Evidence map›Paper›PMID 18178964›Full record

ArticleThe Journal of biological chemistry2008

Neutrophil elastase cleaves laminin-332 (laminin-5) generating peptides that are chemotactic for neutrophils.

Piotr Mydel, J Michael Shipley, Tracy L Adair-Kirk, Diane G Kelley, Thomas J Broekelmann, Robert P Mecham, Robert M Senior

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed, 1 pooled it
4.5field-weighted citation impact, top 5% 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

65 citing papers in PubMed, 1 synthesis or guideline pooled it, 113 citations in OpenAlex.

  1. Pooled it
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  5. Basement membranes in lung development, disease, and repair.Matrix biology : journal of the International Society for Matrix Biology · 2025
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5 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

7 authors at 2 institutions in 1 country.

Piotr MydelDepartment of Medicine, Division of Pulmonary and Critical Care Medicine, Washington University School of Medicine, 660 S. Euclid Avenue, St. Louis, MO 63110, USA.
J Michael Shipley
Tracy L Adair-Kirk
Diane G Kelley
Thomas J Broekelmann
Robert P Mecham
Robert M Senior
Pulmonary and Critical Care Associates · USWashington University in St. Louis · US

Funding

VASCULAR CELL DIVERSITY IN PULMONARY HYPERTENSIONP01HL029594 · NHLBI · WASHINGTON UNIVERSITY · PI HOLTZMAN, MICHAEL J · 1985 to 2012
$23.8M
NHLBI NIH HHS HL 29594
6 · The paper itself

Abstract

Proteolytic processing of laminin-332 by matrix metalloproteinase (MMP)-2 and MMP-14 has been shown to yield fragments that are promigratory for epithelial cells. During acute and chronic inflammation, proteases are elaborated by neutrophils and macrophages that can degrade basement membranes. We investigated the susceptibility of laminin-332 to degradation by the following neutrophil and macrophage proteases: neutrophil elastase (NE), cathepsin G, proteinase-3, and MMPs-2, -8, -9, and -12. Protease-specific differences were seen in the capacity to cleave the individual chains of laminin-332. NE and MMP-12 showed the greatest activity toward the gamma2 chain, generating a fragment similar in size to the gamma2x fragment generated by MMP-2. The digestion pattern of laminin-332 by degranulated neutrophils was nearly identical to that generated with NE alone. Digestion by supernatants of degranulated neutrophils was blocked by an inhibitor of NE, and NE-deficient neutrophils were essentially unable to digest laminin-332, suggesting that NE is the major neutrophil-derived protease that degrades laminin-332. In vivo, laminin gamma2 fragments were found in the bronchoalveolar lavage fluid of wild-type mice treated with lipopolysaccharide, whereas that obtained from NE-deficient mice showed a different cleavage pattern. In addition, NE cleaved a synthetic peptide derived from the region of human laminin gamma2 containing the MMP-2 cleavage site, suggesting that NE may generate laminin-332 fragments that are also promigratory. Both laminin-332 fragments generated by NE digestion and NE-digested laminin gamma2 peptide were found to be chemotactic for neutrophils. Collectively, these data suggest that degradation of laminin-332 by NE generates fragments with important biological activities.

Indexed as

AnimalsBronchoalveolar Lavage FluidCathepsin GCathepsinsCell Adhesion MoleculesCell DegranulationChemotactic FactorsHumansKalininLamininLeukocyte ElastaseLipopolysaccharidesMaleMatrix MetalloproteinasesMiceMice, KnockoutCathepsin GCathepsinsCell Adhesion MoleculesChemotactic FactorsCTSG protein, humanCtsg protein, mouseCtsg protein, ratKalininLAMC2 protein, humanLamininLeukocyte ElastaseLipopolysaccharidesMatrix MetalloproteinasesMyeloblastinPeptidesSerine Endopeptidases

Identifiers

PMID18178964
PMCPMC2442305
OpenAlexW2099328737

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.