Evidence map›Paper›PMID 21713659›Full record

ReviewAdvances in experimental medicine and biology2011

Mast cell proteases as protective and inflammatory mediators.

George H Caughey

Abstract readReview
In one paragraph

Review in Advances in experimental medicine and biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
21.9field-weighted citation impact, top 1% 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

80 citing papers in PubMed, 160 citations in OpenAlex.

  1. Trial
  2. Review
  3. Hereditary alpha tryptasemia and clinical implications.World journal of clinical cases · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Sex Difference in the Effect ofJournal of cancer prevention · 2024
    Article
  8. Article
  9. The Protective Effect ofJournal of cancer prevention · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Do mast cells contribute to the continued survival of vertebrates?APMIS : acta pathologica, microbiologica, et immunologica Scandinavica · 2022
    Review
  14. Article
  15. Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. Review

20 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 CaugheyDepartment of Medicine, University of California at San Francisco, San Francisco, Califonia, USA. george.caughey@ucsf.edu
University of California, San Francisco · US

Funding

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

Abstract

Proteases are the most abundant class of proteins produced by mast cells. Many of these are stored in membrane-enclosed intracellular granules until liberated by degranulating stimuli, which include cross-linking of high affinity IgE receptor F(c)εRI by IgE bound to multivalent allergen. Understanding and separating the functions of the proteases is important because expression differs among mast cells in different tissue locations. Differences between laboratory animals and humans in protease expression also influence the degree of confidence with which results obtained in animal models of mast cell function can be extrapolated to humans. The inflammatory potential of mast cell proteases was the first aspect of their biology to be explored and has received the most attention, in part because some of them, notably tryptases and chymases, are biomarkers of local and systemic mast cell degranulation and anaphylaxis. Although some of the proteases indeed augment allergic inflammation and are potential targets for inhibition to treat asthma and related allergic disorders, they are protective and even anti-inflammatory in some settings. For example, mast cell tryptases may protect from serious bacterial lung infections and may limit the "rubor" component of inflammation caused by vasodilating neuropeptides in the skin. Chymases help to maintain intestinal barrier function and to expel parasitic worms and may support blood pressure during anaphylaxis by generating angiotensin II. In other life-or-death examples, carboxypeptidase A3 and other mast cell peptidases limit systemic toxicity of endogenous peptideslike endothelin and neurotensin during septic peritonitis and inactivate venom-associated peptides. On the other hand, mast cell peptidase-mediated destruction of protective cytokines, like IL-6, can enhance mortality from sepsis. Peptidases released from mast cells also influence nonmast cell proteases, such as by activating matrix metalloproteinase cascades, which are important in responses to infection and resolution of tissue injury. Overall, mast cell proteases have a variety of roles, inflammatory and anti-inflammatory, protective and deleterious, in keeping with the increasingly well-appreciated contributions of mast cells in allergy, tissue homeostasis and innate immunity.

Indexed as

AnimalsHumansInflammation MediatorsMast CellsPeptide HydrolasesInflammation MediatorsPeptide Hydrolases

Identifiers

PMID21713659
PMCPMC3954859
OpenAlexW1937792941

What OpenQuestion holds

Textmetadata
LicenceTDM
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.