ArticleCellular microbiology2010
Secreted cysteine proteases of the carcinogenic liver fluke, Opisthorchis viverrini: regulation of cathepsin F activation by autocatalysis and trans-processing by cathepsin B.
Article in Cellular microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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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.
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Who cites it
20 citing papers in PubMed, 40 citations in OpenAlex.
- Trematode Genomics and Proteomics.Advances in experimental medicine and biology · 2024Article
- Development of a subunit vaccine against the cholangiocarcinoma causingFrontiers in immunology · 2024Article
- Transcriptome changes of liver fluke Opisthorchis viverrini in diabetic hamsters.Parasite (Paris, France) · 2024Article
- Cystatins from the Human Liver FlukePathogens (Basel, Switzerland) · 2023Article
- Amino acids serve as an important energy source for adult flukes of Clonorchis sinensis.PLoS neglected tropical diseases · 2020Article
- Adaptive Radiation of the Flukes of the Family Fasciolidae Inferred from Genome-Wide Comparisons of Key Species.Molecular biology and evolution · 2020Article
- The MultitaskingFrontiers in immunology · 2019Article
- Opisthorchis viverrini Proteome and Host-Parasite Interactions.Advances in parasitology · 2018Review
- Molecular and Biochemical Characterization of Opisthorchis viverrini Calreticulin.The Korean journal of parasitology · 2017Article
- Cysteine Proteases: Modes of Activation and Future Prospects as Pharmacological Targets.Frontiers in pharmacology · 2016Review
- Article
- Characterization of the secreted cathepsin B cysteine proteases family of the carcinogenic liver fluke Clonorchis sinensis.Parasitology research · 2014Article
- The tumorigenic liver fluke Opisthorchis viverrini--multiple pathways to cancer.Trends in parasitology · 2012Review
- Evaluation of liver fluke recombinant cathepsin B-1 protease as a serodiagnostic antigen for human opisthorchiasis.Parasitology international · 2012Article
- Molecular changes in Opisthorchis viverrini (Southeast Asian liver fluke) during the transition from the juvenile to the adult stage.PLoS neglected tropical diseases · 2012Article
- Structural basis for inhibition of cathepsin B drug target from the human blood fluke, Schistosoma mansoni.The Journal of biological chemistry · 2011Article
- Inflammatory response to liver fluke Opisthorchis viverrini in mice depends on host master coregulator MTA1, a marker for parasite-induced cholangiocarcinoma in humans.Hepatology (Baltimore, Md.) · 2011Article
- RNA interference targeting cathepsin B of the carcinogenic liver fluke, Opisthorchis viverrini.Parasitology international · 2011Article
- Infection with the carcinogenic human liver fluke, Opisthorchis viverrini.Molecular bioSystems · 2011Review
- Collagenolytic activities of the major secreted cathepsin L peptidases involved in the virulence of the helminth pathogen, Fasciola hepatica.PLoS neglected tropical diseases · 2011Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 4 countries.
Funding
Abstract
Opisthorchis viverrini is an important helminth pathogen of humans that is endemic in Thailand and Laos. Adult flukes reside within host bile ducts and feed on epithelial tissue and blood cells. Chronic opisthorchiasis is associated with severe hepatobiliary diseases such as cholangiocarcinoma. Here we report that adult O. viverrini secrete two major cysteine proteases: cathepsin F (Ov-CF-1) and cathepsin B1 (Ov-CB-1). Ov-CF-1 is secreted as an inactive zymogen that autocatalytically processes and activates to a mature enzyme at pH 4.5 via an intermolecular cleavage at the prosegment-mature domain junction. Ov-CB-1 is also secreted as a zymogen but, in contrast to Ov-CF-1, is fully active against peptide and macromolecular substrates despite retaining the N-terminal prosegment. The active Ov-CB-1 zymogen was capable of trans-activating Ov-CF-1 by proteolytic removal of its prosegment at pH 5.5, a pH at which the Ov-CF-1 zymogen cannot autocatalytically activate. Both cathepsins hydrolyse human haemoglobin but their combined action more efficiently degrades haemoglobin to smaller peptides than each enzyme alone. Ov-CF-1 degraded extracellular matrix proteins more effectively than Ov-CB-1 at physiological pH. We propose that Ov-CB-1 regulates Ov-CF-1 activity and that both enzymes work together to degrade host tissue contributing to the development of liver fluke-associated cholangiocarcinoma.
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Registered trials
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.