Protein Sensors of Reactive Oxygen Species, Part A: Selenoproteins and Thioredoxin

Erscheinungsjahr 2002
ISBN: 978-0-12-182248-4
Verlag: William Andrew Publishing

Buch, Englisch, 511 Seiten, Format (B × H): 152 mm x 229 mm, Gewicht: 830 g

This volume of Methods in Enzymology is concerned with the rapidly developing field of selenoprotein synthesis and its related molecular genetics. Progressive information on the topics of proteins as redox sensors, selenoproteins, and the thioredoxin system is studied using methods such as bioinformatics, DNA chip technology, cell biology, molecular genetics, and enzymology. The information on novel selenoproteins identified from genomic sequence data, as well as current knowledge on glutathione peroxidases, selenoprotein P, iodothyronine deiodinases, and thioredoxin reductases, is presented in a method-based approach.

Zielgruppe

Biochemists, pharmacologists, physiologists, cell biologists, molecular biologists, and biomedical researchers.

Fachgebiete

• Naturwissenschaften Physik Angewandte Physik Biophysik
• Naturwissenschaften Biowissenschaften Enzymologie
• Naturwissenschaften Biowissenschaften Angewandte Biologie Biophysik

Inhaltsverzeichnis

Section I: Selenoproteins

[1]: Selenoprotein Biosynthesis: Purification and Assay of Components Involved in Selenocysteine Biosynthesis and Insertion in Escherichia coli

[2]: Selenocysteine Insertion Sequence Element Characterization and Selenoprotein Expression

[3]: Transfer RNAs That Insert Selenocysteine

[4]: Purification and Analysis of Selenocysteine Insertion Sequence-Binding Protein 2

[5]: Nonsense-Mediated Decay: Assaying for Effects on Selenoprotein mRNAs

[6]: Novel Selenoproteins Identified from Genomic Sequence Data

[7]: Semisynthesis of Proteins Containing Selenocysteine

[8]: Mammalian Selenoprotein Gene Signature: Identification and Functional Analysis of Selenoprotein Genes Using Bioinformatics Methods

[9]: Estimation of Individual Types of Glutathione Peroxidases

[10]: High-Throughput 96-Well Microplate Assays for Determining Specific Activities of Glutathione Peroxidase and Thioredoxin Reductase

[11]: Selenoprotein P

[12]: Iodothyronine Deiodinases

[13]: Expression and Regulation of Thioredoxin Reductases and Other Selenoproteins in Bone

[14]: Selenoprotein W

[15]: Genetic and Functional Analysis of Mammalian Sep15 Selenoprotein

[16]: Selenocysteine Lyase from Mouse Liver

[17]: Selenocysteine Methyltransferase

[18]: Phospholipid-Hydroperoxide Glutathione Peroxidase in Sperm

[19]: In Vivo Antioxidant Role of Glutathione Peroxidase: Evidence from Knockout Mice

[20]: Recombinant Expression of Mammalian Selenocysteine-Containing Thioredoxin Reductase and Other Selenoproteins in Escherichia coli

[21]: Mammalian Thioredoxln Reductases as Hydroperoxide Reductases

[22]: Tryparedoxin and Tryparedoxin Peroxidase

[23]: Trypanothione and Tryparedoxin in Ribonucleotide Reduction

[24]: Selenium- and Vitamin E-Dependent Gene Expression in Rats: Analysis of Differentially Expressed mRNAs

Section II: Thioredoxin

[25]: Overview

[26]: Thioredoxin and Glutaredoxin Isoforms

[27]: Mammalian Thioredoxin Reductases

[28]: Mitochondrial Thioredoxin Reductase and Thiol Status

[29]: Protein Electrophoretic Mobility Shift Assay to Monitor Redox State of Thioredoxin in Cells

[30]: Recycling of Vitamin C by Mammalian Thioredoxin Reductase

[31]: Thioredoxin Cytokine Action

[32]: Identification of Thioredoxin-Linked Proteins by Fluorescence Labeling Combined with Isoelectric Focusing/Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis

[33]: Thioredoxin and Mechanism of Inflammatory Response

[34]: Redox State of Cytoplasmic Thioredoxin

[35]: Thioredoxin, Thioredoxin Reductase, and Thioredoxin Peroxidase of Malaria Parasite Plasmodium falciparum

[36]: Human Placenta Thioredoxin Reductase: Preparation and Inhibitor Studies

[37]: Classification of Plant Thioredoxins by Sequence Similarity and Intron Position

[38]: Ferredoxin-Dependent Thioredoxin Reductase: A Unique Iron-Sulfur Protein

[39]: Plant Thioredoxin Gene Expression: Control by Light, Circadian Clock, and Heavy Metals

[40]: Thioredoxin Genes in Lens: Regulation by Oxidative Stress

[41]: Thioredoxin Overexpression in Transgenic Mice

[42]: Multiplex Reverse Transcription-Polymerase Chain Reaction for Determining Transcriptional Regulation of Thioredoxin and Glutaredoxin Pathways

[43]: Redox Regulation of Cell Signaling by Thioredoxin Reductases

Author index

Subject index

Über Autor(innen)

Helmut Sies is an Honorary Member of the American Society for Biochemistry and Molecular Biology. He received an Honorary Ph.D. from the University of Buenos Aires, Argentina in 1996. Dr. Sies is a member of the Northrhine-Westphalian Academy of Sciences, Germany, and a Corresponding Member of both the Academy of Sciences of Heidelberg, Germany, and the Academy of Medicine, Buenos Aires, Argentina. He has received many awards and prizes, including the FEBS Anniversary Prize awarded by the Federation of European Biochemical Societies, 1978; the Distinguished Foreign Scholar award, MASUA, 1985; the Silver Medal, Karolinska Institute, Stockholm, 1986; the Ernst Jung Preis fur Medizin, 1988; the Claudius-Galenus-Preis, 1990; and the ISFE-Preis, 1994. Dr. Sies sereves on the editorial board and advisory committee for twelve journals, has edited numerous books, and has published more than 400 original articles and chapters. He received his M.D. at the University of Munich in 1967 and currently serves as Full Professor and Chairman of the Department of Physiological Chemistry at the University of Dusseldorf.