O-GlcNAcylation and oxidation of proteins: is signalling in the cardiovascular system becoming sweeter?

Hdl Handle:
http://hdl.handle.net/10675.2/805
Title:
O-GlcNAcylation and oxidation of proteins: is signalling in the cardiovascular system becoming sweeter?
Authors:
Lima, Victor V.; Spitler, Kathryn M.; Choi, Hyehun; Webb, R. Clinton; Tostes, Rita C.
Abstract:
O-GlcNAcylation is an unusual form of protein glycosylation, where a single-sugar [GlcNAc (N-acetylglucosamine)] is added (via β-attachment) to the hydroxyl moiety of serine and threonine residues of nuclear and cytoplasmic proteins. A complex and extensive interplay exists between O-GlcNAcylation and phosphorylation. Many phosphorylation sites are also known glycosylation sites, and this reciprocal occupancy may produce different activities or alter the stability in a target protein. The interplay between these two post-translational modifications is not always reciprocal, as some proteins can be concomitantly phosphorylated and O-GlcNAcylated, and the adjacent phosphorylation or O-GlcNAcylation can regulate the addition of either moiety. Increased cardiovascular production of ROS (reactive oxygen species), termed oxidative stress, has been consistently reported in various chronic diseases and in conditions where O-GlcNAcylation has been implicated as a contributing mechanism for the associated organ injury/protection (for example, diabetes, Alzheimer's disease, arterial hypertension, aging and ischaemia). In the present review, we will briefly comment on general aspects of O-GlcNAcylation and provide an overview of what has been reported for this post-translational modification in the cardiovascular system. We will then specifically address whether signalling molecules involved in redox signalling can be modified by O-GlcNAc (O-linked GlcNAc) and will discuss the critical interplay between O-GlcNAcylation and ROS generation. Experimental evidence indicates that the interactions between O-GlcNAcylation and oxidation of proteins are important not only for cell regulation in physiological conditions, but also under pathological states where the interplay may become dysfunctional and thereby exacerbate cellular injury.
Citation:
Clin Sci (Lond). 2012 Oct 1; 123(Pt 8):473-486
Issue Date:
1-Oct-2012
URI:
http://hdl.handle.net/10675.2/805
DOI:
10.1042/CS20110638
PubMed ID:
22757958
PubMed Central ID:
PMC3389386
Type:
Article
ISSN:
1470-8736
Appears in Collections:
Department of Physiology: Faculty Research and Presentations

Full metadata record

DC FieldValue Language
dc.contributor.authorLima, Victor V.en_US
dc.contributor.authorSpitler, Kathryn M.en_US
dc.contributor.authorChoi, Hyehunen_US
dc.contributor.authorWebb, R. Clintonen_US
dc.contributor.authorTostes, Rita C.en_US
dc.date.accessioned2012-10-26T20:30:47Z-
dc.date.available2012-10-26T20:30:47Z-
dc.date.issued2012-10-1en_US
dc.identifier.citationClin Sci (Lond). 2012 Oct 1; 123(Pt 8):473-486en_US
dc.identifier.issn1470-8736en_US
dc.identifier.pmid22757958en_US
dc.identifier.doi10.1042/CS20110638en_US
dc.identifier.urihttp://hdl.handle.net/10675.2/805-
dc.description.abstractO-GlcNAcylation is an unusual form of protein glycosylation, where a single-sugar [GlcNAc (N-acetylglucosamine)] is added (via β-attachment) to the hydroxyl moiety of serine and threonine residues of nuclear and cytoplasmic proteins. A complex and extensive interplay exists between O-GlcNAcylation and phosphorylation. Many phosphorylation sites are also known glycosylation sites, and this reciprocal occupancy may produce different activities or alter the stability in a target protein. The interplay between these two post-translational modifications is not always reciprocal, as some proteins can be concomitantly phosphorylated and O-GlcNAcylated, and the adjacent phosphorylation or O-GlcNAcylation can regulate the addition of either moiety. Increased cardiovascular production of ROS (reactive oxygen species), termed oxidative stress, has been consistently reported in various chronic diseases and in conditions where O-GlcNAcylation has been implicated as a contributing mechanism for the associated organ injury/protection (for example, diabetes, Alzheimer's disease, arterial hypertension, aging and ischaemia). In the present review, we will briefly comment on general aspects of O-GlcNAcylation and provide an overview of what has been reported for this post-translational modification in the cardiovascular system. We will then specifically address whether signalling molecules involved in redox signalling can be modified by O-GlcNAc (O-linked GlcNAc) and will discuss the critical interplay between O-GlcNAcylation and ROS generation. Experimental evidence indicates that the interactions between O-GlcNAcylation and oxidation of proteins are important not only for cell regulation in physiological conditions, but also under pathological states where the interplay may become dysfunctional and thereby exacerbate cellular injury.en_US
dc.rights© 2012 The Author(s) The author(s) has paid for this article to be freely available under the terms of the Creative Commons Attribution Non-Commercial Licence (http://creativecommons.org/licenses/by-nc/2.5/) which permits unrestricted non-commercial use, distribution and reproduction in any medium, provided the original work is properly cited.en_US
dc.subjectReview Articleen_US
dc.subjectS9en_US
dc.titleO-GlcNAcylation and oxidation of proteins: is signalling in the cardiovascular system becoming sweeter?en_US
dc.typeArticleen_US
dc.identifier.pmcidPMC3389386en_US
dc.contributor.corporatenameDepartment of Physiology-
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