Evidence map›Paper›PMID 25267995›Full record

ArticleJournal of lipid research2014

Renal sulfatides: sphingoid base-dependent localization and region-specific compensation of CerS2-dysfunction.

Christian Marsching, Mariona Rabionet, Daniel Mathow, Richard Jennemann, Christiane Kremser, Stefan Porubsky, Christian Bolenz, Klaus Willecke, Hermann-Josef Gröne, Carsten Hopf and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

16 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Sulfatides are endogenous ligands for the TLR4-MD-2 complex.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Identification ofJournal of the American Society of Nephrology : JASN · 2019
    Article
  11. Review
  12. Kidney Lipidomics by Mass Spectrometry Imaging: A Focus on the Glomerulus.International journal of molecular sciences · 2019
    Review
  13. Article
  14. Article
  15. Article
  16. Article
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

11 authors at 5 institutions in 1 country.

Christian MarschingCenter for Applied Research "Applied Biomedical Mass Spectrometry" (ABIMAS), Mannheim, Germany Lipid Pathobiochemistry Group within Department of Cellular and Molecular Pathology German Cancer Research Center (DKFZ), Heidelberg, Germany Institute of Medical Technology, University of Heidelberg and Mannheim University of Applied Sciences, Mannheim, Germany.
Mariona RabionetLipid Pathobiochemistry Group within Department of Cellular and Molecular Pathology German Cancer Research Center (DKFZ), Heidelberg, Germany.
Daniel MathowGerman Cancer Research Center (DKFZ), Heidelberg, Germany.
Richard JennemannGerman Cancer Research Center (DKFZ), Heidelberg, Germany.
Christiane KremserMolecular Genetics, Life and Medical Sciences (LIMES) Institute, University of Bonn, Bonn, Germany.
Stefan PorubskyDepartments of Pathology and Urology.
Christian BolenzUniversity Medical Center Mannheim, University of Heidelberg, Mannheim, Germany.
Klaus WilleckeMolecular Genetics, Life and Medical Sciences (LIMES) Institute, University of Bonn, Bonn, Germany.
Hermann-Josef GröneCenter for Applied Research "Applied Biomedical Mass Spectrometry" (ABIMAS), Mannheim, Germany German Cancer Research Center (DKFZ), Heidelberg, Germany.
Carsten HopfCenter for Applied Research "Applied Biomedical Mass Spectrometry" (ABIMAS), Mannheim, Germany Institute of Medical Technology, University of Heidelberg and Mannheim University of Applied Sciences, Mannheim, Germany Lipid Pathobiochemistry Group within Department of Cellular and Molecular Pathology.
Roger SandhoffCenter for Applied Research "Applied Biomedical Mass Spectrometry" (ABIMAS), Mannheim, Germany Lipid Pathobiochemistry Group within Department of Cellular and Molecular Pathology German Cancer Research Center (DKFZ), Heidelberg, Germany Instrumental Analytics and Bioanalytics, Mannheim University of Applied Sciences, Mannheim, Germany.
German Cancer Research Center · DEUniversity of Bonn · DEHeidelberg University · DEMannheim University of Applied Sciences · DEUniversity Hospital Heidelberg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mammalian kidneys are rich in sulfatides. Papillary sulfatides, especially, contribute to renal adaptation to chronic metabolic acidosis. Due to differences in their cer-amide (Cer) anchors, the structural diversity of renal sulfatides is large. However, the underling biological function of this complexity is not understood. As a compound's function and its tissue location are intimately connected, we analyzed individual renal sulfatide distributions of control and Cer synthase 2 (CerS)2-deficient mice by imaging MS (IMS) and by LC-MS(2) (in controls for the cortex, medulla, and papillae separately). To explain locally different structures, we compared our lipid data with regional mRNA levels of corresponding anabolic enzymes. The combination of IMS and in source decay-LC-MS(2) analyses revealed exclusive expression of C20-sphingosine-containing sulfatides within the renal papillae, whereas conventional C18-sphingosine-containing compounds were predominant in the medulla, and sulfatides with a C18-phytosphingosine were restricted to special cortical structures. CerS2 deletion resulted in bulk loss of sulfatides with C23/C24-acyl chains, but did not lead to decreased urinary pH, as previously observed in sulfatide-depleted kidneys. The reasons may be the almost unchanged C22-sulfatide levels and constant total renal sulfatide levels due to compensation with C16- to C20-acyl chain-containing compounds. Intriguingly, CerS2-deficient kidneys were completely depleted of phytosphingosine-containing cortical sulfatides without any compensation.

Indexed as

AnimalsFemaleGene Expression Regulation, EnzymologicKidneyMiceMolecular ImagingOrgan SpecificityRNA, MessengerSerine C-PalmitoyltransferaseSphingosine N-AcyltransferaseSulfoglycosphingolipidsCers2 protein, mouseRNA, MessengerSerine C-PalmitoyltransferaseSphingosine N-AcyltransferasessSPTaSulfoglycosphingolipidsceramide synthase 2cortexelectrospray ionization-mass spectrometrygalactosylceramide I3-sulfateimaging mass spectrometryin source decayknockoutlactosylceramide II3-sulfateliquid chromatographymatrix-assisted laser desorption/ionization-time-of-flightmedullapapillaeserine palmitoyl-coenzyme A transferase small subunitssphingosinetandem mass spectrometry

Identifiers

PMID25267995
PMCPMC4617137
OpenAlexW2145202716

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.