Peroxiredoxin 6 in the repair of peroxidized cell membranes and cell signaling

Fisher, Aron B.

doi:10.1016/j.abb.2016.12.003

Cited by 148 publications

(139 citation statements)

References 162 publications

(304 reference statements)

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“…), but this may be a compensatory mechanism. Oxidative modification of Prx2 and Prx6 not only contribute to impairment of the antioxidant response in the central nervous system in AD, but also may impact the signaling properties of Prxs and their ability repair peroxidized cell membranes (Fisher ) and to prevent, or delay, apoptotic cell death (Hampton and O'Connor ). In addition to their antioxidant function, Prxs also exhibit thiol redox‐regulated chaperone activity (Kumsta and Jakob ; Conway and Lee ).…”

Section: Redox Proteomics and Aβ(1–42)‐mediated Oxidative Stress In Tmentioning

confidence: 99%

Redox proteomics and amyloid β‐peptide: insights into Alzheimer disease

Butterfield

Boyd‐Kimball

2018

Journal of Neurochemistry

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Alzheimer disease (AD) is a progressive neurodegenerative disorder associated with aging and characterized pathologically by the presence of senile plaques, neurofibrillary tangles, and neurite and synapse loss. Amyloid beta-peptide (1-42) [Aβ(1-42)], a major component of senile plaques, is neurotoxic and induces oxidative stress in vitro and in vivo. Redox proteomics has been used to identify proteins oxidatively modified by Aβ(1-42) in vitro and in vivo. In this review, we discuss these proteins in the context of those identified to be oxidatively modified in animal models of AD, and human studies including familial AD, pre-clinical AD (PCAD), mild cognitive impairment (MCI), early AD, late AD, Down syndrome (DS), and DS with AD (DS/AD). These redox proteomics studies indicate that Aβ(1-42)-mediated oxidative stress occurs early in AD pathogenesis and results in altered antioxidant and cellular detoxification defenses, decreased energy yielding metabolism and mitochondrial dysfunction, excitotoxicity, loss of synaptic plasticity and cell structure, neuroinflammation, impaired protein folding and degradation, and altered signal transduction. Improved access to biomarker imaging and the identification of lifestyle interventions or treatments to reduce Aβ production could be beneficial in preventing or delaying the progression of AD. This article is part of the Proteomics special issue.

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Section: Redox Proteomics and Aβ(1–42)‐mediated Oxidative Stress In Tmentioning

confidence: 99%

Redox proteomics and amyloid β‐peptide: insights into Alzheimer disease

Butterfield

Boyd‐Kimball

2018

Journal of Neurochemistry

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“…In most cases, this disulfide is subsequently reduced by thioredoxin (Trx) (10). In contrast, 1-Cys Prxs do not have a C R , and the sulfenic acid is directly reduced by a thiol-disulfide oxidoreductase (Trx or glutaredoxin (Grx)) or low-molecularweight reductants (glutathione or ascorbate) (11). Remarkably, the type of Prx (1-Cys or 2-Cys) present at the mitochondria of distinct organisms is not conserved.…”

mentioning

confidence: 99%

Proteolytic cleavage by the inner membrane peptidase (IMP) complex or Oct1 peptidase controls the localization of the yeast peroxiredoxin Prx1 to distinct mitochondrial compartments

