Cathelicidins, multifunctional peptides of the innate immunity

Clicks: 4
ID: 299358
2003
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Abstract
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.
Reference Key
openalex_W1983987058 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Margherita Zanetti
Journal journal of leukocyte biology
Year 2003
DOI
10.1189/jlb.0403147
URL
https://doi.org/10.1189/jlb.0403147
Keywords Keywords not found

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