Evidence map›Paper›PMID 22134920›Full record

ArticleThe Journal of biological chemistry2012

Regulation of peroxisomal lipid metabolism by catalytic activity of tumor suppressor H-rev107.

Toru Uyama, Ikuyo Ichi, Nozomu Kono, Asuka Inoue, Kazuhito Tsuboi, Xing-Hua Jin, Nobukazu Araki, Junken Aoki, Hiroyuki Arai, Natsuo Ueda

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

23 citing papers in PubMed, 47 citations in OpenAlex.

  1. The Phospholipase AJournal of lipid and atherosclerosis · 2026
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  11. Hypoxia and Selective Autophagy in Cancer Development and Therapy.Frontiers in cell and developmental biology · 2018
    Review
  12. Peroxisomal Dysfunction in Age-Related Diseases.Trends in endocrinology and metabolism: TEM · 2017
    Review
  13. Article
  14. Article
  15. The HRASLS (PLA/AT) subfamily of enzymes.Journal of biomedical science · 2015
    Review
  16. Article
  17. Article
  18. Pla2g16 phospholipase mediates gain-of-function activities of mutant p53.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  19. 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 1 country.

Toru UyamaDepartment of Biochemistry, Kagawa University School of Medicine, 1750-1 Ikenobe, Miki, Kagawa 761-0793, Japan.
Ikuyo Ichi
Nozomu Kono
Asuka Inoue
Kazuhito Tsuboi
Xing-Hua Jin
Nobukazu Araki
Junken Aoki
Hiroyuki Arai
Natsuo Ueda
Kagawa University · JPThe University of Tokyo · JPTohoku University · JPJapan Science and Technology Agency · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

H-rev107 is a mammalian protein belonging to the HRAS-like suppressor family. Although the protein was originally found as a tumor suppressor, currently it is receiving considerable attention as a regulator of adipocyte lipolysis. We recently revealed that purified recombinant H-rev107 has phospholipase A(1/2) activity, releasing free fatty acids from glycerophospholipids with a preference for esterolysis at the sn-1 position. In the present study, we constitutively expressed H-rev107 in cloned HEK293 cells to examine its biological function in living cells. Initially, the cells accumulated free fatty acids. We also found a remarkable decrease in the levels of ether-type lipids, including plasmalogen and ether-type triglyceride, with a concomitant increase in fatty alcohols, substrates for the biosynthesis of ether-type lipids. Considering that peroxisomes are involved in the ether-type lipid biosynthesis, we next focused on peroxisomes and found that the peroxisomal markers 70-kDa peroxisomal membrane protein and catalase were abnormally distributed in the transfected cells. These biochemical and morphological abnormalities were not seen in HEK293 cells stably expressing a catalytically inactive mutant of H-rev107. When H-rev107 or its fusion protein with enhanced green fluorescence protein was transiently expressed in mammalian cells, both proteins were associated with peroxisomes in some of the observed cells. These results suggest that H-rev107 interferes with the biosynthesis of ether-type lipids and is responsible for the dysfunction of peroxisomes in H-rev107-expressing cells.

Indexed as

AnimalsCHO CellsCloning, MolecularCricetinaeCricetulusGene ExpressionHEK293 CellsHumansLipid MetabolismLipidsMicePeroxisomesPhospholipases A2, Calcium-IndependentTumor Suppressor ProteinsLipidsPhospholipases A2, Calcium-IndependentPlaat3 protein, mouseTumor Suppressor Proteins

Identifiers

PMID22134920
PMCPMC3268428
OpenAlexW2002995480

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.