Evidence map›Paper›PMID 21880860›Full record

ArticleJournal of lipid research2011

Enzymological analysis of the tumor suppressor A-C1 reveals a novel group of phospholipid-metabolizing enzymes.

Naoki Shinohara, Toru Uyama, Xing-Hua Jin, Kazuhito Tsuboi, Takeharu Tonai, Hitoshi Houchi, Natsuo Ueda

Open access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed, 55 citations in OpenAlex.

  1. The Phospholipase AJournal of lipid and atherosclerosis · 2026
    Review
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  3. Recent Progress inInternational journal of molecular sciences · 2025
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  4. Review
  5. Article
  6. Article
  7. Current Knowledge on Mammalian Phospholipase AMolecules (Basel, Switzerland) · 2022
    Review
  8. PLAAT1 inhibits type I interferon responseFrontiers in immunology · 2022
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. LipoproteinmBio · 2020
    Article
  15. Endocannabinoids and relatedInflammation and regeneration · 2018
    Review
  16. Article
  17. Article
  18. The HRASLS (PLA/AT) subfamily of enzymes.Journal of biomedical science · 2015
    Review
  19. Article
  20. 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

7 authors at 3 institutions in 2 countries.

Naoki ShinoharaDepartment of Biochemistry, Kagawa University School of Medicine, Miki, Kagawa 761-0793, Japan.
Toru Uyama
Xing-Hua Jin
Kazuhito Tsuboi
Takeharu Tonai
Hitoshi Houchi
Natsuo Ueda
Kagawa University · JPKagawa University Hospital · JPUji Hospital · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A-C1 protein is the product of a tumor suppressor gene negatively regulating the oncogene Ras and belongs to the HRASLS (HRAS-like suppressor) subfamily. We recently found that four members of this subfamily expressed in human tissues function as phospholipid-metabolizing enzymes. Here we examined a possible enzyme activity of A-C1. The homogenates of COS-7 cells overexpressing recombinant A-C1s from human, mouse, and rat showed a phospholipase A½ (PLA½) activity toward phosphatidylcholine (PC). This finding was confirmed with the purified A-C1. The activity was Ca²⁺ independent, and dithiothreitol and Nonidet P-40 were indispensable for full activity. Phosphatidylethanolamine (PE) was also a substrate and the phospholipase A₁ (PLA₁) activity was dominant over the PLA₂ activity. Furthermore, the protein exhibited acyltransferase activities transferring an acyl group of PCs to the amino group of PEs and the hydroxyl group of lyso PCs. As for tissue distribution in human, mouse, and rat, A-C1 mRNA was abundantly expressed in testis, skeletal muscle, brain, and heart. These results demonstrate that A-C1 is a novel phospholipid-metabolizing enzyme. Moreover, the fact that all five members of the HRASLS subfamily, including A-C1, show similar catalytic properties strongly suggests that these proteins constitute a new class of enzymes showing PLA½ and acyltransferase activities.

Indexed as

Enzyme AssaysAmino Acid SequenceAnimalsBiocatalysisCOS CellsGene Expression Regulation, EnzymologicHumansMiceMolecular Sequence DataPhospholipases APhospholipidsProteinsRatsPhospholipases APhospholipidsPLAAT1 protein, humanProteins

Identifiers

PMID21880860
PMCPMC3196224
OpenAlexW2078506867

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.