Characterization of Antibacterial COOH-terminal Proenkephalin-A-derived Peptides (PEAP) in Infectious Fluids

Goumon, Yannick; Lugardon, Karine; Kieffer, Bruno; Lefèvre, Jean‐François; Dorsselaer, Alain Van; Aunis, Dominique; Metz‐Boutigue, Marie‐Hélène

doi:10.1074/jbc.273.45.29847

Cited by 63 publications

(42 citation statements)

References 90 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…After lyophilization, synthetic peptides were analyzed by sequencing (7,15) and matrix-assisted laser desorption-ionization time-of-flight mass spectrometry (5,16,17). Chromofungin corresponds to the bovine CGA-(47-66) sequence RIL-SILRHQNLLKELQDLAL.…”

Section: Methodsmentioning

confidence: 99%

“…We have recently discovered new natural antimicrobial peptides derived from the processing of chromogranins A (CGA) 1 and B (CGB) and of proenkephalin-A, which are secreted with catecholamines upon stimulation of chromaffin cells in adrenal medulla (2)(3)(4)(5)(6)(7). These peptides have been hypothesized to play a role in stress situations, acting as an immediate protective shield against pathogens (6).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Structural and Biological Characterization of Chromofungin, the Antifungal Chromogranin A-(47–66)-derived Peptide

Lugardon¹,

Chasserot‐Golaz²,

Kieffer³

et al. 2001

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

In order to examine thoroughly the antifungal activity of chromofungin, confocal laser microscopy was used to demonstrate the ability of the rhodamine-labeled peptide to interact with the fungal cell wall, to cross the plasma membrane, and to accumulate in Aspergillus fumigatus, Alternaria brassicola, and Candida albicans. Our present data reveal that chromofungin inhibits calcineurin activity, extending a previous observation that the N-terminal region of chromogranin A interacts with calmodulin in the presence of calcium. Therefore, the destabilization of fungal wall and plasma membrane, together with the possible intracellular inhibition of calmodulin-dependent enzymes, is likely to represent the mechanism by which vasostatin-I and chromofungin exert antifungal activity.

show abstract

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

Structural and Biological Characterization of Chromofungin, the Antifungal Chromogranin A-(47–66)-derived Peptide

Lugardon¹,

Chasserot‐Golaz²,

Kieffer³

et al. 2001

Journal of Biological Chemistry

Self Cite

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

103

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

“…Glycosylated and phosphorylated CgA-derived peptide (bovine adrenal) show antibacterial activity (106) and CgB-derived peptide, secretolytin, also exhibits antibacterial activity (107). Further, the C terminal of proenkephalin-A-derived peptide possesses anti-bacterial potency (108). These antimicrobial activities in the granin derivatives of salivary glands and saliva are considered to act as part of a defense system for preventing oral mucosal infections.…”

Section: Chromograninmentioning

confidence: 99%

Antimicrobial Peptides in Saliva and Salivary Glands: Their Roles in the Oral Defense System

et al. 2006

View full text Add to dashboard Cite

Characterization of Antibacterial COOH-terminal Proenkephalin-A-derived Peptides (PEAP) in Infectious Fluids

Cited by 63 publications

References 90 publications

Structural and Biological Characterization of Chromofungin, the Antifungal Chromogranin A-(47–66)-derived Peptide

Structural and Biological Characterization of Chromofungin, the Antifungal Chromogranin A-(47–66)-derived Peptide

Domain 5 of High Molecular Weight Kininogen Is Antibacterial

Antimicrobial Peptides in Saliva and Salivary Glands: Their Roles in the Oral Defense System

Contact Info

Product

Resources

About