Evidence map›Paper›PMID 12737627›Full record

ArticleThe Biochemical journal2003

A novel protein phosphatase 2A (PP2A) is involved in the transformation of human protozoan parasite Trypanosoma cruzi.

Jorge González, Alberto Cornejo, Marcia R M Santos, Esteban M Cordero, Bessy Gutiérrez, Patricio Porcile, Renato A Mortara, Hernán Sagua, José Franco Da Silveira, Jorge E Araya

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2003. 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
1.4field-weighted citation impact, top 17% 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, 39 citations in OpenAlex.

  1. Interaction With the Extracellular Matrix Triggers Calcium Signaling inFrontiers in cellular and infection microbiology · 2021
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  10. Alcoholic-induced hepatic steatosis--role of ceramide and protein phosphatase 2A.Translational research : the journal of laboratory and clinical medicine · 2011
    Review
  11. Trypanosomatid protein phosphatases.Molecular and biochemical parasitology · 2010
    Review
  12. Inhibitory effect of ethanol on AMPK phosphorylation is mediated in part through elevated ceramide levels.American journal of physiology. Gastrointestinal and liver physiology · 2010
    Article
  13. Effect of ethanol on hydrogen peroxide-induced AMPK phosphorylation.American journal of physiology. Gastrointestinal and liver physiology · 2008
    Article
  14. Article
  15. 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

10 authors at 2 institutions in 2 countries.

Jorge GonzálezParasitology Unit, Department of Medical Technology, University of Antofagasta, Antofagasta, PO Box 170, Chile. jgonzalez@uantof.cl
Alberto Cornejo
Marcia R M Santos
Esteban M Cordero
Bessy Gutiérrez
Patricio Porcile
Renato A Mortara
Hernán Sagua
José Franco Da Silveira
Jorge E Araya
University of Antofagasta · CLUniversidade Federal de São Paulo · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Here we provide evidence for a critical role of PP2As (protein phosphatase 2As) in the transformation of Trypanosoma cruzi. In axenic medium at pH 5.0, trypomastigotes rapidly transform into amastigotes, a process blocked by okadaic acid, a potent PP2A inhibitor, at concentrations as low as 0.1 microM. 1-Norokadaone, an inactive okadaic acid analogue, did not affect the transformation. Electron microscopy studies indicated that okadaic acid-treated trypomastigotes had not undergone ultrastructural modifications, reinforcing the idea that PP2A inhibits transformation. Using a microcystin-Sepharose affinity column we purified the native T. cruzi PP2A. The enzyme displayed activity against 32P-labelled phosphorylase a that was inhibited in a dose-dependent manner by okadaic acid. The protein was also submitted to MS and, from the peptides obtained, degenerate primers were used to clone a novel T. cruzi PP2A enzyme by PCR. The isolated gene encodes a protein of 303 amino acids, termed TcPP2A, which displayed a high degree of homology (86%) with the catalytic subunit of Trypanosoma brucei PP2A. Northern-blot analysis revealed the presence of a major 2.1-kb mRNA hybridizing in all T. cruzi developmental stages. Southern-blot analysis suggested that the TcPP2A gene is present in low copy number in the T. cruzi genome. These results are consistent with the mapping of PP2A genes in two chromosomal bands by pulsed-field gel electrophoresis and chromoblot hybridization. Our studies suggest that in T. cruzi PP2A is important for the complete transformation of trypomastigotes into amastigotes during the life cycle of this protozoan parasite.

Indexed as

Amino Acid SequenceAnimalsChemical FractionationCytoskeletal ProteinsEnzyme InhibitorsFlagellaGenes, ProtozoanGenomeGrowth InhibitorsHumansMolecular Sequence DataOkadaic AcidPhosphoprotein PhosphatasesPhosphorylationProtein Phosphatase 2Transcription, GeneticCytoskeletal ProteinsEnzyme InhibitorsGrowth InhibitorsOkadaic AcidPhosphoprotein PhosphatasesProtein Phosphatase 2

Identifiers

PMID12737627
PMCPMC1223626
OpenAlexW2151568218

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.