ArticleInternational journal of molecular sciences2020
Mast Cell β-Tryptase Is Enzymatically Stabilized by DNA.
Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 21 citations in OpenAlex.
- Mast cells release DNA Extracellular Traps (DETs) in response to SARS-CoV-2 and its spike protein.Cell communication and signaling : CCS · 2026Article
- Mast cell-driven remodeling of pulmonary immune and stromal landscapes in COVID-19.Scientific reports · 2026Article
- Article
- Immunomodulatory Significance of Mast Cell Exosomes (MC-EXOs) in Immune Response Coordination.Clinical reviews in allergy & immunology · 2025Review
- Article
- Amyloid Beta Peptides Lead to Mast Cell Activation in a Novel 3D Hydrogel Model.International journal of molecular sciences · 2023Article
- Mast Cells as a Potential Target of Molecular Hydrogen in Regulating the Local Tissue Microenvironment.Pharmaceuticals (Basel, Switzerland) · 2023Review
- Mast Cell Tryptase and Carboxypeptidase A3 in the Formation of Ovarian Endometrioid Cysts.International journal of molecular sciences · 2023Article
- UltramicronizedBiomolecules · 2023Article
- Protease Profile of Tumor-Associated Mast Cells in Melanoma.International journal of molecular sciences · 2022Article
- Review
- Mast Cell Tryptase Potentiates Neutrophil Extracellular Trap Formation.Journal of innate immunity · 2022Article
- Article
- Tryptase Regulates the Epigenetic Modification of Core Histones in Mast Cell Leukemia Cells.Frontiers in immunology · 2021Article
- Renal Mast Cell-Specific Proteases in the Pathogenesis of Tubulointerstitial Fibrosis.The journal of histochemistry and cytochemistry : official journal of the Histochemistry SocietyArticle
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Tryptase is a tetrameric serine protease located within the secretory granules of mast cells. In the secretory granules, tryptase is stored in complex with negatively charged heparin proteoglycans and it is known that heparin is essential for stabilizing the enzymatic activity of tryptase. However, recent findings suggest that enzymatically active tryptase also can be found in the nucleus of murine mast cells, but it is not known how the enzmatic activity of tryptase is maintained in the nuclear milieu. Here we hypothesized that tryptase, as well as being stabilized by heparin, can be stabilized by DNA, the rationale being that the anionic charge of DNA could potentially substitute for that of heparin to execute this function. Indeed, we showed that double-stranded DNA preserved the enzymatic activity of human β-tryptase with a similar efficiency as heparin. In contrast, single-stranded DNA did not have this capacity. We also demonstrated that DNA fragments down to 400 base pairs have tryptase-stabilizing effects equal to that of intact DNA. Further, we showed that DNA-stabilized tryptase was more efficient in degrading nuclear core histones than heparin-stabilized enzyme. Finally, we demonstrated that tryptase, similar to its nuclear localization in murine mast cells, is found within the nucleus of primary human skin mast cells. Altogether, these finding reveal a hitherto unknown mechanism for the stabilization of mast cell tryptase, and these findings can have an important impact on our understanding of how tryptase regulates nuclear events.
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Registered trials
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