Evidence map›Paper›PMID 32632018›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Adiponectin and related C1q/TNF-related proteins bind selectively to anionic phospholipids and sphingolipids.

Jessica J Ye, Xin Bian, Jaechul Lim, Ruslan Medzhitov

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. 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
4.4field-weighted citation impact, top 4% 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, 45 citations in OpenAlex.

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  18. C1q as a potential tolerogenic therapeutic in transplantation.American journal of transplantation : official journal of the American Society of Transplantation and the American Society of Transplant Surgeons · 2021
    Article
  19. Review
  20. Adiponectin and Asthma: Knowns, Unknowns and Controversies.International journal of molecular sciences · 2021
    Review
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

4 authors at 1 institution in 1 country.

Jessica J YeHHMI, Yale University, New Haven, CT 06520.ORCID 0000-0001-8392-7423
Xin BianDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT 06520.
Jaechul LimHHMI, Yale University, New Haven, CT 06520.ORCID 0000-0002-6075-2656
Ruslan MedzhitovHHMI, Yale University, New Haven, CT 06520; ruslan.medzhitov@yale.edu.ORCID 0000-0002-7021-2012
Yale University · US

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007205 · NIGMS · YALE UNIVERSITY · PI KAZMIERCZAK, BARBARA I · 1985 to 2019
$42.9M
INTERDISCIPLINARY IMMUNOLOGY TRAINING PROGRAMT32AI007019 · NIAID · YALE UNIVERSITY · PI Carrie L. Lucas, David G. Schatz · 1985 to 2026
$14.4M
Role of GDF15 in the Regulation of Host Tolerance to InflammationR01AI144152 · NIAID · YALE UNIVERSITY · PI MEDZHITOV, RUSLAN · 2019 to 2023
$2.1M
Howard Hughes Medical InstituteNIAID NIH HHS R01 AI144152NIAID NIH HHS T32 AI007019NIGMS NIH HHS T32 GM007205
6 · The paper itself

Abstract

Adiponectin (Acrp30) is an adipokine associated with protection from cardiovascular disease, insulin resistance, and inflammation. Although its effects are conventionally attributed to binding Adipor1/2 and T-cadherin, its abundance in circulation, role in ceramide metabolism, and homology to C1q suggest an overlooked role as a lipid-binding protein, possibly generalizable to other C1q/TNF-related proteins (CTRPs) and C1q family members. To investigate this, adiponectin, representative family members, and variants were expressed in Expi293 cells and tested for binding to lipids in liposomes using density centrifugation. Binding to physiological lipids were also analyzed using gradient ultracentrifugation, liquid chromatography-mass spectrometry, and shotgun lipidomics. Interestingly, adiponectin selectively bound several anionic phospholipids and sphingolipids, including phosphatidylserine, ceramide-1-phosphate, glucosylceramide, and sulfatide, via the C1q domain in an oligomerization-dependent fashion. Binding to lipids was observed in liposomes, low-density lipoproteins, cell membranes, and plasma. Other CTRPs and C1q family members (Cbln1, CTRP1, CTRP5, and CTRP13) also bound similar lipids. These findings suggest that adiponectin and CTRPs function not only as hormones, but also as lipid opsonins, as may other C1q family proteins.

Indexed as

AdipokinesAdiponectinAnimalsAnionsCell MembraneCholesterol, LDLComplement C1qHumansLipid MetabolismLipidomicsLipoproteinsLiposomesMaleMiceMice, Inbred C57BLMice, KnockoutAdipokinesAdiponectinAdipoq protein, mouseAnionsCholesterol, LDLComplement C1qLipoproteinsLiposomesOpsonin ProteinsPhospholipidsSphingolipidsTNF protein, humanTumor Necrosis Factor-alphaadipokineadiponectinlipid bindingopsonin

Identifiers

PMID32632018
PMCPMC7382265
OpenAlexW3039224551

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.