ArticleThe Journal of biological chemistry2008
Quantifying cathepsin S activity in antigen presenting cells using a novel specific substrate.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 62 citations in OpenAlex.
- Engineering Cathepsin S Selective Chemical Probes and Antibody-Drug Conjugates through Substrate Profiling with Unnatural Amino Acids.Journal of medicinal chemistry · 2026Article
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- Controlling intracellular processing to enhance spherical nucleic acid immune stimulation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The pH-Dependent Specificity of Cathepsin S and Its Implications for Inflammatory Communications and Disease.Biochemistry · 2025Article
- Structural and Stability Analysis of GRP Family Allergens Pru p 7 and Cry j 7, Which Cause Pollen and Food Allergy Syndrome.Biomolecules · 2025Article
- Key Genes in Olfactory Disorder in Experimental Autoimmune Encephalomyelitis Identified by Transcriptomic Analysis of the Olfactory Bulbs.Molecular neurobiology · 2024Article
- Dipeptide-Derived Alkynes as Potent and Selective Irreversible Inhibitors of Cysteine Cathepsins.Journal of medicinal chemistry · 2023Article
- Challenges and opportunities in analyzing and modeling peptide presentation by HLA-II proteins.Frontiers in immunology · 2023Article
- Peptidyl-Resin Substrates as a Tool in the Analysis of Caspase Activity.Molecules (Basel, Switzerland) · 2022Article
- Structure determinants defining the specificity of papain-like cysteine proteases.Computational and structural biotechnology journal · 2022Review
- New inhibitors of cathepsin V impair tumor cell proliferation and elastin degradation and increase immune cell cytotoxicity.Computational and structural biotechnology journal · 2022Article
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- 1,4-Disubstituted 1,2,3-Triazoles as Amide Bond Surrogates for the Stabilisation of Linear Peptides with Biological Activity.Molecules (Basel, Switzerland) · 2020Review
- Thrombin alters the synthesis and processing of CYR61/CCN1 in human corneal stromal fibroblasts and myofibroblasts through multiple distinct mechanisms.Molecular vision · 2020Article
- Cysteine-type cathepsins promote the effector phase of acute cutaneous delayed-type hypersensitivity reactions.Theranostics · 2019Article
- Eliciting unnatural immune responses by activating cryptic epitopes in viral antigens.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018Article
- Retinoic acid prevents immunogenicity of milk lipocalin Bos d 5 through binding to its immunodominant T-cell epitope.Scientific reports · 2018Article
- Protective cellular immunity generated by cross-presenting recombinant overlapping peptide proteins.Oncotarget · 2017Article
- Investigation into the Biological Impact of Block Size on Cathepsin S-Degradable HPMA Copolymers.Molecular pharmaceutics · 2017Article
- Highly sensitive and adaptable fluorescence-quenched pair discloses the substrate specificity profiles in diverse protease families.Scientific reports · 2017Article
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Authors and funding
2 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cathepsin S (CatS) is a lysosomal cysteine protease belonging to the papain superfamily. Because of the relatively broad substrate specificity of this family, a specific substrate for CatS is not yet known. Based on a detailed study of the CatS endopeptidase specificity, using six series of internally quenched fluorescent peptides, we were able to design a specific substrate for CatS. The peptide series was based on the sequence GRWHTVGLRWE-Lys(Dnp)-DArg-NH2, which shows only one single cleavage site between Gly and Leu and where every substrate position between P-3 and P-3' was substituted with up to 15 different amino acids. The endopeptidase specificity of CatS was mainly determined by the P-2, P-1', and the P-3' substrate positions. Based on this result, systematically modified substrates were synthesized. Two of these modified substrates, Mca-GRWPPMGLPWE-Lys(Dnp)-DArg-NH2 and Mca-GRWHPMGAPWE-Lys(Dnp)-DArg-NH2, did not react with the purified cysteine proteases cathepsin B (CatB) and cathepsin L (CatL). Using a specific CatS inhibitor, we could further show that these two peptides were not cleaved by endosomal fractions of antigen presenting cells (APCs), when CatS was inhibited and related cysteine proteases cathepsin B, H, L and X were still active. Although aspartic proteases like cathepsin E and cathepsin D were also present, our substrates were suitable to quantify cathepsin S activity specifically in APCs, including B cells, macrophages, and dendritic cells without the use of any protease inhibitor. We find that CatS activity differs significantly not only between the three types of professional APCs but also between endosomal and lysosomal compartments.
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