Mast cell tryptases and chymases in inflammation and host defense.
Open accessAbstract
Tryptases and chymases are the major proteins stored and secreted by mast cells. The types, amounts, and properties of these serine peptidases vary by mast cell subtype, tissue, and mammal of origin. Membrane-anchored gamma-tryptases are tryptic, prostasin-like, type I peptidases that remain membrane attached on release and act locally. Soluble tryptases, including their close relatives, mastins, form inhibitor-resistant oligomers that act more remotely. Befitting their greater destructive potential, chymases are quickly inhibited after release, although some gain protection by associating with proteoglycans. Most chymase-like enzymes, including mast cell cathepsin G, hydrolyze chymotryptic substrates, an uncommon capability in the proteome. Some rodent chymases, however, have mutations resulting in elastolytic activity. Secreted tryptases and chymases promote inflammation, matrix destruction, and tissue remodeling by several mechanisms, including destroying procoagulant, matrix, growth, and differentiation factors and activating proteinase-activated receptors, urokinase, metalloproteinases, and angiotensin. They also modulate immune responses by hydrolyzing chemokines and cytokines. At least one chymase protects mice from intestinal worms. Tryptases and chymases can also oppose inflammation by inactivating allergens and neuropeptides causing inflammation and bronchoconstriction. Thus, like mast cells themselves, mast cell serine peptidases play multiple roles in host defense, and any accounting of benefit versus harm is necessarily context specific.
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Mast cell degranulation releases histamine, MMPs, tryptase and VEGF, which are involved in the attachment and posterior invasion of the embryo into the uterus.
“their degranulation causes the release of pivotal factors, e.g., histamine, MMPs, tryptase and VEGF, which are known to be involved in the attachment and posterior invasion of the embryo into the uterus.”
From Estradiol and Progesterone Regulate the Migration of Mast Cells from the Periphery to the Uterus and Induce Their Maturation and Degranulation (2010) · cites this paper as [30]
The Introduction (page unavailable) says mast-cell degranulation releases tryptase and histamine, and separately describes mast-cell proteases activating MMP-9. It does not establish that degranulation releases all four listed factors or that they participate in embryo attachment and invasion into the uterus; searches for implantation and VEGF did not find that connection. (LLM, conf=0.87)
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Self-citationNew developments in the genetics and activation of mast cell proteases
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Dog mastocytoma tryptase: Affinity purification, characterization, and amino-terminal sequence
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A Despecialization Step Underlying Evolution of a Family of Serine Proteases
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Potent selective nonpeptidic inhibitors of human lung tryptase
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Self-citationExpansion of the mast cell chymase locus over the past 200 million years of mammalian evolution
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Lack of expression of the tryptase mouse mast cell protease 7 in mast cells of the C57BL/6J mouse.
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Dog mast cell chymase: molecular cloning and characterization
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Rapid lineage-specific diversification of the mast cell chymase locus during mammalian evolution
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Distribution of chymase-containing mast cells in human bronchi.
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Albumin Is a Substrate of Human Chymase
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Role of tryptase in immediate cutaneous responses in allergic sheep
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Formation of Enzymatically Active, Homotypic, and Heterotypic Tetramers of Mouse Mast Cell Tryptases
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Transgenic study of the function of chymase in heart remodeling
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Effects of a reversible β‐tryptase and trypsin inhibitor (RWJ‐58643) on nasal allergic responses
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Self-citationBivalent inhibition of β-Tryptase: distance scan of neighboring subunits by dibasic inhibitors
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Mastin is a gelatinolytic mast cell peptidase resembling a mini-proteasome
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Self-citationSyntheses and evaluation of amidinobenzofuran derivatives as tryptase inhibitors
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A functional comparison of canine and murine bone marrow derived cultured mast cells
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Lys40 but not Arg143 influences selectivity of angiotensin conversion by human α-chymase
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Purification and Characterization of Dog Mast Cell Protease-3, an Oligomeric Relative of Tryptases
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Self-citationCloning and expression of the dog mast cell alpha-chymase gene
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Self-citationProteolysis of Pericellular Matrix
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Human Chymase Expression in a Mice Induces Mild Hypertension with Left Ventricular Hypertrophy
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Genetic insights into mast cell chymase and tryptase function
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Self-citationTherapeutic Targets in Airway Inflammation
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The development of allergic inflammation
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“histamine, tryptases, MMPs, VEGF, [2,30,45,47].”
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Positive selection on apoptosis related genes
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- Authors
- Caughey, G. H.
- Affiliations
- San Francisco VA Medical Center (US)
- Corresponding author
- Caughey, George H.
- ORCID
- Caughey, George H.
- Venue
- Immunological Reviews
- Publisher
- Wiley
- Published
- 2007-05-07
- Volume
- 217
- Issue
- 1
- Pages
- 141-154
- ISSN
- 0105-2896 (ISSN-L)
- 1600-065X
- PMC
- PMC2275918
- OpenAlex
- W1993305093
- Cited by
- 442
- References
- 142
- Citations by year
- 2026: 9 · 2025: 16 · 2024: 27 · 2023: 27 · 2022: 23 · 2021: 24 · 2020: 24 · 2019: 28 · 2018: 19 · 2017: 22 · 2016: 19 · 2015: 23 · 2014: 28 · 2013: 33 · 2012: 22
- FWCI
- 2.00
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Immunological Reviews (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Heart, Lung, and Blood Institute (HL024136, P01HL024136)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Mast cells and histamine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Health Sciences › Medicine › Physiology › Asthma and respiratory diseases
- Keywords
- mast cells, tryptase, chymase, serine protease, prostasin, cathepsin G, protease inhibitors, proteoglycans, protease-activated receptors, urokinase, matrix metalloproteinases, angiotensin, intestinal worm infection, allergen inactivation, neuropeptide inactivation, inflammation, tissue remodeling, host defense
- MeSH terms
- Animals, Humans, Inflammation, Mast Cells, Serine Endopeptidases, Tryptases, Chymases
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