Evidence map›Paper›PMID 24732803›Full record

ArticleMolecular and cellular biology2014

Thioesterase superfamily member 2 (Them2) and phosphatidylcholine transfer protein (PC-TP) interact to promote fatty acid oxidation and control glucose utilization.

Yuki Kawano, Baran A Ersoy, Yingxia Li, Shin Nishiumi, Masaru Yoshida, David E Cohen

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.7field-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

21 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
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  8. The ThioesteraseOmics : a journal of integrative biology · 2021
    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

6 authors at 3 institutions in 2 countries.

Yuki KawanoDepartment of Medicine, Division of Gastroenterology, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts, USA.
Baran A ErsoyDepartment of Medicine, Division of Gastroenterology, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts, USA.
Yingxia LiDepartment of Medicine, Division of Gastroenterology, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts, USA.
Shin NishiumiDepartment of Internal Medicine, Division of Gastroenterology, Kobe University Graduate School of Medicine, Kobe, Japan.
Masaru YoshidaDepartment of Internal Medicine, Division of Gastroenterology, Kobe University Graduate School of Medicine, Kobe, Japan Department of Internal Medicine related, Division of Metabolomics Research, Kobe University Graduate School of Medicine, Kobe, Japan Integrated Center for Mass Spectrometry, Kobe University Graduate School of Medicine, Kobe, Japan.
David E CohenDepartment of Medicine, Division of Gastroenterology, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts, USA dcohen@partners.org.
Harvard University · USKobe University · JPBrigham and Women's Hospital · US

Funding

STRUCTURE-FUNCTION RELATIONSHIPS IN THE ALIMENTARY TRACTP30DK034854 · NIDDK · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAYNE I LENCER · 1986 to 2026
$32.4M
Phospholipid-Mediated Metabolic Control in the Pathogenesis of NAFLDR01DK056626 · NIDDK · YESHIVA UNIVERSITY · PI COHEN, DAVID E. · 2000 to 2024
$10.3M
Regulation of Hepatic Lipid and Glucose Metabolism by PC-TP/StarD2R37DK048873 · NIDDK · WEILL MEDICAL COLL OF CORNELL UNIV · PI COHEN, DAVID E. · 2012 to 2021
$5.5M
NIDDK NIH HHS P30 DK034854NIDDK NIH HHS R01 DK056626NIDDK NIH HHS R01 DK56626NIDDK NIH HHS R37 DK048873NIDDK NIH HHS R37 DK48873
6 · The paper itself

Abstract

Thioesterase superfamily member 2 (Them2) is a mitochondrion-associated long-chain fatty acyl coenzyme A (CoA) thioesterase that is highly expressed in the liver and oxidative tissues. Them2 activity in vitro is increased when it interacts with phosphatidylcholine transfer protein (PC-TP), a cytosolic lipid binding protein. Them2-/- and Pctp-/- mice exhibit enhanced hepatic insulin sensitivity and increased adaptive thermogenesis, and Them2-/- mice are also resistant to diet-induced hepatic steatosis. Although we showed previously that a Them2-PC-TP complex suppresses insulin signaling, the enzymatic activity of Them2 suggests additional direct involvement in regulating hepatic nutrient homeostasis. Here we used cultured primary hepatocytes to elucidate biochemical and cellular mechanisms by which Them2 and PC-TP regulate lipid and glucose metabolism. Under conditions simulating fasting, Them2-/- and Pctp-/- hepatocytes each exhibited decreased rates of fatty acid oxidation and gluconeogenesis. In results indicative of Them2-dependent regulation by PC-TP, chemical inhibition of PC-TP failed to reproduce these changes in Them2-/- hepatocytes. In contrast, rates of glucose oxidation and lipogenesis in the presence of high glucose concentrations were decreased only in Them2-/- hepatocytes. These findings reveal a primary role for Them2 in promoting mitochondrial oxidation of fatty acids and glucose in the liver.

Indexed as

AnimalsCells, CulturedEnergy MetabolismFatty AcidsFatty LiverGluconeogenesisGlucoseHepatocytesLipid MetabolismLipogenesisLiverMaleMiceMice, KnockoutMitochondriaOxidation-ReductionAcot13 protein, mouseFatty AcidsGlucosePhospholipid Transfer ProteinsThiolester Hydrolases

Identifiers

PMID24732803
PMCPMC4054321
OpenAlexW2124331361

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.