Regulation of Proteolysis at the Neutrophil-Substrate Interface by Secretory Leukoprotease Inhibitor
Abstract
Human neutrophils can initiate the rapid degradation of extracellular matrix macromolecules by localizing the destructive process to sites of cell-substrate contact. Although plasma and its filtrates contain multiple proteinase inhibitors, these inhibitors did not prevent neutrophils from attacking either underlying fibronectin or elastin. However, subjacent substrates could be protected from neutrophils by recombinant secretory leukoprotease inhibitor, a structurally unique serine proteinase inhibitor whose natural counterpart is normally confined to human mucous secretions. The identification of this extravascular proteinase inhibitor as a potent regulator of subjacent proteolysis could lead to the development of a new class of anti-inflammatory therapeutics.
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HNE is targeted by reversible inhibitors including SLPI and elafin, and by the irreversible serpin A1AT, which predominately controls HNE activity in the lung.
“To ameliorate the hazards of unrestrained HNE activity, the enzyme is targeted by reversible inhibitors, including the secretory leukoprotease inhibitor (SLPI) [11], elafin [12], and the irreversible serpin inhibitor alpha 1 anti-trypsin (A1AT), which predominately controls HNE activity in the lung.”
From Discrimination of Methionine Sulfoxide and Sulfone by Human Neutrophil Elastase (2021) · cites this paper as [11]
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Discrimination of Methionine Sulfoxide and Sulfone by Human Neutrophil Elastase
Leahy, D., Grant, C., Jackson, A., Duff, A., Tardiota, N., Van Haeften, J., Chen, X., Peake, J. M., Kruppa, M. D., Smith, E. T., et al. (2021) · Molecules · doi:10.3390/molecules26175344 · Cited by 2 · see citing works
“To ameliorate the hazards of unrestrained HNE activity, the enzyme is targeted by reversible inhibitors, including the secretory leukoprotease inhibitor (SLPI) [11], elafin [12], and the irreversible serpin inhibitor alpha 1 anti-trypsin (A1AT), which predominately controls HNE activity in the lung.”
Background
- Authors
- Rice, W. G., & Weiss, S. J.
- Affiliations
- University of Michigan (US)
- Venue
- Science
- Published
- 1990-07-13
- Volume
- 249
- Issue
- 4965
- Pages
- 178-181
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1969254666
- Cited by
- 165
- References
- 0
- Citations by year
- 2024: 1 · 2022: 2 · 2021: 3 · 2020: 2 · 2019: 2 · 2018: 2 · 2017: 3 · 2016: 1 · 2015: 1 · 2013: 4
- FWCI
- 9.21
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (2r01hl028024-08)
- National Heart, Lung, and Blood Institute (HL-28024)
- National Institute of Allergy and Infectious Diseases (AI 21301)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Health Sciences › Medicine › Hematology › Blood Coagulation and Thrombosis Mechanisms
- Keywords
- secretory leukocyte protease inhibitor, neutrophils, extracellular matrix degradation, serine protease inhibitors, fibronectin, elastin, cell-substrate interface, proteolysis regulation, anti-inflammatory agents, mucus secretion
- MeSH terms
- Cell Adhesion, Cells, Cultured, Elastin, Extracellular Matrix, Fibronectins, Humans, Neutrophils, Proteins, Recombinant Proteins, Solubility, Serine Proteinase Inhibitors, Proteinase Inhibitory Proteins, Secretory
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