Molecular Characterization and Gene Expression Profiling ... - CUSAT

Chapter 1
number of excellent reviews have covered this large group of AMPs
(Simmaco et al., 1998; Rinaldi, 2002; Bulet et al., 2004).
Cathelicidins are a large and diverse group of vertebrate AMPs. Most
cathelicidins are stored in an inactive propeptide state, mostly within
granules of circulating immune cells. Neutrophil secretory granules are the
predominant source of cathelicidins, but they may also be expressed in
mucosal surfaces in the mouth, lung, and genitourinary tract and in skin
keratinocytes in inflammatory disorders (Frohm et al., 1997). Cathelicidins
have been isolated from many mammalian species, such as mice, rabbits,
sheep, horses, and humans.
One of the best characterized bovine AMPs is BMAP-28, an α-helical
peptide which rapidly permeabilizes the membranes of a broad spectrum of
bacteria and fungi at moderate concentrations in vitro (Skerlavaj et al., 1996).
In contrast, only one cathelicidin is expressed in humans: LL-37 (hCAP18). In
addition to direct microbicidal activity, LL-37 has important additional roles
in host defense, including chemotactic properties and modulation of
inflammatory responses (Zanetti, 2004; Bowdish et al., 2005b). A second
prominent group of mammalian AMPs is the defensins (Ganz, 2003) cyclic
peptides which are categorized into three subfamilies on the basis of the
disulfide pairings between their six conserved cysteine residues or their
macrocyclic nature. As with cathelicidins, vertebrate defensins are
synthesized as prepeptides which require proteolytic processing to their
active peptide forms (Tang et al., 1999). Depending on the species, defensins
are found in the granules of neutrophils, macrophages, NK cells, intestinal
Paneth cells and epithelial tissues, the skin, certain mucosal surfaces such as
the respiratory passage and urinogenital tract, and many bodily fluids (Fang
et al., 2003).
Molecular Characterization and Gene Expression Profiling of Antimicrobial Peptides in Penaeid Shrimps
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