Evidence map›Paper›PMID 18667693›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

GDPD5 is a glycerophosphocholine phosphodiesterase that osmotically regulates the osmoprotective organic osmolyte GPC.

Morgan Gallazzini, Joan D Ferraris, Maurice B Burg

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

52 citing papers in PubMed, 92 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Neurotransmitter acetylcholine mediates the mummification ofApplied and environmental microbiology · 2024
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

3 authors at 2 institutions in 1 country.

Morgan GallazziniLaboratory of Kidney and Electrolyte Metabolism, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20982, USA. gallazzinim@nhlbi.nih.gov
Joan D Ferraris
Maurice B Burg
National Heart Lung and Blood Institute · USNational Institutes of Health · US

Funding

Light Microscopy CoreZICHL006019 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI COMBS, CHRISTIAN · 2009 to 2025
$29.3M
ROLE OF ORGANIC OSMOLYTES IN RENAL CELLSZ01HL001283 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI BURG, MAURICE BENJAM · 1988 to 2008
$3.8M
Response Of Renal Cells To Osmotic StressZIAHL001283 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI BURG, MAURICE BENJAM · 2009 to 2010
$3.5M
Intramural NIH HHS
6 · The paper itself

Abstract

Glycerophosphocholine (GPC) is an abundant osmoprotective renal medullary organic osmolyte. We previously found that its synthesis from phosphatidylcholine is catalyzed by tonicity-regulated activity of the phospholipase B, neuropathy target esterase. We also found that its degradation is catalyzed by glycerophosphocholine phosphodiesterase (GPC-PDE) activity and that elevating osmolality from 300 to 500 mosmol/kg by adding NaCl or urea, inhibits GPC-PDE activity, which contributes to the resultant increase of GPC. In the present studies we identify GDPD5 (glycerophosphodiester phosphodiesterase domain containing 5) as a GPC-PDE that is rapidly inhibited by high NaCl or urea. Recombinant GDPD5 colocalizes with neuropathy target esterase in the perinuclear region of HEK293 cells, and immuno-precipitated recombinant GDPD5 degrades GPC in vitro. The in vitro activity is reduced when the cells from which the GDPD5 is immuno-precipitated have been exposed to high NaCl or urea. In addition, high NaCl decreases mRNA abundance of GDPD5 via an increase of its degradation rate, although high urea does not. At 300 mosmol/kg siRNA knockdown of GDPD5 increases GPC in mouse inner medullary collecting duct-3 cells, and over expression of recombinant GDPD5 increases cellular GPC-PDE activity, accompanied by decreased GPC. We conclude that GDPD5 is a GPC-PDE that contributes to osmotic regulation of cellular GPC.

Indexed as

Analysis of VarianceAnimalsBlotting, WesternCell LineDNA PrimersGlycerylphosphorylcholineHumansImmunoprecipitationKidneyMiceMicroscopy, FluorescencePhosphoric Diester HydrolasesReverse Transcriptase Polymerase Chain ReactionRNA InterferenceRNA, Small InterferingSodium ChlorideDNA Primersglycerophosphocholine phosphodiesteraseGlycerylphosphorylcholinePhosphoric Diester HydrolasesRNA, Small InterferingSodium ChlorideUrea

Identifiers

PMID18667693
PMCPMC2504799
OpenAlexW2084976551

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.