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.
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|Titolo:||Structural and Functional Consequences induced by post-translational modifications in α-Defensins|
|Rivista:||INTERNATIONAL JOURNAL OF PEPTIDES|
|Citazione:||E., B., A., B., M., P., Pogni, R., & E., T. (2011). Structural and Functional Consequences induced by post-translational modifications in α-Defensins. INTERNATIONAL JOURNAL OF PEPTIDES, 2011, 1-7.|
|Appare nelle tipologie:||1.1 Articolo in rivista|