ArticleBiological chemistry2010
Nuclear cysteine cathepsin variants in thyroid carcinoma cells.
Article in Biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 71 citations in OpenAlex.
- Novel Nucleus-Oriented Quenched Activity-Based Probes Link Cathepsin Nuclear Localization with Mitosis.ACS sensors · 2025Article
- Evaluating the Relationship between Cathepsins and Papillary Thyroid Carcinoma: A Mendelian Randomization Study.Endocrine, metabolic & immune disorders drug targets · 2025Article
- Distinct Cleavage Properties of Cathepsin B Compared to Cysteine Cathepsins Enable the Design and Validation of a Specific Substrate for Cathepsin B over a Broad pH Range.Biochemistry · 2023Article
- Review
- Investigations on Primary Cilia of Nthy-ori 3-1 Cells upon Cysteine Cathepsin Inhibition or Thyrotropin Stimulation.International journal of molecular sciences · 2023Article
- The role of primary cilia in thyroid diseases.Frontiers in endocrinology · 2023Review
- Cathepsin V regulates cell cycle progression and histone stability in the nucleus of breast cancer cells.Frontiers in pharmacology · 2023Article
- Extralysosomal cathepsin B in central nervous system: Mechanisms and therapeutic implications.Brain pathology (Zurich, Switzerland) · 2022Review
- Cathepsin B Gene Knockout Improves Behavioral Deficits and Reduces Pathology in Models of Neurologic Disorders.Pharmacological reviews · 2022Review
- Low-level lysosomal membrane permeabilization for limited release and sublethal functions of cathepsin proteases in the cytosol and nucleus.FEBS open bio · 2022Review
- Molecular Features of CA-074 pH-Dependent Inhibition of Cathepsin B.Biochemistry · 2022Article
- Selective Neutral pH Inhibitor of Cathepsin B Designed Based on Cleavage Preferences at Cytosolic and Lysosomal pH Conditions.ACS chemical biology · 2021Article
- Procathepsin V Is Secreted in a TSH Regulated Manner from Human Thyroid Epithelial Cells and Is Accessible to an Activity-Based Probe.International journal of molecular sciences · 2020Article
- Cathepsin Inhibition Modulates Metabolism and Polarization of Tumor-Associated Macrophages.Cancers · 2020Article
- Spatiotemporal proteomics uncovers cathepsin-dependent macrophage cell death during Salmonella infection.Nature microbiology · 2020Article
- Mast Cell β-Tryptase Is Enzymatically Stabilized by DNA.International journal of molecular sciences · 2020Article
- Association of Epithelial Mesenchymal Transition with prostate and breast health disparities.PloS one · 2018Article
- Proteolysis mediated by cysteine cathepsins and legumain-recent advances and cell biological challenges.Protoplasma · 2015Review
- Cathepsin B in antigen-presenting cells controls mediators of the Th1 immune response during Leishmania major infection.PLoS neglected tropical diseases · 2014Article
- Effect of EGb761 on light-damaged retinal pigment epithelial cells.International journal of ophthalmology · 2014Article
Corrections and comments
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Authors and funding
12 authors at 6 institutions in 5 countries.
Funding
Abstract
The cysteine peptidase cathepsin B is important in thyroid physiology by being involved in thyroid prohormone processing initiated in the follicular lumen and completed in endo-lysosomal compartments. However, cathepsin B has also been localized to the extrafollicular space and is therefore suggested to promote invasiveness and metastasis in thyroid carcinomas through, e.g., ECM degradation. In this study, immunofluorescence and biochemical data from subcellular fractionation revealed that cathepsin B, in its single- and two-chain forms, is localized to endo-lysosomes in the papillary thyroid carcinoma cell line KTC-1 and in the anaplastic thyroid carcinoma cell lines HTh7 and HTh74. This distribution is not affected by thyroid stimulating hormone (TSH) incubation of HTh74, the only cell line that expresses a functional TSH-receptor. Immunofluorescence data disclosed an additional nuclear localization of cathepsin B immunoreactivity. This was supported by biochemical data showing a proteolytically active variant slightly smaller than the cathepsin B proform in nuclear fractions. We also demonstrate that immunoreactions specific for cathepsin V, but not cathepsin L, are localized to the nucleus in HTh74 in peri-nucleolar patterns. As deduced from co-localization studies and in vitro degradation assays, we suggest that nuclear variants of cathepsins are involved in the development of thyroid malignancies through modification of DNA-associated proteins.
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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.