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An essential function of innate immunity is initiating inflammatory responses to limit the spread of invading pathogens, followed by regulatory mechanisms aimed at resolving inflammation and returning the immune system to homeostasis. These meticulously regulated processes are triggered by various pathogen-associated molecular patterns or endogenous damage-associated molecular patterns. A group of natural peptides that have gained notoriety in recent years as immune-modulatory molecules contributing to both resolution of infections and inflammation, thus playing a role in maintaining homeostasis are host defense peptides (HDPs). These are gene-encoded cationic short peptides, less than 50 amino acids with an overall positive charge of +2 to +7, and ≥30% of hydrophobic residues. The two most well characterized families of HDPs in mammals are cathelicidins and defensins. We will focus on cathelicidin HDPs in this review.  Genes encoding cathelicidin HDPs have a highly conserved N-terminal cathelin domain in their precursor protein (Tomasinsig and Zanetti, 2005). This conserved cathelin domain has helped in the discovery of new cathelicidins from diverse species including non-mammalian species such as chicken, trout, and hagfish. The biological active mature mammalian cathelicidin peptides are processed from their precursor protein by proteolytic cleavage by serine proteases, e.g., proteinase 3, elastase, and kallikrein (Shinnar et al., 2003; Morizane et al., 2010). The biologically active mature cathelicidins are diverse in their sequence and structure, and can be classified into four structural groups; amphipathic α-helices (e.g., murine CRAMP), β-hairpin molecules (e.g., porcine protegrin 1), those with extended structures (e.g., bovine indolicidin), and cyclic peptides (e.g., bactenecin). Mammalian cathelicidins are found in granules of neutrophils as well as other cell types such as myeloid precursors, epithelial cells, mast cells, lymphocytes, and keratinocytes. These peptides are expressed in a wide variety of tissues (oral cavity, skin, intestine, lungs, cervix, etc.) and found in body fluids such as plasma, breast milk, saliva, gastric juice, semen, sweat, and bronchoalveolar fluid (Nijnik and Hancock, 2009). The biologically active mature cathelicidin peptides have been demonstrated to mediate a wide range of activity from antimicrobial to immune-modulatory (discussed below). Some of the most well studied cathelicidins are human LL-37, murine CRAMP, bovine BMAP-28, and porcine PR-39.

Multiple Immune-Modulatory Functions Of Cathelicidin Host Defense Peptides