ArticleBiological chemistry2016
Procathepsin E is highly abundant but minimally active in pancreatic ductal adenocarcinoma tumors.
Article in Biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Addressing the unmet clinical need for low-volume assays in early diagnosis of pancreatic cancer.Frontiers in gastroenterology (Lausanne, Switzerland) · 2023Article
- Multiplex substrate profiling by mass spectrometry for proteases.Methods in enzymology · 2023Article
- Drug Repurposing Opportunities in Pancreatic Ductal Adenocarcinoma.Pharmaceuticals (Basel, Switzerland) · 2021Review
- Cathepsin E expression and activity: Role in the detection and treatment of pancreatic cancer.Pancreatology : official journal of the International Association of Pancreatology (IAP) ... [et al.] · 2019Review
- Global substrate specificity profiling of post-translational modifying enzymes.Protein science : a publication of the Protein Society · 2018Review
- Pancreatic cancer: Current status and Challenges.Current pharmacology reports · 2017Article
- Global Protease Activity Profiling Provides Differential Diagnosis of Pancreatic Cysts.Clinical cancer research : an official journal of the American Association for Cancer Research · 2017Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The cathepsin family of lysosomal proteases is increasingly being recognized for their altered expression in cancer and role in facilitating tumor progression. The aspartyl protease cathepsin E is overexpressed in several cancers and has been investigated as a biomarker for pancreatic ductal adenocarcinoma (PDAC). Here we show that cathepsin E expression in mouse PDAC tumors is increased by more than 400-fold when compared to healthy pancreatic tissue. Cathepsin E accumulates over the course of disease progression and accounts for more than 3% of the tumor protein in mice with end-stage disease. Through immunoblot analysis we determined that only procathepsin E exists in mouse PDAC tumors and cell lines derived from these tumors. By decreasing the pH, this procathepsion E is converted to the mature form, resulting in an increase in proteolytic activity. Although active site inhibitors can bind procathepsin E, treatment of PDAC mice with the aspartyl protease inhibitor ritonavir did not decrease tumor burden. Lastly, we used multiplex substrate profiling by mass spectrometry to identify two synthetic peptides that are hydrolyzed by procathepsin E near neutral pH. This work represents a comprehensive analysis of procathepsin E in PDAC and could facilitate the development of improved biomarkers for disease detection.
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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.