Evidence map›Paper›PMID 17526733›Full record

ArticleMolecular and cellular biology2007

Enhanced sensitivity to cholera toxin in ADP-ribosylarginine hydrolase-deficient mice.

Jiro Kato, Jianfeng Zhu, Chengyu Liu, Joel Moss

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

40 citing papers in PubMed, 62 citations in OpenAlex.

  1. Review
  2. Review
  3. ADP-Ribosylation in Antiviral Innate Immune Response.Pathogens (Basel, Switzerland) · 2023
    Review
  4. Article
  5. Review
  6. Functional roles of ADP-ribosylation writers, readers and erasers.Frontiers in cell and developmental biology · 2022
    Review
  7. Article
  8. Review
  9. Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Review
  15. Review
  16. Review
  17. Review
  18. Review
  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

4 authors at 2 institutions in 1 country.

Jiro KatoPulmonary-Critical Care Medicine Branch, National Heart, Lung and Blood Institute, National Institutes of Health, Building 10, Room 6D05, MSC 1590, Bethesda, MD 20892-1590, USA.
Jianfeng Zhu
Chengyu Liu
Joel Moss
National Heart Lung and Blood Institute · USNational Institutes of Health · US

Funding

ADP-ribosylation CyclesZIAHL000659 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI MOSS, JOEL · 2009 to 2025
$29.8M
ADP-RIBOSYLATION CYCLESZ01HL000659 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI MOSS, JOEL · 1993 to 2008
$2.1M
Intramural NIH HHS
6 · The paper itself

Abstract

Cholera toxin (CT) produced by Vibrio cholerae causes the devastating diarrhea of cholera by catalyzing the ADP-ribosylation of the alpha subunit of the intestinal Gs protein (Gsalpha), leading to characteristic water and electrolyte losses. Mammalian cells contain ADP-ribosyltransferases similar to CT and an ADP-ribosyl(arginine)protein hydrolase (ADPRH), which cleaves the ADP-ribose-(arginine)protein bond, regenerating native protein and completing an ADP-ribosylation cycle. We hypothesized that ADPRH might counteract intoxication by reversing the ADP-ribosylation of Gsalpha. Effects of intoxication on murine ADPRH-/- cells were greater than those on wild-type cells and were significantly reduced by overexpression of wild-type ADPRH in ADPRH-/- cells, as evidenced by both ADP-ribose-arginine content and Gsalpha modification. Similarly, intestinal loops in the ADPRH-/- mouse were more sensitive than their wild-type counterparts to toxin effects on fluid accumulation, Gsalpha modification, and ADP-ribosylarginine content. Thus, CT-catalyzed ADP-ribosylation of cell proteins can be counteracted by ADPRH, which could function as a modifier gene in disease. Further, our study demonstrates that enzymatic cross talk exists between bacterial toxin ADP-ribosyltransferases and host ADP-ribosylation cycles. In disease, toxin-catalyzed ADP-ribosylation overwhelms this potential host defense system, resulting in persistence of ADP-ribosylation and intoxication of the cell.

Indexed as

Adenosine Diphosphate RiboseAnimalsBody FluidsCatalysisCholera ToxinCyclic AMPEmbryo, MammalianExonsGene TargetingGTP-Binding Protein alpha Subunits, GsHeterozygoteIntestinesMiceMice, Inbred C57BLMice, KnockoutMutant ProteinsAdenosine Diphosphate RiboseADP-ribosylarginineADP-ribosylarginine hydrolaseCholera ToxinCyclic AMPGTP-Binding Protein alpha Subunits, GsMutant ProteinsN-Glycosyl HydrolasesRecombinant Proteins

Identifiers

PMID17526733
PMCPMC1952103
OpenAlexW2109231616

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.