The DOI matches its Crossref record; 124 of the 126 references it cites were found in a registry or an index.
Cathelicidins, multifunctional peptides of the innate immunity
Abstract
Cathelicidins comprise a family of mammalian proteins containing a C-terminal cationic antimicrobial domain that becomes active after being freed from the N-terminal cathelin portion of the holoprotein. Many other members of this family have been identified since the first cathelicidin sequences were reported 10 years ago. The mature peptides generally show a wide spectrum of antimicrobial activity and, more recently, some of them have also been found to exert other biological activities. The human cathelicidin peptide LL-37 is chemotactic for neutrophils, monocytes, mast cells, and T cells; induces degranulation of mast cells; alters transcriptional responses in macrophages; stimulates wound vascularization and re-epithelialization of healing skin. The porcine PR-39 has also been involved in a variety of processes, including promotion of wound repair, induction of angiogenesis, neutrophils chemotaxis, and inhibition of the phagocyte NADPH oxidase activity, whereas the bovine BMAP-28 induces apoptosis in transformed cell lines and activated lymphocytes and may thus help with clearance of unwanted cells at inflammation sites. These multiple actions provide evidence for active participation of cathelicidin peptides in the regulation of the antimicrobial host defenses.
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“whereas sheep and cows have numerous genes that have been duplicated only recently 54”
From Genome analysis of the platypus reveals unique signatures of evolution (2008) · cites this paper as [54]
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Hancock, R. E. W., & Diamond, G. (2000) · Trends in Microbiology · doi:10.1016/s0966-842x(00)01823-0 · Cited by 1,233
Innate antimicrobial peptide protects the skin from invasive bacterial infection
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2 of the 126 references couldn’t be matched to a known paper.
Research works printed but not linked: 2
- Strukelj, 1995, Molecular cloning and identification of a novel porcine cathelin-like antibacterial peptide precursor, Biol. Chem. Hoppe Seyler, 376, 507
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Jenssen, H., Hamill, P., & Hancock, R. E. W. (2006) · Clinical Microbiology Reviews · doi:10.1128/cmr.00056-05 · Cited by 2,605
Plasmacytoid dendritic cells sense self-DNA coupled with antimicrobial peptide
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Antimicrobial host defence peptides: functions and clinical potential
Mookherjee, N., Anderson, M. A., Haagsman, H. P., & Davidson, D. J. (2020) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0058-8 · Cited by 1,502
Metadata
- Authors
- Zanetti, M.
- Affiliations
- University of Udine (IT)
- Corresponding author
- Zanetti, Margherita
- Venue
- Journal of Leukocyte Biology
- Publisher
- Oxford University Press (OUP)
- Published
- 2003-07-22
- Volume
- 75
- Issue
- 1
- Pages
- 39-48
- ISSN
- 0741-5400 (ISSN-L)
- 1938-3673
- OpenAlex
- W1983987058
- Cited by
- 988
- References
- 126
- Citations by year
- 2026: 14 · 2025: 16 · 2024: 38 · 2023: 27 · 2022: 42 · 2021: 35 · 2020: 51 · 2019: 42 · 2018: 51 · 2017: 35 · 2016: 49 · 2015: 48 · 2014: 58 · 2013: 61 · 2012: 44
- FWCI
- 4.97
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Leukocyte Biology (publishedVersion)
- PubMed (publishedVersion)
- Institutional Research Information System (University of Udine) (submittedVersion)
- Funders
- Dept. Biochemistry of the University of Trieste
- Dept. Biomedical Sciences and Technology of the University of Udine
- Italian Ministry for University and Research (P.R.I.N. Cofin. 2000 and 2002)
- CNR (Agenzia 2000)
- Topics
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › S100 Proteins and Annexins
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- cathelicidin, innate immunity, antimicrobial peptides, LL-37, PR-39, neutrophil chemotaxis, mast cell degranulation, angiogenesis, wound healing, apoptosis, NADPH oxidase inhibition
- MeSH terms
- Animals, Blood Proteins, Cattle, Chemotaxis, Leukocyte, Humans, Immunity, Innate, Macrophages, Protein Precursors, Proteins, T-Lymphocytes, Antimicrobial Cationic Peptides
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