ArticleBiochimica et biophysica acta2010
Selective detection of Cathepsin E proteolytic activity.
Article in Biochimica et biophysica acta, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 24 citations in OpenAlex.
- 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
- Recombinant protein susceptibility to proteolysis in the plant cell secretory pathway is pH-dependent.Plant biotechnology journal · 2018Article
- Peptide aptamer-modified single-walled carbon nanotube-based transistors for high-performance biosensors.Scientific 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
- Monitoring pancreatic carcinogenesis by the molecular imaging of cathepsin E in vivo using confocal laser endomicroscopy.PloS one · 2014Article
- Targeting cathepsin E in pancreatic cancer by a small molecule allows in vivo detection.Neoplasia (New York, N.Y.) · 2013Article
- Pancreatic cancer-associated Cathepsin E as a drug activator.Journal of controlled release : official journal of the Controlled Release Society · 2013Article
- Designing and developing S100P inhibitor 5-methyl cromolyn for pancreatic cancer therapy.Molecular cancer therapeutics · 2013Article
- Article
- Biochemical characterization and structural modeling of human cathepsin E variant 2 in comparison to the wild-type protein.Biological chemistry · 2012Article
- Molecular imaging of Cathepsin E-positive tumors in mice using a novel protease-activatable fluorescent probe.Molecular bioSystems · 2011Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
backgroundAspartic proteases Cathepsin (Cath) E and D are two different proteases, but they share many common characteristics, including molecular weight, catalytic mechanism, substrate preferences, proteolytic conditions and inhibition susceptibility. To define the biological roles of these proteases, it is necessary to elucidate their substrate specificity. In the present study, we report a new peptide-substrate that is only sensitive to Cath E but not Cath D.
methodsSubstrate e, Mca-Ala-Gly-Phe-Ser-Leu-Pro-Ala-Lys(Dnp)-DArg-CONH₂, designed in such a way that due to the close proximity of a Mca-donor and a Dnp-acceptor, near complete intramolecular quenching effect was achieved in its intact state. After the proteolytic cleavage of the hydrophobic motif of peptide substrate, both Mca and Dnp would be further apart, resulting in bright fluorescence.
resultsSubstrate e showed a 265 fold difference in the net fluorescence signals between Cath E and D. This Cath E selectivity was established by having -Leu**Pro- residues at the scissile peptide bond. The confined cleavage site of substrate e was confirmed by LC-MS. The catalytic efficiency (K(cat)/K(M)) of Cath E for substrate e was 16.7 μM⁻¹S⁻¹. No measurable catalytic efficiency was observed using Cath D and no detectable fluorescent changes when incubated with Cath S and Cath B.
conclusionsThis study demonstrated the promise of using the developed fluorogenic substrate e as a selective probe for Cath E proteolytic activity measurement. GENERAL SIGNIFICANCE: This study forms the foundation of Cath E specific inhibitor development in further studies.
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