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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Yang, D., Chen, Q., Schmidt, A. P., Anderson, G. M., Wang, J., Wooters, J., Oppenheim, J. J., & Chertov, O. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.192.7.1069 · Cited by 1,238
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Bernfield, M. R., Kokenyesi, R., Kato, M., Hinkes, M. T., Spring, J., Gallo, R. L., & Lose, E. J. (1992) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.08.110192.002053 · Cited by 1,099
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Strukelj, 1995, Molecular cloning and identification of a novel porcine cathelin-like antibacterial peptide precursor, Biol. Chem. Hoppe Seyler, 376, 507
Larrick, 1995, Human CAP18: a novel antimicrobial lipopolysaccharide-binding protein, Infect. Immun., 63, 1291, 10.1128/iai.63.4.1291-1297.1995 · DOI

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Zarember, K. A. (2005) · Journal of Clinical Investigation · doi:10.1172/jci25740 · Cited by 109
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The protein and lipid composition of the membrane of milk fat globules depends on their size
Lu, J., Argov-Argaman, N., Anggrek, J., Boeren, S. A., van Hooijdonk, T., Vervoort, J. J. M., & Hettinga, K. A. (2016) · Journal of Dairy Science · doi:10.3168/jds.2015-10375 · Cited by 104
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Mookherjee, N., Hamill, P., Gardy, J. L., Blimkie, D., Falsafi, R., Chikatamarla, A., Arenillas, D. J., Doria, S., Kollmann, T. R., & Hancock, R. E. W. (2009) · Molecular BioSystems · doi:10.1039/b813787k · Cited by 110
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Linde, A., Ross, C. R., Davis, E. G., Dib, L. H., Blecha, F., & Melgarejo, T. (2008) · Journal of Veterinary Internal Medicine · doi:10.1111/j.1939-1676.2007.0038.x · Cited by 100
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Harder, J., Gläser, R., & Schröder, J. (2007) · Journal of Endotoxin Research · doi:10.1177/0968051907088275 · Cited by 101
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Wolf, M., & Moser, B. (2012) · Frontiers in Immunology · doi:10.3389/fimmu.2012.00213 · Cited by 96
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da Silva, B. R., de Freitas, V. A. A., Neto, L. G. D. N., Carneiro, V. A., Arruda, F. V. S., de Aguiar, A. S. W., Cavada, B. S., & Teixeira, E. H. (2012) · Peptides · doi:10.1016/j.peptides.2012.05.015 · Cited by 101
Innate immunity to mycobacteria: vitamin D and autophagy
Jo, E.-K. (2010) · Cellular Microbiology · doi:10.1111/j.1462-5822.2010.01491.x · Cited by 98
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Iba, T., Hashiguchi, N., Nagaoka, I., Tabe, Y., & Murai, M. (2013) · Journal of Intensive Care · doi:10.1186/2052-0492-1-13 · Cited by 101
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Karczewski, J., Dobrowolska, A., Rychlewska-Hańczewska, A., & Adamski, Z. (2016) · Autoimmunity · doi:10.3109/08916934.2016.1166214 · Cited by 96
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Garcia, A., Ösapay, G., Tran, P. A., Yuan, J. J., & Selsted, M. E. (2008) · Infection and Immunity · doi:10.1128/iai.01100-08 · Cited by 96
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SHAH, P. M., Hsiao, F. S., Ho, Y.-H., & Chen, C. (2015) · PROTEOMICS · doi:10.1002/pmic.201500380 · Cited by 102
Quantitative proteomic analysis of milk fat globule membrane (MFGM) proteins in human and bovine colostrum and mature milk samples through iTRAQ labeling
Yang, M., Cong, M., Peng, X., Wu, J., Wu, R., Liu, B., Ye, W., & Yue, X. (2016) · Food & Function · doi:10.1039/c6fo00083e · Cited by 96
Immunosenescence and Influenza Vaccine Efficacy
Sambhara, S. R., & McElhaney, J. E. (2009) · Current topics in microbiology and immunology · doi:10.1007/978-3-540-92165-3_20 · Cited by 98

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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