Biochimica et Biophysica Acta (BBA) - General Subjects
PrefaceCellular functions of glutathione
Section snippets
Christopher Horst Lillig, gained a Diploma in Biology (1998) and the degree of a Doctor of Natural Sciences (Dr. rer. nat., 2001) from the Ruhr-Universität Bochum in Germany. In 2001, he joined the Medical Nobel Institute for Biochemistry, Karolinska Institutet, Stockholm, Sweden, as postdoctoral fellow under the guidance of Arne Holmgren. He continued as group leader at the Medical Nobel Institute for Biochemistry when he was awarded the Fellowship for the Achievement of Docent Competence by
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Methionine sulfoxide reductase B from Corynebacterium diphtheriae catalyzes sulfoxide reduction via an intramolecular disulfide cascade
2020, Journal of Biological ChemistryCitation Excerpt :Although hMsrB3 has three catalytic cysteines, it has a different mechanism than the one we observed for Cd-MsrB, where the disulfide recognized by Trx is between a nucleophilic and only one specific resolving cysteine (Cys-122–Cys-66) (42). As most organisms could use an alternative reducing system, such as the LMW thiol glutathione (GSH)/GSH reductase system (21, 50), we decided to investigate whether Cd-MsrB could also be coupled to an alternative reducing pathway found in Actinobacteria, which is the MSH pathway (10, 26, 33–35, 51). MSH is involved in different processes during oxidative stress, including being a cofactor of important antioxidant enzymes (52).
The role of ethyl acrylate induced GSH depletion in the rodent forestomach and its impact on MTD and in vivo genotoxicity in developing an adverse outcome pathway (AOP)
2018, Regulatory Toxicology and PharmacologyCitation Excerpt :This supports the importance of developing relevant in vivo data to provide histopathological and biochemical information regarding the KE in the hypothesized mechanism. The knowledge base on the function of GSH in the cell has been accumulating for over 125 years (Lillig and Berndt, 2013) as has the understanding of its distribution and function within cellular compartments and organelles. Cellular systems exist to maintain the steady state balance of GSH to provide protective mechanisms to prevent cytotoxicity.
Genomic, Lipidomic and Metabolomic Analysis of Cyclooxygenase-null Cells: Eicosanoid Storm, Cross Talk, and Compensation by COX-1
2016, Genomics, Proteomics and BioinformaticsCitation Excerpt :There was an increase in genes encoding various GST isoforms, including GST theta 1 (Gstt1), GST alpha 4 (Gsta4), GST kappa 1 (Gstk1), and microsomal GST 1 and 2 (Mgst1, Mgst2), in COX-2-/- cells as compared to WT, WT + IL-1β, and COX-1-/- cells. Similarly, increased expression was also revealed for genes encoding superoxide dismutase (Sod), peroxiredoxin (Prdx), and proteins involved in the phospholipid translocation, such as scramblase 2 (Plscr2) [30–33]. The Database Search Tool for the Retrieval of Interacting Genes/Proteins (STRING) contains information on about 5.2 million proteins in 1133 species from experimental data, computational prediction methods, and public text collections.
Redox regulation of differentiation and de-differentiation
2015, Biochimica et Biophysica Acta - General Subjects
Christopher Horst Lillig, gained a Diploma in Biology (1998) and the degree of a Doctor of Natural Sciences (Dr. rer. nat., 2001) from the Ruhr-Universität Bochum in Germany. In 2001, he joined the Medical Nobel Institute for Biochemistry, Karolinska Institutet, Stockholm, Sweden, as postdoctoral fellow under the guidance of Arne Holmgren. He continued as group leader at the Medical Nobel Institute for Biochemistry when he was awarded the Fellowship for the Achievement of Docent Competence by the Swedish Society for Medical Research (SSMF) in 2005. One of his major achievements in Stockholm was the discovery of iron–sulfur glutaredoxins. Christopher Horst Lillig returned to Germany in 2006, when he was awarded the position of an Independent Emmy-Noether Group Leader in the Collaborative Research Centre 593 by the German Science Foundation (DFG). Dr. Lillig received his venia legendi in the fields of biochemistry and cell biology in 2010 and joined the Ernst-Moritz Arndt Universiät in Greifswald, Germany in 2011, where his workgroup focuses on the identification and characterization of redox signaling mechanisms in various physiological and pathological conditions.
Carsten Berndt received both the Diploma (Department of Plant Physiology, 2000) and the degree of a Doctor of Natural Sciences (Dr. rer. nat., Department of Biochemistry of Plants, 2004) from the Ruhr-University Bochum, Germany. During his PhD he investigated the role of [FeS] clusters in sulfur assimilation. Afterwards he moved to Arne Holmgren, head of the Medical Nobel Institute for Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden, where he contributed to the characterization of glutaredoxins as [FeS] proteins and the important function of glutathione in cofactor coordination as well as to the identification of glutaredoxin-dependent redox signaling during embryonic development. Since 2011 Dr. Berndt investigates specific thiol redox regulated pathways during development and pathology of the central nervous system at the Department of Neurology, Heinrich-Heine University, Düsseldorf, Germany.