice, Inbred C57BLMyelin Basic ProteinPhosphopyruvate HydrataseProtein-Arginine DeiminasesProteinsCitrullineFructose-Bisphosphate AldolaseGlial Fibrillary Acidic ProteinHydrolasesMyelin Basic ProteinPhosphopyruvate HydrataseProtein-Arginine DeiminasesProteinsPrPSc Proteins

Identifiers

PMID18787103
PMCPMC2543080
OpenAlexW1799202546

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.