Evidence map›Paper›PMID 25667419›Full record

ArticleJournal of lipid research2015

Functional characterization of enzymes catalyzing ceramide phosphoethanolamine biosynthesis in mice.

Andreas Bickert, Christina Ginkel, Matthijs Kol, Katharina vom Dorp, Holger Jastrow, Joachim Degen, René L Jacobs, Dennis E Vance, Elke Winterhager, Xian-Cheng Jiang and 4 more

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 29 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed, 1 pooled it
3.4field-weighted citation impact, top 8% 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

29 citing papers in PubMed, 1 synthesis or guideline pooled it, 49 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Sphingolipids in neurodegenerative diseases.Frontiers in neuroscience · 2023
    Review
  12. Article
  13. Article
  14. Sphingomyelin Synthase Family and Phospholipase Cs.Advances in experimental medicine and biology · 2022
    Article
  15. Sphingomyelin synthase related protein is a mammalian phosphatidylethanolamine phospholipase C.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2021
    Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 6 institutions in 4 countries.

Andreas BickertMolecular Genetics, Life, and Medical Sciences Institute University of Bonn, 53115 Bonn, Germany.
Christina GinkelMolecular Genetics, Life, and Medical Sciences Institute University of Bonn, 53115 Bonn, Germany.
Matthijs KolMolecular Cell Biology Division, Department of Biology/Chemistry, University of Osnabrück, 49076 Osnabrück, Germany.
Katharina vom DorpInstitute of Molecular Physiology and Biotechnology of Plants, University of Bonn, 53115 Bonn, Germany.
Holger JastrowImaging Center Essen, Electron Microscopy Unit, University Hospital University of Duisburg-Essen, 45147 Essen, Germany.
Joachim DegenMolecular Genetics, Life, and Medical Sciences Institute University of Bonn, 53115 Bonn, Germany.
René L JacobsDepartments of Agricultural, Food, and Nutritional Science, Molecular and Cell Biology of Lipids, University of Alberta, T6G 2S2 Edmonton, Canada.
Dennis E VanceBiochemistry, University of Alberta, T6G 2S2 Edmonton, Canada.
Elke WinterhagerDepartment of Molecular Biology, University of Duisburg-Essen, 45147 Essen, Germany.
Xian-Cheng JiangDepartment of Anatomy and Cell Biology, SUNY Downstate Medical Center, Brooklyn, NY 11203.
Peter DörmannInstitute of Molecular Physiology and Biotechnology of Plants, University of Bonn, 53115 Bonn, Germany.
Pentti SomerharjuMedical Biochemistry, Institute of Biomedicine, University of Helsinki, 00014 Helsinki, Finland.
Joost C M HolthuisMolecular Cell Biology Division, Department of Biology/Chemistry, University of Osnabrück, 49076 Osnabrück, Germany.
Klaus WilleckeMolecular Genetics, Life, and Medical Sciences Institute University of Bonn, 53115 Bonn, Germany.
University of Bonn · DEOsnabrück University · DEUniversity of Alberta · CAUniversity of Duisburg-Essen · DESUNY Downstate Health Sciences University · USUniversity of Helsinki · FI

Funding

Canadian Institutes of Health Research MOP5182
6 · The paper itself

Abstract

Besides bulk amounts of SM, mammalian cells produce small quantities of the SM analog ceramide phosphoethanolamine (CPE). Little is known about the biological role of CPE or enzymes responsible for CPE production. Heterologous expression studies revealed that SM synthase (SMS)2 is a bifunctional enzyme producing both SM and CPE, whereas SMS-related protein (SMSr) serves as monofunctional CPE synthase. Acute disruption of SMSr catalytic activity in cultured cells causes a rise in endoplasmic reticulum (ER) ceramides, fragmentation of ER exit sites, and induction of mitochondrial apoptosis. To address the relevance of CPE biosynthesis in vivo, we analyzed the tissue-specific distribution of CPE in mice and generated mouse lines lacking SMSr and SMS2 catalytic activity. We found that CPE levels were >300-fold lower than SM in all tissues examined. Unexpectedly, combined inactivation of SMSr and SMS2 significantly reduced, but did not eliminate, tissue-specific CPE pools and had no obvious impact on mouse development or fertility. While SMSr is widely expressed and serves as the principal CPE synthase in the brain, blocking its catalytic activity did not affect ceramide levels or secretory pathway integrity in the brain or any other tissue. Our data provide a first inventory of CPE species and CPE-biosynthetic enzymes in mammals.

Indexed as

BiocatalysisAnimalsBrainCatalytic DomainCell SurvivalEnzyme ActivationExonsGene DeletionGene Expression Regulation, EnzymologicLiverMaleMiceMice, Inbred C57BLOrgan SpecificityPhosphatidylethanolamine N-MethyltransferasePoint Mutationceramide phosphoethanolaminePhosphatidylethanolamine N-MethyltransferaseSgms2 protein, mouseSphingomyelinsTransferases (Other Substituted Phosphate Groups)brain lipidsenzyme inactivationgeneticsmass spectrometrysphingolipidssphingomyelin synthasesphingomyelin synthase-related proteinsterile α motif domain-containing protein 8transgenic mice

Identifiers

PMID25667419
PMCPMC4373740
OpenAlexW2031850927

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.