Gomes

Palma

Barros

et al. 2017

Journal of Biological Chemistry

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Yeast Prx1 is a mitochondrial 1-Cys peroxiredoxin that catalyzes the reduction of endogenously generated HO Prx1 is synthesized on cytosolic ribosomes as a preprotein with a cleavable N-terminal presequence that is the mitochondrial targeting signal, but the mechanisms underlying Prx1 distribution to distinct mitochondrial subcompartments are unknown. Here, we provide direct evidence of the following dual mitochondrial localization of Prx1: a soluble form in the intermembrane space and a form in the matrix weakly associated with the inner mitochondrial membrane. We show that Prx1 sorting into the intermembrane space likely involves the release of the protein precursor within the lipid bilayer of the inner membrane, followed by cleavage by the inner membrane peptidase. We also found that during its import into the matrix compartment, Prx1 is sequentially cleaved by mitochondrial processing peptidase and then by octapeptidyl aminopeptidase 1 (Oct1). Oct1 cleaved eight amino acid residues from the N-terminal region of Prx1 inside the matrix, without interfering with its peroxidase activity Remarkably, the processing of peroxiredoxin (Prx) proteins by Oct1 appears to be an evolutionarily conserved process because yeast Oct1 could cleave the human mitochondrial peroxiredoxin Prx3 when expressed in Altogether, the processing of peroxiredoxins by Imp2 or Oct1 likely represents systems that control the localization of Prxs into distinct compartments and thereby contribute to various mitochondrial redox processes.

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“…In general, flaviviruses replicate on the endoplasmic reticulum (ER), including the lysosome, after invading the target cells (Okamoto et al, 2017). 1-Cys Prx in mammalian cells is known to be localized in the cytoplasm and lysosome (Fisher, 2017), and thus, 1-Cys Prx would be abundant in the ER that produces lysosome. In addition, cyclophilin A, one of the immunophilins, facilitates the replication of flaviviruses to interact with virus-derived non-structural proteins (Qing et al, 2009), and cyclophilin A would be related to 1-Cys Prx (Prx VI) (Ishii et al, 2012).…”

Section: Discussionmentioning

confidence: 99%

A Peroxiredoxin From the Haemaphysalis longicornis Tick Affects Langat Virus Replication in a Hamster Cell Line

Kusakisako

Morokuma

Talactac

et al. 2020

Front. Cell. Infect. Microbiol.

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Ticks are hematophagous arthropods, and their blood feeding on vertebrate hosts is essential for their development. The vertebrate blood contains high levels of free iron that can react with oxygen in ticks, resulting in the production of hydrogen peroxide (H 2 O 2 ), one of the reactive oxygen species. Peroxiredoxins (Prxs), H 2 O 2 -scavenging enzymes, take on an important role in the ticks' oxidative stress coping mechanism. Ticks also transmit several disease-causing pathogens, including tick-borne encephalitis virus (TBEV), in animals and humans. Therefore, the control of ticks and tick-borne pathogens is a key issue that needs to be addressed. Infection with an arthropod-borne flavivirus is known to induce oxidative stress in insect cells. We hypothesize that vector-derived Prxs could have an effect on the infection and/or replication of flaviviruses in the hosts, since ticks Prxs are possibly transmitted from ticks to their hosts. In this study, we established stable strains of baby hamster kidney (BHK) cells expressing two types of H 2 O 2 -scavenging Prxs from the hard tick Haemaphysalis longicornis (BHK-HlPrx and BHK-HlPrx2 cells). Although the infection of TBEV surrogate Langat virus (LGTV) did not induce H 2 O 2 production in normal BHK cells, the mortality rate and the virus titer of LGTV infected BHK-HlPrx cells increased. In addition, HlPrx proteins in BHK cells can facilitate LGTV replication in cells, while HlPrx2 proteins in BHK cells cannot. The results also demonstrated that this facilitation of LGTV replication by the 1-Cys Prx in the BHK cells is not by scavenging H 2 O 2 but by an unknown mechanism. In order to understand this mechanism, more studies using tick-derived cells and ticks are necessary.

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Peroxiredoxin 6 in the repair of peroxidized cell membranes and cell signaling

Cited by 148 publications

References 162 publications

Redox proteomics and amyloid β‐peptide: insights into Alzheimer disease

Redox proteomics and amyloid β‐peptide: insights into Alzheimer disease

Proteolytic cleavage by the inner membrane peptidase (IMP) complex or Oct1 peptidase controls the localization of the yeast peroxiredoxin Prx1 to distinct mitochondrial compartments

A Peroxiredoxin From the Haemaphysalis longicornis Tick Affects Langat Virus Replication in a Hamster Cell Line

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