Evidence map›Paper›PMID 7593196›Full record

ArticleThe Journal of cell biology1995

Cell surface-bound elastase and cathepsin G on human neutrophils: a novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases.

C A Owen, M A Campbell, P L Sannes, S S Boukedes, E J Campbell

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
123citing papers in PubMed, 1 pooled it
5.5field-weighted citation impact, top 3% 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

123 citing papers in PubMed, 1 synthesis or guideline pooled it, 383 citations in OpenAlex.

  1. Neutrophil elastase in bronchiectasis.Respiratory research · 2017
    Pooled it
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Targeting neutrophil serine proteases in bronchiectasis.The European respiratory journal · 2025
    Review
  10. Review
  11. Article
  12. Neutrophil serine proteases in cystic fibrosis: role in disease pathogenesis and rationale as a therapeutic target.European respiratory review : an official journal of the European Respiratory Society · 2024
    Review
  13. Review
  14. Article
  15. Review
  16. Acute Inflammation in Tissue Healing.International journal of molecular sciences · 2022
    Review
  17. Article
  18. Article
  19. Review
  20. Article

63 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

5 authors at 1 institution in 1 country.

C A OwenDepartment of Medicine, University of Utah Health Sciences Center, Salt Lake City 84132, USA.
M A Campbell
P L Sannes
S S Boukedes
E J Campbell
University of Utah · US

Funding

ALVEOLAR BASEMENT MEMBRANE/CELL INTERACTIONS IN THE LUNGR01HL044497 · NHLBI · NORTH CAROLINA STATE UNIVERSITY RALEIGH · PI SANNES, PHILIP L. · 1992 to 2013
$3.7M
Alveolar Basement Membrane/Cell Interactions in the LungR56HL044497 · NHLBI · NORTH CAROLINA STATE UNIVERSITY RALEIGH · PI SANNES, PHILIP L. · 2008 to 2008
$371k
LOCALIZED PROTEOLYSIS IN PULMONARY INFLAMMATIONR01HL046440 · NHLBI · UNIVERSITY OF UTAH · PI CAMPBELL, EDWARD J · 1991 to 2000
$251k
NHLBI NIH HHS HL24748NHLBI NIH HHS HL44497NHLBI NIH HHS HL46440
6 · The paper itself

Abstract

Serine proteinases of human polymorphonuclear neutrophils play an important role in neutrophil-mediated proteolytic events; however, the non-oxidative mechanisms by which the cells can degrade extracellular matrix in the presence of proteinase inhibitors have not been elucidated. Herein, we provide the first report that human neutrophils express persistently active cell surface-bound human leukocyte elastase and cathepsin G on their cell surface. Unstimulated neutrophils have minimal cell surface expression of these enzymes; however, phorbol ester induces a 30-fold increase. While exposure of neutrophils to chemoattractants (fMLP and C5a) stimulates modest (two- to threefold) increases in cell surface expression of serine proteinases, priming with concentrations of lipopolysaccharide as low as 100 fg/ml leads to striking (up to 10-fold) increase in chemoattractant-induced cell surface expression, even in the presence of serum proteins. LPS-primed and fMLP-stimulated neutrophils have approximately 100 ng of cell surface human leukocyte elastase activity per 10(6) cells. Cell surface-bound human leukocyte elastase is catalytically active, yet is remarkably resistant to inhibition by naturally occurring proteinase inhibitors. These data indicate that binding of serine proteinases to the cell surface focuses and preserves their catalytic activity, even in the presence of proteinase inhibitors. Upregulated expression of persistently active cell surface-bound serine proteinases on activated neutrophils provides a novel mechanism to facilitate their egress from the vasculature, penetration of tissue barriers, and recruitment into sites of inflammation. Dysregulation of the cell surface expression of these enzymes has the potential to cause tissue destruction during inflammation.

Indexed as

Cathepsin GCathepsinsChemotactic FactorsEnzyme InhibitorsExtracellular MatrixHumansImmunohistochemistryLeukocyte ElastaseLipopolysaccharidesMembrane ProteinsMolecular WeightNeutrophilsOxidation-ReductionPancreatic ElastaseSerine EndopeptidasesCathepsin GCathepsinsChemotactic FactorsCTSG protein, humanEnzyme InhibitorsLeukocyte ElastaseLipopolysaccharidesMembrane ProteinsPancreatic ElastaseSerine Endopeptidases

Identifiers

PMID7593196
PMCPMC2120617
OpenAlexW2100266174

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.