Redox Biology and Diseases
Redox Biology explores the cellular and physiological functions of biological molecules having distinctive chemical reactivity and redox properties, in particular oxygen and derived reduced species (hydrogen peroxide or H2O2, the superoxide anion or O2–), iron and other biological redox metals, and the sulfur-containing amino acids methionine, with its S-methyl thioether side chain, and cysteine with its thiol (-SH) side chains. Due to their reactivity and redox properties, these molecules engage into redox reactions that are at the heart of multiple life-essential cellular enzymatic, metabolic and synthetic processes: energy production, DNA synthesis and repair, protein translation, protein secretion, stress protection and homeostasis, cellular signaling and biological clocks control. Cellular redox-based reactions have two general characteristics: (i) a high connective nature within each system, between these systems and with general cellular metabolism; (ii) the need for their strict cellular control due to the potential reactivity of reaction intermediates to avoid propagation of abnormal reactions that can lead to oxidative stress and cell death. In the past, these reactions were essentially considered by their enzymology and studied in vitro, and in Redox Biology they are repositioned in the context of the cell. As they pervade most if not all cellular processes, exploring these reactions in vivo requires integrated cellular approaches that consider the cell as a whole. Redox biology and its physiopathological impact is a fundamental issue in human health because deregulation underlies major diseases, mostly related to aging, such as cancers, neurodegenerative, metabolic and inflammatory diseases.
Our team has pioneered the field of redox biology, and is internationally recognized for its expertise in reactions involving the reversible oxidation of cysteine residues, iron, and the signaling by H2O2. Our current research now focuses on the mechanisms of cellular thiol-redox homeostasis that considers the different compartments of the eukaryotic cell, in particular the endoplasmic reticulum and links with mitochondria, and on the mechanism of the machinery that assembles iron-sulfur clusters (ISC), which are protein cofactors made of iron and sulfur and are present in a multitude of proteins and processes.
Gwenaelle LE PAVEC
Non permanent members