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Cathelicidins, multifunctional peptides of the innate immunity
Author(s) -
Zanetti Margherita
Publication year - 2004
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1189/jlb.0403147
Subject(s) - cathelicidin , biology , innate immune system , antimicrobial peptides , chemotaxis , phagocyte , degranulation , microbiology and biotechnology , beta defensin , angiogenesis , zymosan , nadph oxidase , inflammation , immunology , antimicrobial , immune system , phagocytosis , biochemistry , cancer research , receptor , in vitro , reactive oxygen species
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.