Evidence map›Paper›PMID 24894599›Full record

ArticlePurinergic signalling2014

Schistosome apyrase SmATPDase1, but not SmATPDase2, hydrolyses exogenous ATP and ADP.

Akram A Da'dara, Rita Bhardwaj, Patrick J Skelly

Open access · bronzeAbstract read
In one paragraph

Article in Purinergic signalling, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.5field-weighted citation impact, top 13% 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

15 citing papers in PubMed, 33 citations in OpenAlex.

  1. Schistosoma mansoni and the purinergic halo.Trends in parasitology · 2022
    Review
  2. Article
  3. Mining Helminths for Novel Therapeutics.Trends in molecular medicine · 2021
    Review
  4. Review
  5. Basic Coagulation Profiles and Platelet Count AmongResearch and reports in tropical medicine · 2020
    Article
  6. Why Do Intravascular Schistosomes Coat Themselves in Glycolytic Enzymes?BioEssays : news and reviews in molecular, cellular and developmental biology · 2019
    Article
  7. Gene Expression in Developmental Stages ofInternational journal of molecular sciences · 2019
    Article
  8. Review
  9. Article
  10. Article
  11. IntravascularFrontiers in immunology · 2018
    Article
  12. Article
  13. Review
  14. Flavonoids and Sesquiterpene Lactones fromEvidence-based complementary and alternative medicine : eCAM · 2016
    Article
  15. Review
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 1 institution in 1 country.

Akram A Da'daraMolecular Helminthology Laboratory, Department of Infectious Disease and Global Health, Cummings School of Veterinary Medicine, Tufts University, North Grafton, MA, USA.
Rita Bhardwaj
Patrick J Skelly
Tufts University · US

Funding

Gene silencing in schistosomes using RNAiR01AI056273 · NIAID · TUFTS UNIVERSITY BOSTON · PI Patrick J Skelly · 2004 to 2026
$7.2M
Functional Characterization of the Schistosome TegumentR56AI056273 · NIAID · TUFTS UNIVERSITY BOSTON · PI SKELLY, PATRICK J · 2021 to 2021
$413k
NIAID NIH HHS AI-056273NIAID NIH HHS HHSN272201000005CNIAID NIH HHS HHSN272201000005INIAID NIH HHS R01 AI056273NIAID NIH HHS R56 AI056273
6 · The paper itself

Abstract

Schistosomes are parasitic worms that can live in the bloodstream of their vertebrate hosts for many years. It has been proposed that the worms impinge on host purinergic signalling by degrading proinflammatory molecules like ATP as well as prothrombotic mediators like ADP. This capability may help explain the apparent refractoriness of the worms to both immune elimination and thrombus formation. Three distinct ectoenzymes, expressed at the host-exposed surface of the worm's tegument, are proposed to be involved in the catabolism of ATP and ADP. These are alkaline phosphatase (SmAP), phosphodiesterase (SmNPP-5), and ATP diphosphohydrolase (SmATPDase1). It has recently been shown that only one of these enzymes-SmATPDase1-actually degrades exogenous ATP and ADP. However, a second ATP diphosphohydrolase homolog (SmATPDase2) is located in the tegument and has been reported to be released by the worms. It is possible that this enzyme too participates in the cleavage of exogenous nucleotide tri- and di-phosphates. To test this hypothesis, we employed RNA interference (RNAi) to suppress the expression of the schistosome SmATPDase1 and SmATPDase2 genes. We find that only SmATPDase1-suppressed parasites are significantly impaired in their ability to degrade exogenously added ATP or ADP. Suppression of SmATPDase2 does not appreciably affect the worms' ability to catabolize ATP or ADP. Furthermore, we detect no evidence for the secretion or release of an ATP-hydrolyzing activity by cultured parasites. The results confirm the role of tegumental SmATPDase1, but not SmADTPDase2, in the degradation of the exogenous proinflammatory and prothrombotic nucleotides ATP and ADP by live intravascular stages of the parasite.

Indexed as

Adenosine DiphosphateAdenosine TriphosphateAnimalsApyraseHost-Parasite InteractionsIsoenzymesMolecular Sequence DataReverse Transcriptase Polymerase Chain ReactionRNA, Small InterferingSchistosoma mansoniSchistosomiasis mansoniTranscriptomeTransfectionAdenosine DiphosphateAdenosine TriphosphateApyraseIsoenzymesRNA, Small Interfering

Identifiers

PMID24894599
PMCPMC4272364
OpenAlexW2157131625

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.