Evidence map›Paper›PMID 36068249›Full record

ArticleScientific reports2022

Identification of a broad lipid repertoire associated to the endothelial cell protein C receptor (EPCR).

Elena Erausquin, María Morán-Garrido, Jorge Sáiz, Coral Barbas, Gilda Dichiara-Rodríguez, Alejandro Urdiciain, Jacinto López-Sagaseta

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.9field-weighted citation impact, top 12% 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

6 citing papers in PubMed, 12 citations in OpenAlex.

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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

7 authors at 4 institutions in 1 country.

Elena Erausquin *Unit of Protein Crystallography and Structural Immunology, Navarrabiomed, 31008, Pamplona, Navarra, Spain.
María Morán-Garrido *Centre of Metabolomics and Bioanalysis (CEMBIO), Department of Chemistry and Biochemistry, School of Pharmacy, Universidad San Pablo-CEU, CEU Universities, Urbanización Montepríncipe, 28660, Boadilla del Monte, Spain.
Jorge SáizCentre of Metabolomics and Bioanalysis (CEMBIO), Department of Chemistry and Biochemistry, School of Pharmacy, Universidad San Pablo-CEU, CEU Universities, Urbanización Montepríncipe, 28660, Boadilla del Monte, Spain.
Coral BarbasCentre of Metabolomics and Bioanalysis (CEMBIO), Department of Chemistry and Biochemistry, School of Pharmacy, Universidad San Pablo-CEU, CEU Universities, Urbanización Montepríncipe, 28660, Boadilla del Monte, Spain.
Gilda Dichiara-RodríguezUnit of Protein Crystallography and Structural Immunology, Navarrabiomed, 31008, Pamplona, Navarra, Spain.
Alejandro UrdiciainUnit of Protein Crystallography and Structural Immunology, Navarrabiomed, 31008, Pamplona, Navarra, Spain.
Jacinto López-SagasetaUnit of Protein Crystallography and Structural Immunology, Navarrabiomed, 31008, Pamplona, Navarra, Spain. jacinto.lopez.sagaseta@navarra.es.
Universidad San Pablo CEU · ESUniversidad de Navarra · ESNavarrabiomed · ESUniversidad Publica de Navarra · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Evidence is mounting that the nature of the lipid bound to the endothelial cell protein C receptor (EPCR) has an impact on its biological roles, as observed in anticoagulation and more recently, in autoimmune disease. Phosphatidylethanolamine and phosphatidylcholine species dominate the EPCR lipid cargo, yet, the extent of diversity in the EPCR-associated lipid repertoire is still unknown and remains to be uncovered. We undertook mass spectrometry analyses to decipher the EPCR lipidome, and identified species not yet described as EPCR ligands, such as phosphatidylinositols and phosphatidylserines. Remarkably, we found further, more structurally divergent lipids classes, represented by ceramides and sphingomyelins, both in less abundant quantities. In support of our mass spectrometry results and previous studies, high-resolution crystal structures of EPCR in three different space groups point to a prevalent diacyl phospholipid moiety in EPCR's pocket but a mobile and ambiguous lipid polar head group. In sum, these studies indicate that EPCR can associate with varied lipid classes, which might impact its properties in anticoagulation and the onset of autoimmune disease.

Indexed as

Autoimmune DiseasesPhospholipidsAnticoagulantsBlood Coagulation FactorsEndothelial Protein C ReceptorHumansReceptors, Cell Surfaceactivated protein C receptorAnticoagulantsBlood Coagulation FactorsEndothelial Protein C ReceptorPhospholipidsReceptors, Cell Surface

Identifiers

PMID36068249
PMCPMC9448719
OpenAlexW4294805052

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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.