Evidence map›Paper›PMID 32812201›Full record

ArticleMolecular neurobiology2020

FABP7 Regulates Acetyl-CoA Metabolism Through the Interaction with ACLY in the Nucleus of Astrocytes.

Yoshiteru Kagawa, Banlanjo Abdulaziz Umaru, Hiroki Shima, Ryo Ito, Ryo Zama, Ariful Islam, Shin-Ichiro Kanno, Akira Yasui, Shun Sato, Kosuke Jozaki and 14 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular neurobiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

26 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
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  5. Cholinergic Phenotypes of Acetyl-CoA with ATP-Citrate Lyase Link.International journal of molecular sciences · 2026
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  11. Astrocytic FABP7 Alleviates Depression-Like Behaviors of Chronic Unpredictable Mild Stress Mice by Regulating Neuroinflammation and Hippocampal Spinogenesis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
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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

24 authors at 4 institutions in 1 country.

Yoshiteru KagawaDepartment of Organ Anatomy, Tohoku University Graduate School of Medicine, Sendai, 980-8575, Japan. kagawa@med.tohoku.ac.jp.ORCID http://orcid.org/0000-0003-2963-7905
Banlanjo Abdulaziz UmaruDepartment of Organ Anatomy, Tohoku University Graduate School of Medicine, Sendai, 980-8575, Japan.
Hiroki ShimaDepartment of Biochemistry, Tohoku University Graduate School of Medicine, Sendai, 980-8575, Japan.
Ryo ItoDepartment of Molecular Endocrinology, Tohoku University Graduate School of Medicine, Sendai, 980-8575, Japan.
Ryo ZamaDepartment of Organ Anatomy, Tohoku University Graduate School of Medicine, Sendai, 980-8575, Japan.
Ariful IslamDepartment of Organ Anatomy, Tohoku University Graduate School of Medicine, Sendai, 980-8575, Japan.
Shin-Ichiro KannoDivision of Dynamic Proteome in Aging and Cancer, Institute of Development, Aging and Cancer (IDAC), Tohoku University, Sendai, 980-8575, Japan.
Akira YasuiDivision of Dynamic Proteome in Aging and Cancer, Institute of Development, Aging and Cancer (IDAC), Tohoku University, Sendai, 980-8575, Japan.
Shun SatoDepartment of Obstetrics and Gynecology, Yamaguchi University Graduate School of Medicine, Ube, 755-0046, Japan.
Kosuke JozakiDepartment of Obstetrics and Gynecology, Yamaguchi University Graduate School of Medicine, Ube, 755-0046, Japan.
Subrata Kumar ShilDepartment of Organ Anatomy, Tohoku University Graduate School of Medicine, Sendai, 980-8575, Japan.
Hirofumi MiyazakiDepartment of Organ Anatomy, Tohoku University Graduate School of Medicine, Sendai, 980-8575, Japan.
Shuhei KobayashiDepartment of Organ Anatomy, Tohoku University Graduate School of Medicine, Sendai, 980-8575, Japan.
Yui YamamotoDepartment of Organ Anatomy, Tohoku University Graduate School of Medicine, Sendai, 980-8575, Japan.
Hiroshi KogoDepartment of Anatomy and Cell Biology, Gunma University Graduate School of Medicine, Maebashi, 371-8511, Japan.
Chie Shimamoto-MitsuyamaLaboratory for Molecular Psychiatry, RIKEN Center for Brain Science, Wako, 351-0198, Japan.
Akira SugawaraDepartment of Molecular Endocrinology, Tohoku University Graduate School of Medicine, Sendai, 980-8575, Japan.
Norihiro SuginoDepartment of Obstetrics and Gynecology, Yamaguchi University Graduate School of Medicine, Ube, 755-0046, Japan.
Masayuki KanamoriDepartment of Neurosurgery, Tohoku University Graduate School of Medicine, Sendai, 980-8575, Japan.
Teiji TominagaDepartment of Neurosurgery, Tohoku University Graduate School of Medicine, Sendai, 980-8575, Japan.
Takeo YoshikawaLaboratory for Molecular Psychiatry, RIKEN Center for Brain Science, Wako, 351-0198, Japan.
Kohji FukunagaDepartment of Pharmacology, Tohoku University Graduate School of Pharmaceutical Sciences, Sendai, 980-8578, Japan.
Kazuhiko IgarashiDepartment of Biochemistry, Tohoku University Graduate School of Medicine, Sendai, 980-8575, Japan.
Yuji OwadaDepartment of Organ Anatomy, Tohoku University Graduate School of Medicine, Sendai, 980-8575, Japan. owada@med.tohoku.ac.jp.
Tohoku University · JPYamaguchi University · JPRIKEN Center for Brain Science · JPGunma University · JP

Funding

Japan Agency for Medical Research and Development JP17dm0107071Japan Society for the Promotion of Science 15K16206Japan Society for the Promotion of Science 16H05116Japan Society for the Promotion of Science 17K15539Japan Society for the Promotion of Science 19H04026
6 · The paper itself

Abstract

Fatty acid binding protein 7 (FABP7) is an intracellular fatty acid chaperon that is highly expressed in astrocytes, oligodendrocyte-precursor cells, and malignant glioma. Previously, we reported that FABP7 regulates the response to extracellular stimuli by controlling the expression of caveolin-1, an important component of lipid raft. Here, we explored the detailed mechanisms underlying FABP7 regulation of caveolin-1 expression using primary cultured FABP7-KO astrocytes as a model of loss of function and NIH-3T3 cells as a model of gain of function. We discovered that FABP7 interacts with ATP-citrate lyase (ACLY) and is important for acetyl-CoA metabolism in the nucleus. This interaction leads to epigenetic regulation of several genes, including caveolin-1. Our novel findings suggest that FABP7-ACLY modulation of nuclear acetyl-CoA has more influence on histone acetylation than cytoplasmic acetyl-CoA. The changes to histone structure may modify caveolae-related cell activity in astrocytes and tumors, including malignant glioma.

Indexed as

AcetylationAcetyl Coenzyme AAnimalsAstrocytesATP Citrate (pro-S)-LyaseBase SequenceCaveolin 1Cell NucleusFatty Acid-Binding Protein 7HEK293 CellsHistonesHumansLysineMiceMice, KnockoutModels, BiologicalAcetyl Coenzyme AATP Citrate (pro-S)-LyaseCaveolin 1Fatty Acid-Binding Protein 7HistonesLysineAcetyl-CoAAstrocyteATP-citrate lyase (ACLY)Caveolin-1Fatty acid–binding protein (FABP)Histone acetylation

Identifiers

PMID32812201
PMCPMC7541391
OpenAlexW3066163410

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.