Broad spectrum antibiotic activity of skin‐PYY

Vouldoukis, Ioannis; Shai, Yechiel; Nicolas, Pierre; Mor, Amram

doi:10.1016/0014-5793(96)00050-6

Cited by 74 publications

(50 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…It has been shown to have antifungal properties, e.g. against Candida albicans [27], and more recently against E. coli [28]. Lysozyme was originally identified in mucosal secretions and is present in Bowman s glands and OECs in the lamina propria of the olfactory region [8,29].…”

Section: Discussionmentioning

confidence: 99%

Olfactory ensheathing cells are attracted to, and can endocytose, bacteria

Leung

Chapman

Harris

et al. 2008

Cell. Mol. Life Sci.

View full text Add to dashboard Cite

Abstract. Olfactory ensheathing cells (OECs) have been shown previously to express Toll-like receptors and to respond to bacteria by translocating nuclear factor-kB from the cytoplasm to the nucleus. In this study, we show that OECs extended significantly more pseudopodia when they were exposed to Escherichia coli than in the absence of bacteria (p=0.019). Coimmunoprecipitation showed that E. coli binding to OECs was mediated by Toll-like receptor 4. LysoTracker, a fluorescent probe that accumulates selectively in lysosomes, and staining for type 1 lysosomeassociated membrane proteins demonstrated that endocytosed FITC-conjugated E. coli were translocated to lysosomes. They appeared to be subsequently broken down, as shown by transmission electron microscopy. No obvious adherence to the membrane and less phagocytosis was observed when OECs were incubated with inert fluorescent microspheres. The ability of OECs to endocytose bacteria supports the notion that OECs play an innate immune function by protecting olfactory tissues from bacterial infection.

show abstract

Section: Discussionmentioning

confidence: 99%

Olfactory ensheathing cells are attracted to, and can endocytose, bacteria

Leung

Chapman

Harris

et al. 2008

Cell. Mol. Life Sci.

View full text Add to dashboard Cite

show abstract

“…They are found to mediate chemotaxis (defensins, LL-37) (6 -8), apoptosis (lactoferricin, LL-37) (9 -11), and angiogenesis (PR-39, LL-37) (12,13). Conversely, molecules previously not considered as AMPs, including proinflammatory and chemotactic chemokines (14), neuropeptides (15)(16)(17)(18)(19), and peptide hormones (16,20), have recently been found to exert antibacterial activities. The proinflammatory, chemotactic, and anaphylatoxic peptide C3a, generated during activation of the complement system, displays potent antibacterial effects (21).…”

mentioning

confidence: 99%

Domain 5 of High Molecular Weight Kininogen Is Antibacterial

Nordahl

Rydengård

Mörgelin

et al. 2005

Journal of Biological Chemistry

102

View full text Add to dashboard Cite

Antimicrobial peptides are important effectors of the innate immune system. These peptides belong to a multifunctional group of molecules that apart from their antibacterial activities also interact with mammalian cells and glycosaminoglycans and control chemotaxis, apoptosis, and angiogenesis. Here we demonstrate a novel antimicrobial activity of the heparin-binding and cell-binding domain 5 of high molecular weight kininogen. Antimicrobial epitopes of domain 5 were characterized by analysis of overlapping peptides. A peptide, HKH20 (His 479 -His 498 ), efficiently killed the Gram-negative bacteria Escherichia coli and Pseudomonas aeruginosa and the Gram-positive Enterococcus faecalis. Fluorescence microscopy and electron microscopy demonstrated that HKH20 binds to and induces breaks in bacterial membranes. Furthermore, no discernible hemolysis or membrane-permeabilizing effects on eukaryotic cells were noted. Proteolytic degradation of high molecular weight kininogen by neutrophil-derived proteases as well as the metalloproteinase elastase from P. aeruginosa yielded fragments comprising HKH20 epitopes, indicating that kininogen-derived antibacterial peptides are released during proteolysis.The innate immune system, based on antimicrobial peptides (AMP), 2 provides a rapid and nonspecific response against potentially invasive pathogenic microorganisms. AMPs, first isolated from human leukocyte extracts by Zeya and Spitznagel in 1963 (1), were subsequently discovered in invertebrates (2) and cold-blooded vertebrates (3). At present, over 880 different AMPs have been identified in eukaryotes. During recent years it has become increasingly evident that many antimicrobial peptides are multifunctional (4, 5). They are found to mediate chemotaxis (defensins, LL-37) (6 -8), apoptosis (lactoferricin, LL-37) (9 -11), and angiogenesis (PR-39, LL-37) (12, 13). Conversely, molecules previously not considered as AMPs, including proinflammatory and chemotactic chemokines (14), neuropeptides (15-19), and peptide hormones (16,20), have recently been found to exert antibacterial activities. The proinflammatory, chemotactic, and anaphylatoxic peptide C3a, generated during activation of the complement system, displays potent antibacterial effects (21). Many AMPs, by virtue of their cationicity and amphipathicity, also interact with heparin (22, 23).High molecular weight kininogen (HMWK) is a multifunctional 120-kDa glycoprotein found in plasma (ϳ80 g/ml) (24) and in ␣-granules of platelets (25). The protein is composed of six domains, each having different properties and specific ligands (24). Domains D1-D3 have a cystatin-like structure, and the two latter domains serve as specific inhibitors of cysteine proteinases such as cathepsins and calpains. The D4 domain contains the bradykinin sequence, which is released by plasma kallikreins during contact activation (24, 26). Biologically active kinins can also be generated by the cooperative action of mast cell tryptase and neutrophil elastase (27). Thus, similar to complement degrad...

show abstract

“…Some of them, such as ␣-helical dermaseptins (10,12), temporins (24), and SPYY (31), have been successfully assayed with Leishmania promastigotes.…”

mentioning

confidence: 99%