Inhibitory prodrug mechanism for cysteine cathepsin-targeted self-controlled drug release

References

• Chatterjee K, Zhang J, Honbo N, Karliner JS. Doxorubicin cardiomyopathy. Cardiology. 2010;115:155–62. https://doi.org/10.1159/000265166.
   PubMed Web of Science ®Google Scholar
• Tacar O, Sriamornsak P, Dass CR. Doxorubicin: an update on anticancer molecular action, toxicity and novel drug delivery systems. J Pharm Pharmacol. 2013; 65: 157–70. https://doi.org/10.1111/j.2042-7158.2012.01567.x.
   PubMed Web of Science ®Google Scholar
• Olson OC, Joyce JA. Cysteine cathepsin proteases: regulators of cancer progression and therapeutic response. Nat Rev Cancer. 2015; 15: 712–29. https://doi.org/10.1038/nrc4027.
   PubMed Web of Science ®Google Scholar
• Mai J, Sameni M, Mikkelsen T, Sloane BF. Degradation of extracellular matrix protein tenascin-C by cathepsin B: an interaction involved in the progression of gliomas. Biol Chem. 2005; 383: 1407–13. https://doi.org/10.1515/BC.2002.159.
   Google Scholar
• Gocheva V, Wang H-W, Gadea BB, et al. IL-4 induces cathepsin protease activity in tumor-associated macrophages to promote cancer growth and invasion. Genes Dev. 2010; 24: 241–55. https://doi.org/10.1101/gad.1874010.
   PubMed Web of Science ®Google Scholar
• Sevenich L, Bowman RL, Mason SD, et al. Analysis of tumor- and stroma-supplied proteolytic networks reveals a brain metastasis-promoting role for cathepsin S. Nat Cell Biol. 2014;16:876–88. https://doi.org/10.1038/ncb3011.
   PubMed Web of Science ®Google Scholar
• Sobotič B, Vizovišek M, Vidmar R, et al. Proteomic identification of cysteine cathepsin substrates shed from the surface of cancer cells. Mol Cell Proteomics MCP. 2015;14:2213–28. https://doi.org/10.1074/mcp.M114.044628.
   PubMed Web of Science ®Google Scholar
• Wang B, Sun J, Kitamoto S, et al. Cathepsin S controls angiogenesis and tumor growth via matrix-derived angiogenic factors. J Biol Chem. 2006;281:6020–9. https://doi.org/10.1074/jbc.M509134200.
   PubMed Web of Science ®Google Scholar
• Small DM, Burden RE, Jaworski J, et al. Cathepsin S from both tumor and tumor-associated cells promote cancer growth and neovascularization. Int J Cancer. 2013;133:2102–12. https://doi.org/10.1002/ijc.28238.
   PubMed Web of Science ®Google Scholar
• Verdoes M, Oresic Bender K, Segal E, et al. Improved quenched fluorescent probe for imaging of cysteine cathepsin activity. J Am Chem Soc. 2013;135:14726–30. https://doi.org/10.1021/ja4056068.
   PubMed Web of Science ®Google Scholar
• Jakoš T, Pišlar A, Jewett A, Kos J. Cysteine cathepsins in tumor-associated immune cells. Front Immunol. 2019;10:2037. https://doi.org/10.3389/fimmu.2019.02037.
   PubMed Web of Science ®Google Scholar
• Qian B-Z, Pollard JW. Macrophage diversity enhances tumor progression and metastasis. Cell. 2010;141:39–51. https://doi.org/10.1016/j.cell.2010.03.014.
   PubMed Web of Science ®Google Scholar
• Olson OC, Kim H, Quail DF, et al. Tumor-associated macrophages suppress the cytotoxic activity of antimitotic agents. Cell Rep. 2017;19:101–13. https://doi.org/10.1016/j.celrep.2017.03.038.
   PubMed Web of Science ®Google Scholar
• Van Dalen FJ, Van Stevendaal MHME, Fennemann FL, et al. Molecular repolarisation of tumour-associated macrophages. Molecules. 2018;24:9. https://doi.org/10.3390/molecules24010009.
