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NAD-dependent ADP-ribosylation of the human antimicrobial and immune-modulatory peptide LL-37 by ADP-ribosyltransferase-1.
- Source :
-
Innate immunity [Innate Immun] 2015 Apr; Vol. 21 (3), pp. 314-21. Date of Electronic Publication: 2014 Aug 15. - Publication Year :
- 2015
-
Abstract
- LL-37 is a cationic peptide belonging to the cathelicidin family that has antimicrobial and immune-modulatory properties. Here we show that the mammalian mono-ADP-ribosyltransferase-1 (ART1), which selectively transfers the ADP-ribose moiety from NAD to arginine residues, ADP-ribosylates LL-37 in vitro. The incorporation of ADP-ribose was first observed by Western blot analysis and then confirmed by MALDI-TOF. Mass-spectrometry showed that up to four of the five arginine residues present in LL-37 could be ADP-ribosylated on the same peptide when incubated at a high NAD concentration in the presence of ART1. The attachment of negatively charged ADP-ribose moieties considerably alters the positive charge of the arginine residues thus reducing the cationicity of LL-37. The cationic nature of LL-37 is key for its ability to interact with cell membranes or negatively charged biomolecules, such as DNA, RNA, F-actin and glycosaminoglycans. Thus, the ADP-ribosylation of LL-37 is expected to have the potential to modulate LL-37 biological activities in several physiological and pathological settings.<br /> (© The Author(s) 2014 Reprints and permissions: sagepub.co.uk/journalsPermissions.nav.)
Details
- Language :
- English
- ISSN :
- 1753-4267
- Volume :
- 21
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Innate immunity
- Publication Type :
- Academic Journal
- Accession number :
- 25128692
- Full Text :
- https://doi.org/10.1177/1753425914536242