The DOI matches its Crossref record; 46 of the 50 references it cites were found in a registry or an index.
Cathelicidin family of antimicrobial peptides: proteolytic processing and protease resistance
Abstract
Cathelicidins are a gene family of antimicrobial peptides produced as inactive precursors. Signal peptidase removes the N-terminal signal sequence, while peptidylglycine alpha-amidating monooxygenase often amidates and cleaves the C-terminal region. Removal of the cathelin domain liberates the active antimicrobial peptide. For mammalian sequences, this cleavage usually occurs through the action of elastase, but other tissue-specific processing enzymes may also operate. Once released, these bioactive peptides are susceptible to proteolytic degradation. We propose that some mature cathelicidins are naturally resistant to proteases due to their unusual primary structures. Among mammalian cathelicidins, proline-rich sequences should resist attack by serine proteases because proline prevents cleavage of the scissile bond. In hagfish cathelicidins, the unusual amino acid bromotryptophan may make the active peptides less susceptible to proteolysis for steric reasons. Such protease resistance could extend the pharmacokinetic lifetimes of cathelicidins in vivo, sustaining antimicrobial activity.
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In the citing paper
“Cathelicidins rapidly destroy lipoprotein membranes of microbes enveloped in phagosomes after fusion with lysosomes in macrophages [179,180].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [180]
In the citing paper
“The cathelicidins family shares primary sequence homology with the cystatins, of the cysteine proteinase inhibitor family, although amino acid residues considered important in these cystatins are often missing [180,181].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [180]
Citations
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Research works printed but not linked: 5
- Gennaro, 2000, Biopolymers (Peptide Science), 55, 31, 10.1002/1097-0282(2000)55:1<31::AID-BIP40>3.0.CO;2-9 · DOI
- Shinnar, 2000, FASEB, 14, A1488
- K. Curran, Bromotryptophan: biochemical and biophysical properties of an unusual amino acid in antimicrobial peptides isolated from hagfish, Senior honors thesis, Department of Chemistry, Barnard College, New York, NY, 2002
- H.J. Park, Biological role and physical properties of bromotryptophan in hagfish intestinal antimicrobial peptides, Senior honors thesis, Department of Chemistry, Barnard College, New York, NY, 2003
- Chen, 2000, Biopolymers (Peptide Science), 55, 88, 10.1002/1097-0282(2000)55:1<88::AID-BIP80>3.0.CO;2-K · DOI
Cited by
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Bahar, A. A., & Ren, D. (2013) · Pharmaceuticals · doi:10.3390/ph6121543 · Cited by 1,452
Liévin-Le Moal, V., & Servin, A. L. (2006) · Clinical Microbiology Reviews · doi:10.1128/cmr.19.2.315-337.2006 · Cited by 568
Degradation of Human Antimicrobial Peptide LL-37 by Staphylococcus aureus -Derived Proteinases
Sieprawska‐Lupa, M., Mydel, P. M., Krawczyk, K., Wójcik, K., Puklo, M., Lupa, B., Suder, P., Silberring, J., Reed, M. S., Pohl, J., et al. (2004) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.48.12.4673-4679.2004 · Cited by 567
The human cathelicidin LL-37 — A pore-forming antibacterial peptide and host-cell modulator
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Antimicrobial Peptides from Fish
Masso-Silva, J. A., & Diamond, G. (2014) · Pharmaceuticals · doi:10.3390/ph7030265 · Cited by 358
Metadata
- Authors
- Shinnar, A. E., Butler, K. L., & Park, H. J.
- Affiliations
- Columbia University (US)
- Corresponding author
- Shinnar, Ann Eisenberg
- Venue
- Bioorganic Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-12
- Volume
- 31
- Issue
- 6
- Pages
- 425-436
- ISSN
- 0045-2068 (ISSN-L)
- OpenAlex
- W1966733674
- Cited by
- 170
- References
- 50
- Citations by year
- 2026: 5 · 2025: 6 · 2024: 12 · 2023: 11 · 2022: 3 · 2021: 9 · 2020: 5 · 2019: 6 · 2018: 8 · 2017: 5 · 2016: 9 · 2015: 11 · 2014: 14 · 2013: 10 · 2012: 4
- FWCI
- 3.87
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Bioorganic Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Life Sciences › Immunology and Microbiology › Applied Microbiology and Biotechnology › Antimicrobial agents and applications
- Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
- Keywords
- cathelicidin, antimicrobial peptides, proteolytic processing, protease resistance, signal peptidase, peptidylglycine alpha-amidating monooxygenase, proline-rich sequences, serine protease, pharmacokinetics
- MeSH terms
- Amino Acid Sequence, Animals, Arginine, Binding Sites, Multigene Family, Hagfishes, Humans, Mixed Function Oxygenases, Molecular Sequence Data, Multienzyme Complexes, Endopeptidases, Proline, Proteins, Tryptophan, Cysteine Proteinase Inhibitors, Sequence Homology, Amino Acid, Protein Sorting Signals, Antimicrobial Cationic Peptides, Cathelicidins
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