Oxidative stress and neurodegeneration: The possible contribution of quinone reductase 2

Cassagnes, Laure‐Estelle; Chhour, Monivan; Pério, Pierre; Sudor, Ján; Gayon, Régis; Ferry, Gilles; Boutin, Jean A.; Nepveu, Françoise; Reybier, Karine

doi:10.1016/j.freeradbiomed.2018.03.002

Cited by 44 publications

(40 citation statements)

References 57 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Formaldehyde dehydrogenase (EC 1.2.1.46) and lactoylglutathione lyase (EC 4.4.1.5) oxidise their substrates to organic acids using GSH as a coenzyme [ 43 ]. Quinone reductase (EC 1.6.5.5) provides a two-electron reduction in quinones to dihydroquinones, which prevents the formation of harmful one-electron reduction products—semiquinones; epoxide hydrolase hydrates epoxides to form diols [ 44 ]. In addition, aldehyde dehydrogenase (EC 1.2.1.3) oxidises malonic dialdehyde [ 45 ].…”

Section: Redox System In Health and Disease: Brief Overviewmentioning

confidence: 99%

The Universal Soldier: Enzymatic and Non-Enzymatic Antioxidant Functions of Serum Albumin

et al. 2020

View full text Add to dashboard Cite

As a carrier of many biologically active compounds, blood is exposed to oxidants to a greater extent than the intracellular environment. Serum albumin plays a key role in antioxidant defence under both normal and oxidative stress conditions. This review evaluates data published in the literature and from our own research on the mechanisms of the enzymatic and non-enzymatic activities of albumin that determine its participation in redox modulation of plasma and intercellular fluid. For the first time, the results of numerous clinical, biochemical, spectroscopic and computational experiments devoted to the study of allosteric modulation of the functional properties of the protein associated with its participation in antioxidant defence are analysed. It has been concluded that it is fundamentally possible to regulate the antioxidant properties of albumin with various ligands, and the binding and/or enzymatic features of the protein by changing its redox status. The perspectives for using the antioxidant properties of albumin in practice are discussed.

show abstract

Section: Redox System In Health and Disease: Brief Overviewmentioning

confidence: 99%

The Universal Soldier: Enzymatic and Non-Enzymatic Antioxidant Functions of Serum Albumin

et al. 2020

View full text Add to dashboard Cite

show abstract

“…Furthermore, mAChR activation not only leads to QR2 reduced expression but is also known to affect reactive oxygen species (ROS) clearance (Frinchi et al, 2019). Since QR2 activity can directly influence cellular ROS levels and redox state (Cassagnes et al, 2018), it is unclear whether some of the anti-inflammatory effect of mAChR activation is mediated by QR2 suppression. If so, redox modulation via mAChR-dependent QR2 downregulation hours after novel taste consumption might affect redox sensitive molecules within the cell, altering the neuronal intrinsic properties.…”

Section: Introductionmentioning

confidence: 99%

Muscarinic-Dependent miR-182 and QR2 Expression Regulation in the Anterior Insula Enables Novel Taste Learning

Gould

Elkobi

Edry

et al. 2020

eNeuro

View full text Add to dashboard Cite

show abstract

“…Interestingly, MT3 knockout mice were less susceptible to menadione toxicity [80], suggesting that the inhibition of this receptor may have protective effects. Moreover, knockdown of MT3 by RNA interference in vitro resulted in enhanced expression of antioxidant enzymes [81], while overexpression of MT3 resulted in excessive production of reactive oxygen species [82]. It was shown that melatonin is able to inhibit this receptor at nanomolar levels in which antioxidant effects were documented [83].…”

Section: Roles Of Melatonin Receptors In Stroke Treatmentmentioning

confidence: 99%

Physiological and pharmacological roles of melatonin in the pathophysiological components of cellular injury after ischemic stroke

2020

View full text Add to dashboard Cite

Apart from its metabolic or physiological functions, melatonin has a potent cytoprotective activity in the physiological and pathological conditions. It is synthetized by the pineal gland and released into the blood circulation but particularly cerebrospinal fluid in a circadian manner. It can also easily diffuse through cellular membranes due its small size and lipophilic structure. Its cytoprotective activity has been linked to its potent free radical scavenger activity with the desirable characteristics of a clinically- reliable antioxidant. Melatonin detoxifies oxygen and nitrogen-based free radicals and oxidizing agents, including the highly toxic hydroxyl-and peroxynitrite radicals, initiating cellular damage. However, the cytoprotective activity of melatonin is complex and cannot be solely limited to its free radical scavenger activity. It regulates cellular signaling pathways through receptor– dependent and independent mechanisms. Most of these downstream molecules, such as PI3K/AKT pathway components, also contribute to the cytoprotective effects of melatonin. In this term, melatonin is a promising molecule for the treatment of neurodegenerative disorders, such as ischemic stroke, which melatonin reduces ischemic brain injury in animal models of ischemic stroke. It regulates also circadian rhythm proteins after ischemic stroke, playing roles in cellular survival. In this context, present article summarizes the possible role of melatonin in the pathophysiological events after ischemic stroke.

show abstract

Oxidative stress and neurodegeneration: The possible contribution of quinone reductase 2

Cited by 44 publications

References 57 publications

The Universal Soldier: Enzymatic and Non-Enzymatic Antioxidant Functions of Serum Albumin

The Universal Soldier: Enzymatic and Non-Enzymatic Antioxidant Functions of Serum Albumin

Muscarinic-Dependent miR-182 and QR2 Expression Regulation in the Anterior Insula Enables Novel Taste Learning

Physiological and pharmacological roles of melatonin in the pathophysiological components of cellular injury after ischemic stroke

Contact Info

Product

Resources

About