Evidence map›Paper›PMID 17498057›Full record

ReviewImmunological reviews2007

Mast cell tryptases and chymases in inflammation and host defense.

George H Caughey

Open access · greenAbstract readReview
In one paragraph

Review in Immunological reviews, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 201 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
201citing papers in PubMed, 1 pooled it
8.1field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

201 citing papers in PubMed, 1 synthesis or guideline pooled it, 440 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. The role of myeloid immune cells in lung epithelial repair.American journal of physiology. Lung cellular and molecular physiology · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Interactions Between Tryptase-Positive Mast Cells and Melanin-AInternational journal of molecular sciences · 2025
    Article
  14. Article
  15. Role of Mast Cells and Their Mediators in Chronic Kidney Diseases.International journal of molecular sciences · 2025
    Review
  16. Review
  17. Mast cells promote pathology and susceptibility in tuberculosis.bioRxiv : the preprint server for biology · 2025
    Article
  18. Bidirectional Interplay Between Microglia and Mast Cells.International journal of molecular sciences · 2025
    Review
  19. Article
  20. Article

141 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

George H CaugheyCardiovascular Research Institute, University of California at San Francisco, San Francisco, CA, USA. george.caughey@ucsf.edu
San Francisco VA Medical Center · US

Funding

Tools for Analysis of Airway InflammationP01HL024136 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MCDONALD, DONALD M · 1985 to 2014
$23.3M
NHLBI NIH HHS HL024136NHLBI NIH HHS P01 HL024136
6 · The paper itself

Abstract

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.

Indexed as

AnimalsChymasesHumansInflammationMast CellsSerine EndopeptidasesTryptasesChymasesSerine EndopeptidasesTryptases

Identifiers

PMID17498057
PMCPMC2275918
OpenAlexW1993305093

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.