Evidence map›Paper›PMID 32402239›Full record

ArticleCell chemical biology2020

A Plasma Protein Network Regulates PM20D1 and N-Acyl Amino Acid Bioactivity.

Joon T Kim, Mark P Jedrychowski, Wei Wei, Daniel Fernandez, Curt R Fischer, Steven M Banik, Bruce M Spiegelman, Jonathan Z Long

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed, 14 citations in OpenAlex.

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  9. The Biosynthesis and Metabolism of theFrontiers in molecular biosciences · 2021
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 1 country.

Joon T KimDepartment of Pathology, Stanford University School of Medicine, Stanford, CA 94305, USA; Stanford ChEM-H, Stanford University, Stanford, CA 94305, USA.
Mark P JedrychowskiDepartment of Cancer Biology, Dana-Farber Cancer Institute, and Department of Cell Biology, Harvard Medical School, Boston, MA 02215, USA.
Wei WeiDepartment of Pathology, Stanford University School of Medicine, Stanford, CA 94305, USA; Department of Biology, Stanford University, Stanford, CA 94305, USA; Stanford ChEM-H, Stanford University, Stanford, CA 94305, USA.
Daniel FernandezStanford ChEM-H, Stanford University, Stanford, CA 94305, USA.
Curt R FischerStanford ChEM-H, Stanford University, Stanford, CA 94305, USA.
Steven M BanikDepartment of Chemistry, Stanford University, Stanford, CA 94305, USA; Stanford ChEM-H, Stanford University, Stanford, CA 94305, USA.
Bruce M SpiegelmanDepartment of Cancer Biology, Dana-Farber Cancer Institute, and Department of Cell Biology, Harvard Medical School, Boston, MA 02215, USA.
Jonathan Z LongDepartment of Pathology, Stanford University School of Medicine, Stanford, CA 94305, USA; Stanford ChEM-H, Stanford University, Stanford, CA 94305, USA. Electronic address: jzlong@stanford.edu.
Stanford University · USHarvard University · USStanford Medicine · US

Funding

Stanford Islet Research CoreP30DK116074 · NIDDK · STANFORD UNIVERSITY · PI Seung K Kim · 2017 to 2026
$19.5M
Chemical control of energy metabolism by N-acyl amino acidsR01DK124265 · NIDDK · STANFORD UNIVERSITY · PI LONG, JONATHAN Z · 2020 to 2024
$2.0M
CIRCULATING FACTORS THAT REGULATE BROWN AND BEIGE FATR00DK105203 · NIDDK · STANFORD UNIVERSITY · PI LONG, JONATHAN Z · 2018 to 2020
$728k
Circulating Factors that Regulate Brown and Beige FatK99DK105203 · NIDDK · DANA-FARBER CANCER INST · PI LONG, JONATHAN Z · 2015 to 2016
$182k
NIDDK NIH HHS K99 DK105203NIDDK NIH HHS P30 DK116074NIDDK NIH HHS R00 DK105203NIDDK NIH HHS R01 DK124265
6 · The paper itself

Abstract

N-acyl amino acids are a family of cold-inducible circulating lipids that stimulate thermogenesis. Their biosynthesis is mediated by a secreted enzyme called PM20D1. The extracellular mechanisms that regulate PM20D1 or N-acyl amino acid activity in the complex environment of blood plasma remains unknown. Using quantitative proteomics, here we show that PM20D1 circulates in tight association with both low- and high-density lipoproteins. Lipoprotein particles are powerful co-activators of PM20D1 activity in vitro and N-acyl amino acid biosynthesis in vivo. We also identify serum albumin as a physiologic N-acyl amino acid carrier, which spatially segregates N-acyl amino acids away from their sites of production, confers resistance to hydrolytic degradation, and establishes an equilibrium between thermogenic "free" versus inactive "bound" fractions. These data establish lipoprotein particles as principal extracellular sites of N-acyl amino acid biosynthesis and identify a lipoprotein-albumin network that regulates the activity of a circulating thermogenic lipid family.

Indexed as

Adipose Tissue, BrownAdipose Tissue, WhiteAmidohydrolasesAmino AcidsAnimalsApolipoproteins EArachidonic AcidsBlood ProteinsCell LineGlycineHumansLipoproteinsMaleMiceMice, Inbred C57BLMice, KnockoutAmidohydrolasesAmino AcidsApoe protein, mouseApolipoproteins EArachidonic AcidsBlood ProteinsGlycineLipoproteinsN-arachidonylglycinePM20D1 protein, humanSerum AlbuminAlzheimerAPOEcirculatingHDLLDLlipidslipoproteinN-acyl amino acidobesityplasmaPM20D1

Identifiers

PMID32402239
PMCPMC7502524
OpenAlexW3025482730

What OpenQuestion holds

Textmetadata
LicenceTDM
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.