Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/5954
Title: Structural and Functional Consequences induced by post-translational modifications in α-Defensins
Authors: E., Balducci
A., Bonucci
M., Picchianti
Pogni, Rebecca 
E., Talluri
Issue Date: 2011
Project: None 
Journal: INTERNATIONAL JOURNAL OF PEPTIDES
Abstract: 
HNP-1 is an antimicrobial peptide that undergoes proteolytic cleavage to become a mature peptide. This process represents the mechanism commonly used by the cells to obtain a fully active antimicrobial peptide. In addition, it has been recently described that HNP-1 is recognized as substrate by the arginine-specific ADP-ribosyltransferase-1. Arginine-specific mono-ADPribosylation is an enzyme-catalyzed post-translational modification in which NAD+ serves as donor of the ADP-ribose moiety, which is transferred to the guanidino group of arginines in target proteins. While the arginine carries one positive charge, the ADP-ribose is negatively charged at the phosphate moieties at physiological pH. Therefore, the attachment of one or more ADPribose units results in amarked change of cationicity. ADP-ribosylation of HNP-1 drastically reduces its cytotoxic and antibacterial activities. While the chemotactic activity of HNP-1 remains unaltered, its ability to induce interleukin-8 production is enhanced. The arginine 14 of HNP-1 modified by the ADP-ribose is in some cases processed into ornithine, perhaps representing a different modality in the regulation of HNP-1 activities.
Description: 
19328
URI: http://hdl.handle.net/20.500.12779/5954
ISSN: 1687-9767
DOI: 10.1155/2011/594723
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