ArticleBiological chemistry2016
Photoactivated inhibition of cathepsin K in a 3D tumor model.
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 17 papers.
What it found
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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
17 citing papers in PubMed, 25 citations in OpenAlex.
- Mixed Ru(II)-Ir(III) Complexes as Photoactive Inhibitors of the Major Human Drug Metabolizing Enzyme CYP3A4.Inorganic chemistry · 2024Article
- The Proteolytic Landscape of Ovarian Cancer: Applications in Nanomedicine.International journal of molecular sciences · 2022Review
- Photocytotoxicity and photoinduced phosphine ligand exchange in a Ru(ii) polypyridyl complex.Chemical science · 2022Article
- Light-responsive and Protic Ruthenium Compounds Bearing Bathophenanthroline and Dihydroxybipyridine Ligands Achieve Nanomolar Toxicity towards Breast Cancer Cells.Photochemistry and photobiology · 2022Article
- The Development of Ru(II)-Based Photoactivated Chemotherapy Agents.Molecules (Basel, Switzerland) · 2021Review
- Singlet Oxygen Formation vs Photodissociation for Light-Responsive Protic Ruthenium Anticancer Compounds: The Oxygenated Substituent Determines Which Pathway Dominates.Inorganic chemistry · 2021Article
- Visible-to-NIR-Light Activated Release: From Small Molecules to Nanomaterials.Chemical reviews · 2020Article
- Targeting cathepsin K diminishes prostate cancer establishment and growth in murine bone.Journal of cancer research and clinical oncology · 2019Article
- Catch and Release Photosensitizers: Combining Dual-Action Ruthenium Complexes with Protease Inactivation for Targeting Invasive Cancers.Journal of the American Chemical Society · 2018Article
- New Ru(ii) complex for dual photochemotherapy: release of cathepsin K inhibitor andDalton transactions (Cambridge, England : 2003) · 2018Article
- Ru(II) Polypyridyl Complexes Derived from Tetradentate Ancillary Ligands for Effective Photocaging.Accounts of chemical research · 2018Article
- Effects of the Bidentate Ligand on the Photophysical Properties, Cellular Uptake, and (Photo)cytotoxicity of Glycoconjugates Based on the [Ru(tpy)(NN)(L)]Chemistry (Weinheim an der Bergstrasse, Germany) · 2018Article
- Ru(ii) polypyridyl complexes as photocages for bioactive compounds containing nitriles and aromatic heterocycles.Chemical communications (Cambridge, England) · 2018Article
- Photochemical and Photobiological Activity of Ru(II) Homoleptic and Heteroleptic Complexes Containing Methylated Bipyridyl-type Ligands.Inorganic chemistry · 2017Article
- Caging the uncageable: using metal complex release for photochemical control over irreversible inhibition.Chemical communications (Cambridge, England) · 2016Article
- Effects of Methyl Substitution in Ruthenium Tris(2-pyridylmethyl)amine Photocaging Groups for Nitriles.Inorganic chemistry · 2016Article
- New 3D-Culture Approaches to Study Interactions of Bone Marrow Adipocytes with Metastatic Prostate Cancer Cells.Frontiers in endocrinology · 2016Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Collagenolytic activity of cathepsin K is important for many physiological and pathological processes including osteoclast-mediated bone degradation, macrophage function and fibroblast-mediated matrix remodeling. Here, we report application of a light-activated inhibitor for controlling activity of cathepsin K in a 3D functional imaging assay. Using prostate carcinoma cell line engineered to overexpress cathepsin K, we demonstrate the utility of the proteolytic assay in living tumor spheroids for the evaluation and quantification of the inhibitor effects on cathepsin K-mediated collagen I degradation. Importantly, we also show that utilizing the ruthenium-caged version of a potent nitrile cathepsin K inhibitor (4), cis-[Ru(bpy)2(4)2](BF4)2 (5), offers significant advantage in terms of effective concentration of the inhibitor and especially its light-activated control in the 3D assay. Our results suggest that light activation provides a suitable, attractive approach for spatial and temporal control of proteolytic activity, which remains a critical, unmet need in treatment of human diseases, especially cancer.
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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.