Evidence map›Paper›PMID 36997727›Full record

ArticleThe Journal of antibiotics2023

Allantopyrone A interferes with the degradation of hypoxia-inducible factor 1α protein by reducing proteasome activity in human fibrosarcoma HT-1080 cells.

Chiharu Okuda, Yuto Ueda, Makoto Muroi, Emiko Sanada, Hiroyuki Osada, Yoshihito Shiono, Ken-Ichi Kimura, Kenji Takeda, Koichiro Kawaguchi, Takao Kataoka

Abstract read
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Article in The Journal of antibiotics, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.5field-weighted citation impact, top 28% 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

0 citing papers in PubMed, 2 citations in OpenAlex.

No citing paper in PubMed yet.

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 5 institutions in 1 country.

Chiharu OkudaDepartment of Applied Biology, Kyoto Institute of Technology, Kyoto, Japan.
Yuto UedaDepartment of Applied Biology, Kyoto Institute of Technology, Kyoto, Japan.
Makoto MuroiBiomolecular Characterization Unit, Technology Platform Division, RIKEN Center for Sustainable Resource Science, Saitama, Japan.
Emiko SanadaChemical Resource Development Research Unit, Technology Platform Division, RIKEN Center for Sustainable Resource Science, Saitama, Japan.
Hiroyuki OsadaChemical Resource Development Research Unit, Technology Platform Division, RIKEN Center for Sustainable Resource Science, Saitama, Japan.ORCID 0000-0002-3606-4925
Yoshihito ShionoDepartment of Food, Life, and Environmental Science, Faculty of Agriculture, Yamagata University, Yamagata, Japan.
Ken-Ichi KimuraThe United Graduate School of Agricultural Sciences, Iwate University, Iwate, Japan.ORCID 0000-0002-4344-2525
Kenji TakedaDepartment of Applied Biology, Kyoto Institute of Technology, Kyoto, Japan.
Koichiro KawaguchiDepartment of Applied Biology, Kyoto Institute of Technology, Kyoto, Japan.
Takao KataokaDepartment of Applied Biology, Kyoto Institute of Technology, Kyoto, Japan. takao.kataoka@kit.ac.jp.ORCID 0000-0002-6000-4500
Kyoto Institute of Technology · JPRIKEN Center for Sustainable Resource Science · JPIwate University · JPUniversity of Shizuoka · JPYamagata University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Allantopyrone A is an α-pyrone metabolite that was originally isolated from the endophytic fungus Allantophomopsis lycopodina KS-97. We previously demonstrated that allantopyrone A exhibits anti-cancer, anti-inflammatory, and neuroprotective activities. In the present study, we showed that allantopyrone A up-regulated the protein expression of hypoxia-inducible factor (HIF)-1α in human fibrosarcoma HT-1080 cells. It also up-regulated the mRNA expression of BNIP3 and ENO1, but not other HIF target genes or HIF1A. Allantopyrone A did not inhibit the prolyl hydroxylation of HIF-1α, but enhanced the ubiquitination of cellular proteins. Consistent with this result, chymotrypsin-like and trypsin-like proteasome activities were reduced, but not completely inactivated by allantopyrone A. Allantopyrone A decreased the amount of proteasome catalytic subunits. Therefore, the present results showed that allantopyrone A interfered with the degradation of HIF-1α protein by reducing proteasome activity in human fibrosarcoma HT-1080 cells.

Indexed as

FibrosarcomaProteasome Endopeptidase ComplexHumansHypoxiaHypoxia-Inducible Factor 1, alpha SubunitPyronesallantopyrone AHypoxia-Inducible Factor 1, alpha SubunitProteasome Endopeptidase ComplexPyrones

Identifiers

PMID36997727
OpenAlexW4361274403

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.