Evidence map›Paper›PMID 18092178›Full record

ArticleParasitology research2008

Characterization of cysteine proteases from the carcinogenic liver fluke, Opisthorchis viverrini.

Natthawut Kaewpitoon, Thewarach Laha, Sasithorn Kaewkes, Puangrat Yongvanit, Paul J Brindley, Alex Loukas, Banchob Sripa

Abstract read
PubMed Publisher
In one paragraph

Article in Parasitology research, 2008. 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
1.9field-weighted citation impact, top 16% 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, 25 citations in OpenAlex.

  1. Trematode Genomics and Proteomics.Advances in experimental medicine and biology · 2024
    Article
  2. Cystatins from the Human Liver FlukePathogens (Basel, Switzerland) · 2023
    Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Inhibition of cathepsin B activity by 2,3,7,8-tetrachlorodibenzo-p-dioxin.Environmental science and pollution research international · 2015
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Asparaginyl endopeptidase from the carcinogenic liver fluke, Opisthorchis viverrini, and its potential for serodiagnosis.International journal of infectious diseases : IJID : official publication of the International Society for Infectious Diseases · 2008
    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

7 authors at 3 institutions in 3 countries.

Natthawut KaewpitoonGraduate School, Khon Kaen University, Khon Kaen, Thailand.
Thewarach Laha
Sasithorn Kaewkes
Puangrat Yongvanit
Paul J Brindley
Alex Loukas
Banchob Sripa
Khon Kaen University · THQIMR Berghofer Medical Research Institute · AUTulane University · US

Funding

Pathogenesis of Liver Fluke Induced Cancer in ThailandU01AI065871 · NIAID · TULANE UNIVERSITY OF LOUISIANA · PI BRINDLEY, PAUL J · 2005 to 2009
$3.5M
NIAID NIH HHS AI065871NIAID NIH HHS U01 AI065871
6 · The paper itself

Abstract

Protease activities in extracts of Opisthorchis viverrini were investigated using gelatin zymography and fluorogenic peptide substrates. Using gelatin-impregnated X-ray film, 2 microg of O. viverrini excretory-secretory products (Ov-ES) and adult somatic extract (Ov-SE) showed proteolytic activity. Zymography of both O. viverrini extracts revealed bands at approximately 30 kDa. Using fluorogenic peptide substrates, the majority of O. viverrini activity was determined to be cathepsin L-like cysteine protease (cleaved Z-Phe-Arg-aminomethylcoumarin (AMC)) whereas little or no activity was ascribable to other classes of proteases. The O. viverrini cysteine protease activity was greatest at pH 6.0 and the activity was inhibited by the class-specific inhibitors, E-64 and Z-Ala-CHN2. Chromatographic purification of O. viverrini cysteine proteases on thiol-sepharose enriched for protein(s) of approximately 30 kDa from Ov-ES and Ov-SE. The activity profile of the purified enzyme was similar to that of the cathepsin L-like activity characterized in Ov-SE and Ov-ES. Furthermore, determination of cysteine protease activity in several developmental stages of the parasite revealed the highest protease activity in metacercariae soluble extract, followed by Ov-ES, egg soluble extract, and Ov-SE. These findings demonstrated that O. viverrini has a cathepsin L-like cysteine protease(s) and suggested that abundant cysteine protease activity was present in metacercariae where the hydrolase might be involved in cyst excystation during mammalian infection.

Indexed as

CathepsinsCysteine EndopeptidasesAnimalsCathepsin LChromatography, AffinityElectrophoresis, Polyacrylamide GelFluorometryGelatinHelminth ProteinsOpisthorchisCathepsin LCathepsinsCysteine EndopeptidasesGelatinHelminth Proteins

Identifiers

PMID18092178
OpenAlexW2075076470

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.