Evidence map›Paper›PMID 21079042›Full record

ReviewPharmacological reviews2010

Neutrophil elastase, proteinase 3, and cathepsin G as therapeutic targets in human diseases.

Brice Korkmaz, Marshall S Horwitz, Dieter E Jenne, Francis Gauthier

Open access · greenAbstract readReview
In one paragraph

Review in Pharmacological reviews, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 442 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
442citing papers in PubMed, 1 pooled it
16.9field-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

442 citing papers in PubMed, 1 synthesis or guideline pooled it, 833 citations in OpenAlex.

  1. Role of Neutrophils on the Ocular Surface.International journal of molecular sciences · 2021
    Pooled it
  2. Trial
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  5. The dipeptidyl peptidase 1 inhibition landscape in bronchiectasis and its future direction.European respiratory review : an official journal of the European Respiratory Society · 2026
    Review
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  19. Stage-Specific Proteomic Profiles in Dental Caries.Journal of dental research · 2026
    Article
  20. Neutrophil extracellular traps (NETosis) in gynecologic cancers: from pathogenesis to therapeutic opportunities: a narrative review.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2026
    Review

382 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

4 authors at 3 institutions in 3 countries.

Brice KorkmazINSERM U-618 Protéases et Vectorisation Pulmonaires, Université François Rabelais, Faculté de médecine, 10 Boulevard Tonnellé, Tours, France. brice.korkmaz@inserm.fr
Marshall S Horwitz
Dieter E Jenne
Francis Gauthier
University of Washington · USInserm · FRUniversité de Tours · FR

Funding

MOLECULAR GENETIC BASIS OF CYCLIC HEMATOPOIESISR01DK058161 · NIDDK · UNIVERSITY OF WASHINGTON · PI HORWITZ, MARSHALL S. · 2000 to 2011
$3.8M
NIDDK NIH HHS R01 DK058161NIDDK NIH HHS R01-DK58161
6 · The paper itself

Abstract

Polymorphonuclear neutrophils are the first cells recruited to inflammatory sites and form the earliest line of defense against invading microorganisms. Neutrophil elastase, proteinase 3, and cathepsin G are three hematopoietic serine proteases stored in large quantities in neutrophil cytoplasmic azurophilic granules. They act in combination with reactive oxygen species to help degrade engulfed microorganisms inside phagolysosomes. These proteases are also externalized in an active form during neutrophil activation at inflammatory sites, thus contributing to the regulation of inflammatory and immune responses. As multifunctional proteases, they also play a regulatory role in noninfectious inflammatory diseases. Mutations in the ELA2/ELANE gene, encoding neutrophil elastase, are the cause of human congenital neutropenia. Neutrophil membrane-bound proteinase 3 serves as an autoantigen in Wegener granulomatosis, a systemic autoimmune vasculitis. All three proteases are affected by mutations of the gene (CTSC) encoding dipeptidyl peptidase I, a protease required for activation of their proform before storage in cytoplasmic granules. Mutations of CTSC cause Papillon-Lefèvre syndrome. Because of their roles in host defense and disease, elastase, proteinase 3, and cathepsin G are of interest as potential therapeutic targets. In this review, we describe the physicochemical functions of these proteases, toward a goal of better delineating their role in human diseases and identifying new therapeutic strategies based on the modulation of their bioavailability and activity. We also describe how nonhuman primate experimental models could assist with testing the efficacy of proposed therapeutic strategies.

Indexed as

Molecular Targeted TherapyAnimalsCatalytic DomainCathepsin GHumansLeukocyte ElastaseLung DiseasesMyeloblastinNeutropeniaPapillon-Lefevre DiseaseCathepsin GLeukocyte ElastaseMyeloblastin

Identifiers

PMID21079042
PMCPMC2993259
OpenAlexW2137522692

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.