Cited by 988Antimicrobial Peptides and ActivitiesS100 Proteins and AnnexinsImmune Response and Inflammation

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Cathelicidins, multifunctional peptides of the innate immunity

Zanetti, Margherita·2004·Journal of Leukocyte Biology

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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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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
DOI: 10.1189/jlb.0403147
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
Licence: academic.oup.com/pages/standard-publication-reuse-rights (vor)
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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Cathelicidins, multifunctional peptides of the innate immunity

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