O-glcnacylation and oxidation of proteins: Is signalling in the cardiovascular system becoming sweeter?

Victor V. Lima, Kathryn Spitler, Hyehun Choi, R Clinton Webb, Rita C. Tostes

Research output: Contribution to journalReview article

26 Citations (Scopus)

Abstract

O-GlcNAcylation is an unusual form of protein glycosylation, where a single-sugar [GlcNAc (Nacetylglucosamine)] 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.

Original languageEnglish (US)
Pages (from-to)473-486
Number of pages14
JournalClinical Science
Volume123
Issue number8
DOIs
StatePublished - Oct 1 2012

Fingerprint

Cardiovascular System
Phosphorylation
Post Translational Protein Processing
Glycosylation
Reactive Oxygen Species
Proteins
Wounds and Injuries
Threonine
Nuclear Proteins
Hydroxyl Radical
Serine
Oxidation-Reduction
Alzheimer Disease
Oxidative Stress
Chronic Disease
Ischemia
Hypertension

Keywords

  • Cardiovascular system
  • Diabetes
  • Inflammation
  • O-linked N-acetylglucosamine (O-glcnac)
  • Phosphorylation.
  • oxidative stress

ASJC Scopus subject areas

  • Medicine(all)

Cite this

O-glcnacylation and oxidation of proteins : Is signalling in the cardiovascular system becoming sweeter? / Lima, Victor V.; Spitler, Kathryn; Choi, Hyehun; Webb, R Clinton; Tostes, Rita C.

In: Clinical Science, Vol. 123, No. 8, 01.10.2012, p. 473-486.

Research output: Contribution to journalReview article

Lima, Victor V. ; Spitler, Kathryn ; Choi, Hyehun ; Webb, R Clinton ; Tostes, Rita C. / O-glcnacylation and oxidation of proteins : Is signalling in the cardiovascular system becoming sweeter?. In: Clinical Science. 2012 ; Vol. 123, No. 8. pp. 473-486.
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