Elafin: an elastase-specific inhibitor of human skin. Purification, characterization, and complete amino acid sequence.
Open accessAbstract
A potent inhibitor of human leukocyte elastase (EC 3.4.21.37) and porcine pancreatic elastase (EC 3.4.21.36) was purified to homogeneity from human horny layers. It inhibits human leukocyte elastase and porcine pancreatic elastase in a 1:1 molar ratio and shows equilibrium dissociation constants of 6 x 10(-10) M and 1 x 10(-9) M, respectively. Inhibition of plasmin, trypsin, alpha-chymotrypsin, and cathepsin G was not observed. This inhibitor proved to be an acid stable basic peptide with an isoelectric point of 9.7. The complete amino acid sequence appears to be unique with 38% homology to the C-terminal half of antileukoprotease. The sequence shows that the inhibitor is composed of 57 amino acids and predicts a Mr of 7017. The high affinity as well as the apparent specificity for elastases suggests a functional role in preventing elastase-mediated tissue proteolysis. It is suggested that the term "elafin" be used to designate this inhibitor.
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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 [12]
Cites
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Aggregated neutrophil extracellular traps limit inflammation by degrading cytokines and chemokines
Schauer, C., Janko, C., Munoz, L. E., Zhao, Y., Kienhöfer, D., Frey, B., Lell, M., Manger, B., Rech, J., Naschberger, E., et al. (2014) · Nature Medicine · doi:10.1038/nm.3547 · Cited by 998 · see citing works
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Food-Grade Bacteria Expressing Elafin Protect Against Inflammation and Restore Colon Homeostasis
Motta, J.-P., Bermúdez-Humarán, L. G., Deraison, C., Martin, L., Rolland, C., Rousset, P., Boue, J., Dietrich, G., Chapman, K., Kharrat, P., et al. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3004212 · Cited by 257 · see citing works
Plasma proteomic biomarker signature of age predicts health and life span
Tanaka, T., Basisty, N., Fantoni, G., Candia, J., Moore, A. Z., Biancotto, A., Schilling, B., Bandinelli, S., & Ferrucci, L. (2020) · eLife · doi:10.7554/elife.61073 · Cited by 213 · see citing works
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
- Wiedow, O., Schröder, J. M., Gregory, H., Young, J. A., & Christophers, E.
- Affiliations
- Christian-Albrechts-Universität zu Kiel (DE)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1990-09
- Volume
- 265
- Issue
- 25
- Pages
- 14791-14795
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1627442108
- Cited by
- 433
- References
- 1
- Citations by year
- 2026: 5 · 2025: 8 · 2024: 3 · 2023: 9 · 2022: 7 · 2021: 5 · 2020: 8 · 2019: 8 · 2018: 5 · 2017: 16 · 2016: 9 · 2015: 8 · 2014: 12 · 2013: 8 · 2012: 19
- FWCI
- 7.28
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Calpain Protease Function and Regulation
- Health Sciences › Medicine › Oncology › Peptidase Inhibition and Analysis
- Keywords
- elafin, elastase inhibitors, neutrophil elastase, porcine pancreatic elastase, skin, amino acid sequence, peptide purification, protease inhibition, tissue proteolysis
- MeSH terms
- Amino Acid Sequence, Chromatography, Gel, Electrophoresis, Polyacrylamide Gel, Humans, Leukocytes, Molecular Sequence Data, Molecular Weight, Pancreatic Elastase, Proteins, Sequence Homology, Nucleic Acid, Skin, Serine Proteinase Inhibitors, Proteinase Inhibitory Proteins, Secretory
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