ArticleThe Journal of biological chemistry2013
Elastin degradation by cathepsin V requires two exosites.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 46 citations in OpenAlex.
- Exploration of tropocollagen unwinding by cathepsin K dimer with chondroitin 4-sulphate through microsecond timescale molecular dynamics.Journal of enzyme inhibition and medicinal chemistry · 2026Article
- Proteolysis at the extracellular matrix interface: Molecular architects and regulators in health and disease.The FEBS journal · 2026Review
- Regulation of Peptidase Activity beyond the Active Site in Human Health and Disease.International journal of molecular sciences · 2023Review
- Cathepsin V regulates cell cycle progression and histone stability in the nucleus of breast cancer cells.Frontiers in pharmacology · 2023Article
- Upregulation of cathepsin L gene under mild cold conditions in young Japanese male adults.Journal of physiological anthropology · 2021Article
- Molecular modeling for potential cathepsin L inhibitor identification as new anti-photoaging agents from tropical medicinal plants.Journal of bioenergetics and biomembranes · 2021Article
- Dual-Mechanism Quenched Fluorogenic Probe Provides Selective and Rapid Detection of Cathepsin L Activity*.ChemMedChem · 2021Article
- Homocysteine in Neurology: A Possible Contributing Factor to Small Vessel Disease.International journal of molecular sciences · 2021Review
- Cathepsin V suppresses GATA3 protein expression in luminal A breast cancer.Breast cancer research : BCR · 2020Article
- Review
- Cathepsin L induced PC-12 cell apoptosis via activation of B-Myb and regulation of cell cycle proteins.Acta pharmacologica Sinica · 2019Article
- Review
- Tri-arginine exosite patch of caspase-6 recruits substrates for hydrolysis.The Journal of biological chemistry · 2019Article
- Cathepsins: Proteases that are vital for survival but can also be fatal.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2018Review
- Cysteine protease cathepsins in cardiovascular disease: from basic research to clinical trials.Nature reviews. Cardiology · 2018Review
- l-Homocysteine-induced cathepsin V mediates the vascular endothelial inflammation in hyperhomocysteinaemia.British journal of pharmacology · 2018Article
- Cathepsin L promotes Vascular Intimal Hyperplasia after Arterial Injury.Molecular medicine (Cambridge, Mass.) · 2017Article
- A composite docking approach for the identification and characterization of ectosteric inhibitors of cathepsin K.PloS one · 2017Article
- Extracellular matrix turnover in coronary artery ectasia patients.Heart and vessels · 2016Article
- A novel approach to inhibit bone resorption: exosite inhibitors against cathepsin K.British journal of pharmacology · 2016Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Cathepsin V is a highly effective elastase and has been implicated in physiological and pathological extracellular matrix degradation. However, its mechanism of action remains elusive. Whereas human cathepsin V exhibits a potent elastolytic activity, the structurally homologous cathepsin L, which shares a 78% amino acid sequence, has only a minimal proteolytic activity toward insoluble elastin. This suggests that there are distinct structural domains that play an important role in elastinolysis. In this study, a total of 11 chimeras of cathepsins V and L were generated to identify elastin-binding domains in cathepsin V. Evaluation of these chimeras revealed two exosites contributing to the elastolytic activity of cathepsin V that are distant from the active cleft of the protease and are located in surface loop regions. Replacement of exosite 1 or 2 with analogous residues from cathepsin L led to a 75 and 43% loss in the elastolytic activity, respectively. Replacement of both exosites yielded a non-elastase variant similar to that of cathepsin L. Identification of these exosites may contribute to the design of inhibitors that will only affect the elastolytic activity of cysteine cathepsins without interfering with other physiological protease functions.
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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.