Why Gluthathione?

Posted on July 9, 2024

Glutathione Graham Noctor,a,1 Guillaume Queval,a, c Amna Mhamdi,a Sejir Chaouch,a and Christine H. Foyerb a Institut de Biologie des Plantes, UMR CNRS 8618, Université de Paris sud 11, 91405 Orsay cedex, France b Centre for Plant Sciences, Faculty of Biology, University of Leeds, Leeds, LS2 9JT, UK c Present address: Department of Plant Systems Biology, Flanders Institute for Biotechnology and Department of Plant Biotechnology and Genetics, Gent University, 9052 Gent, Belgium 1 Address correspondence to [email protected] Glutathione is a simple sulfur compound composed of three amino acids and the major non-protein thiol in many organisms, including plants. The functions of glutathione are manifold but notably include redox-homeostatic buffering. Glutathione status is modulated by oxidants as well as by nutritional and other factors, and can infl uence protein structure and activity through changes in thiol-disulfi de balance. For these reasons, glutathione is a transducer that integrates environmental information into the cellular network. 

While the mechanistic details of this function remain to be fully elucidated, accumulating evidence points to important roles for glutathione and glutathione-dependent proteins in phytohormone signaling and in defense against biotic stress. Work in Arabidopsis is beginning to identify the processes that govern glutathione status and that link it to signaling pathways. As well as providing an overview of the components that regulate glutathione homeostasis (synthesis, degradation, transport, and redox turnover), the present discussion considers the roles of this metabolite in physiological processes such as light signaling, cell death, and defense against microbial pathogen and herbivores. 1. HISTORICAL OVERVIEW In 1888 de Rey-Pailhade discovered that yeast cells contain a substance that he named “philothion”, which reacts spontaneously with elemental sulfur to give hydrogen sulfi de (reviewed by Meister, 1988a). His subsequent studies etablished the widespread presence of philothion in animal and plant tissues, and led to the conclusion that the compound contained cysteine that can undergo reversible oxidation to a disulfi de form in the presence of oxygen (de Rey-Pailhade, 1928). A compound (subsequently accepted to be philothion) was extracted from muscle tissue in 1921 by Hopkins, who reported that it was autooxidizable and contained glutamic acid as well as cysteine. In the absence of a defi nitive composition, he suggested that “provisionally, for easy reference, the name glutathione will perhaps be admissible” (Hopkins, 1921). Hopkins’ view that glutathione was a dipeptide of glutamic acid and cysteine was challenged by a report that the compound was possibly a tripeptide (Hunter and Eagles, 1927). Two years later, the development of a new procedure for preparing the compound in crystalline form confi rmed that glutathione was indeed a tripeptide of glutamic acid, cysteine, and glycine (Hopkins, 1929; Figure 1). In the same year, Hopkins was awarded the Nobel Prize for this and other work on vitamins and related nutritional factors. GSH is used here to indicate the thiol (reduced) form of glutathione while GSSG denotes the disulfi de form. The term ‘glutathione’ is used where no distinction is drawn or both forms may be concerned. 

The path to the characterization of glutathione functions in plants was opened up by another Nobel Prize laureate working on vitamins. Szent-Gyorgyi (1931) observed that cabbage leaf tissue was able to reduce the oxidized form of ascorbic acid, a process that involved the simultaneous oxidation of glutathione. Indeed, the early recognition that ascorbic acid is nearly always found in the reduced state in plants, despite the presence of terminal oxidases and oxidizing catalysts, led to the conclusion that.
Noctor G, Queval G, Mhamdi A, Chaouch S, Foyer CH. Glutathione. Arabidopsis Book. 2011;9:e0142. doi: 10.1199/tab.0142. Epub 2011 Feb 18. PMID: 22303267; PMCID: PMC3267239.