   PubMed Web of Science ®Google Scholar
• Drag M, Salvesen GS. Emerging principles in protease-based drug discovery. Nat Rev Drug Discov. 2010;9:690–701. https://doi.org/10.1038/nrd3053.
   PubMed Web of Science ®Google Scholar
• Choi KY, Swierczewska M, Lee S, Chen X. Protease-activated drug development. Theranostics. 2012;2:156–78. https://doi.org/10.7150/thno.4068.
   PubMed Web of Science ®Google Scholar
• Joshua Y, S H, K F, T F, H N, M G, Nynke S van den B, Jg V-M, A S, D S, S G, et al. A protease-activated, near-infrared fluorescent probe for early endoscopic detection of premalignant gastrointestinal lesions. Proceedings of the National Academy of Sciences of the United States of America. [Accessed 2022 06 05]. https://pubmed.ncbi.nlm.nih.gov/33443161/
   Google Scholar
• Bell-McGuinn KM, Garfall AL, Bogyo M, et al. Inhibition of cysteine cathepsin protease activity enhances chemotherapy regimens by decreasing tumor growth and invasiveness in a mouse model of multistage cancer. Cancer Res 2007;67:7378–85. https://doi.org/10.1158/0008-5472.CAN-07-0602.
   PubMed Web of Science ®Google Scholar
• Dubowchik GM, Firestone RA, Padilla L, et al. Cathepsin B-labile dipeptide linkers for lysosomal release of doxorubicin from internalizing immunoconjugates: model studies of enzymatic drug release and antigen-specific in vitro anticancer activity. Bioconjug Chem. 2002;13:855–69. https://doi.org/10.1021/bc025536j.
   PubMed Web of Science ®Google Scholar
• Moon S-J, Govindan SV, Cardillo TM, et al. Antibody conjugates of 7-ethyl-10-hydroxycamptothecin (SN-38) for targeted cancer chemotherapy. J Med Chem. 2008;51:6916–26. https://doi.org/10.1021/jm800719t.
   PubMed Web of Science ®Google Scholar
• Zhang X, Tang K, Wang H, et al. Design, synthesis, and biological evaluation of new cathepsin B-sensitive camptothecin nanoparticles equipped with a novel multifuctional linker. Bioconjug Chem. 2016;27:1267–75. https://doi.org/10.1021/acs.bioconjchem.6b00099.
   PubMed Web of Science ®Google Scholar
• Karnthaler‐Benbakka C, Koblmüller B, Mathuber M, et al. Synthesis, characterization and in vitro studies of a cathepsin B‐cleavable prodrug of the VEGFR inhibitor sunitinib. Chem Biodivers. 2019;16:e1800520. https://doi.org/10.1002/cbdv.201800520.
   PubMed Web of Science ®Google Scholar
• Gangoda L, Keerthikumar S, Fonseka P, et al. Inhibition of cathepsin proteases attenuates migration and sensitizes aggressive N-Myc amplified human neuroblastoma cells to doxorubicin. Oncotarget. 2015;6:11175–90. https://doi.org/10.18632/oncotarget.3579.
   PubMed Web of Science ®Google Scholar
• Sanman LE, Qian Y, Eisele NA, et al. Disruption of glycolytic flux is a signal for inflammasome signaling and pyroptotic cell death. eLife. 2016;5:e13663. https://doi.org/10.7554/eLife.13663.
   PubMed Web of Science ®Google Scholar
• van der Linden WA, Schulze CJ, Herbert AS, et al. Cysteine cathepsin inhibitors as anti-ebola agents. ACS Infect Dis. 2016; 2: 173–9. https://doi.org/10.1021/acsinfecdis.5b00130.
   PubMed Web of Science ®Google Scholar
• Reales-Calderón JA, Aguilera-Montilla N, Corbí ÁL, et al. Proteomic characterization of human proinflammatory M1 and anti-inflammatory M2 macrophages and their response to Candida Albicans. Proteomics. 2014;14:1503–18. https://doi.org/10.1002/pmic.201300508.
   PubMed Web of Science ®Google Scholar
• Liu Y, Xu R, Gu H, et al. Metabolic reprogramming in macrophage responses. Biomark Res. 2021;9:1. https://doi.org/10.1186/s40364-020-00251-y.
   PubMed Web of Science ®Google Scholar