The DOI matches its Crossref record; 59 of the 59 references it cites were found in a registry or an index.
Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3
Abstract
Cathelicidins are a family of antimicrobial proteins found in the peroxidase-negative granules of neutrophils. The known biologic functions reside in the C-terminus, which must be cleaved from the holoprotein to become active. Bovine and porcine cathelicidins are cleaved by elastase from the azurophil granules to yield the active antimicrobial peptides. The aim of this study was to identify the physiological setting for cleavage of the only human cathelicidin, hCAP-18, to liberate the antibacterial and cytotoxic peptide LL-37 and to identify the protease responsible for this cleavage. Immunoelectron microscopy demonstrated that both hCAP-18 and azurophil granule proteins were present in the phagolysosome. Immunoblotting revealed no detectable cleavage of hCAP-18 in cells after phagocytosis. In contrast, hCAP-18 was cleaved to generate LL-37 in exocytosed material. Of the 3 known serine proteases from azurophil granules, proteinase 3 was solely responsible for cleavage of hCAP-18 after exocytosis. This is the first detailed study describing the generation of a human antimicrobial peptide from a promicrobicidal protein, and it demonstrates that the generation of active antimicrobial peptides from common proproteins occurs differently in related species.
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The antibacterial peptide LL-37 from humans has broad-spectrum antibacterial activity by increasing the membrane permeability of bacteria, neutralizing endotoxins, and suppressing the production of proinflammatory factors.
“The antibacterial peptide LL-37 from humans was found to have broad-spectrum antibacterial activity31–34 by increasing the membrane permeability of bacteria, neutralizing endotoxins, and suppressing the production of proinflammatory factors.35”
From Identification of heptapeptides targeting a lethal bacterial strain in septic mice through an integrative approach (2022) · cites this paper as [35]
Defensins, cathelizidin, and ubiquitin-derived AMPs require processing to their active components through proteolytic cleavage by PMN elastase, proteinase 3, or cathepsins.
“The two latter ones require processing to their active components through proteolytic cleavage by PMN elastase, proteinase 3, or cathepsins, respectively (37, 38).”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [37]
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“The antibacterial peptide LL-37 from humans was found to have broad-spectrum antibacterial activity by increasing the membrane permeability of bacteria, neutralizing endotoxins, and suppressing the production of proinflammatory factors.(35) For this reason, LL-37 is considered an ideal template or a molecular skeleton…”
Background
Metadata
- Authors
- Sørensen, O. E., Follin, P., Johnsen, A. H., Calafat, J., Tjabringa, G. S., Hiemstra, P. S., & Borregaard, N.
- Affiliations
- Linköping University (SE)
- Venue
- Blood
- Publisher
- American Society of Hematology
- Published
- 2001-06-15
- Volume
- 97
- Issue
- 12
- Pages
- 3951-3959
- ISSN
- 0006-4971 (ISSN-L)
- 1528-0020
- OpenAlex
- W2116558722
- Cited by
- 894
- References
- 59
- Citations by year
- 2026: 16 · 2025: 25 · 2024: 24 · 2023: 24 · 2022: 40 · 2021: 45 · 2020: 45 · 2019: 28 · 2018: 35 · 2017: 36 · 2016: 49 · 2015: 55 · 2014: 61 · 2013: 39 · 2012: 42
- FWCI
- 18.49
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Blood (publishedVersion)
- PubMed (publishedVersion)
- Lund University Publications (Lund University) (submittedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › S100 Proteins and Annexins
- Keywords
- LL-37, cathelicidin, antimicrobial peptides, proteinase 3, proteolytic cleavage, proprotein processing, phagolysosomes, exocytosis, neutrophils, serine protease
- MeSH terms
- Exocytosis, Humans, Microscopy, Electron, Neutrophils, Phagocytosis, Serine Endopeptidases, Immunoblotting, Antimicrobial Cationic Peptides, Myeloblastin, Cathelicidins
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