Redox regulation of protein damage in plasma


The presence and concentrations of modified proteins circulating in plasma depend on rates of protein synthesis, modification and clearance. In early studies, the proteins most frequently analysed for damage were those which were more abundant in plasma (e.g. albumin and immunoglobulins) which exist at up to 10 orders of magnitude higher concentrations than other plasma proteins e.g. cytokines. However, advances in analytical techniques using mass spectrometry and immuno-affinity purification methods, have facilitated analysis of less abundant, modified proteins and the nature of modifications at specific sites is now being characterised. The damaging reactive species that cause protein modifications in plasma principally arise from reactive oxygen species (ROS) produced by NADPH oxidases (NOX), nitric oxide synthases (NOS) and oxygenase activities; reactive nitrogen species (RNS) from myeloperoxidase (MPO) and NOS activities; and hypochlorous acid from MPO. Secondary damage to proteins may be caused by oxidized lipids and glucose autooxidation.In this review, we focus on redox regulatory control of those enzymes and processes which control protein maturation during synthesis, produce reactive species, repair and remove damaged plasma proteins. We have highlighted the potential for alterations in the extracellular redox compartment to regulate intracellular redox state and, conversely, for intracellular oxidative stress to alter the cellular secretome and composition of extracellular vesicles. Through secreted, redox-active regulatory molecules, changes in redox state may be transmitted to distant sites. © 2014 The Authors.

Publication DOI:
Divisions: College of Health & Life Sciences
College of Health & Life Sciences > Chronic and Communicable Conditions
College of Health & Life Sciences > School of Biosciences
College of Health & Life Sciences > School of Biosciences > Cellular and Molecular Biomedicine
College of Health & Life Sciences > School of Biosciences > Cell & Tissue Biomedical Research
Additional Information: © 2014 The Authors. Published by Elsevier B.V. This is an open access article under the CC BY-NC-SA license (
Uncontrolled Keywords: ageing,glycosylation,nitration,oxidation,peroxiredoxin,thioredoxin,Biochemistry,Organic Chemistry
Publication ISSN: 2213-2317
Last Modified: 03 May 2024 07:10
Date Deposited: 26 Feb 2014 03:14
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Related URLs: http://www.scop ... tnerID=8YFLogxK (Scopus URL)
PURE Output Type: Article
Published Date: 2014-01-20
Authors: Griffiths, Helen R. (ORCID Profile 0000-0002-2666-2147)
Dias, Irundika (ORCID Profile 0000-0002-6620-8221)
Willetts, Rachel S.
Devitt, Andrew (ORCID Profile 0000-0002-4651-6761)


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