Selenium Its Molecular Biology and Role in Human Health 4th Edition by Dolph Hatfield, Ulrich Schweizer, Petra Tsuji, Vadim Gladyshev 3319412817 9783319412818

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ISBN-10 :  3319412817 

ISBN-13 :  9783319412818

Author:  Dolph L. Hatfield, Ulrich Schweizer, Petra Tsuji, Vadim Gladyshev 

In the current edition, Selenium: Its Molecular Biology and Role in Human Health expands extensively on the previous editions providing readers with the most significant advances in the rapidly developing selenium field. Evidence from epidemiology and veterinary science supports the essential role of selenium in (human) health, but its split personality in both preventing and supporting cancer and also in promoting insulin resistance has become more clearly defined. The pivotal role of glutathione peroxidase 4 in a new process of programmed cell death, ferroptosis, brings new impetus to the field. Recently defined mutations in selenoprotein and biosynthesis factor genes have been identified in patients, and the resulting disorders further emphasize the significance of selenoproteins in human health. The mechanism of selenoprotein biosynthesis, the functions of selenoproteins, and the roles of dietary selenium have been further elucidated, and new regulatory mechanisms involving selenoproteins discovered. The book, therefore, covers the breadth of current selenium research. With up-to-date chapters written by leaders in their fields, it serves as an invaluable resource for novices as well as specialists.

Selenium Its Molecular Biology and Role in Human Health 4th Table of contents:

Part I: The Machinery of Selenoprotein Biosynthesis
Chapter 1: Selenocysteine tRNA[Ser]Sec: From Nonsense Suppressor tRNA to the Quintessential Const
1.1 Introduction
1.2 Primary and Secondary Structures of Sec tRNA
1.3 Um34 Addition to Sec tRNA[Ser]Sec, a Most Highly Specialized Modification
1.4 Trsp, the Sec tRNA[Ser]Sec Gene
1.5 Transcription of Trsp
1.6 The Genetic Codeword for Sec tRNA[Ser]Sec is UGA
1.7 Crystallization of tRNA[Ser]Sec
1.8 Concluding Remarks
References
Chapter 2: Eukaryotic Mechanisms of Selenocysteine Incorporation and Its Reconstitution In Vitro
2.1 Introduction
2.2 UGA Recoding
2.3 SECIS
2.4 SECIS Binding Protein 2
2.5 Sec-Specific Elongation Factor
2.6 Other Factors
2.7 Unique Sec Incorporation: Selenoprotein P
2.8 Impact of In Vitro Translation Systems for Studying Sec Incorporation
2.9 Concluding Remarks
References
Chapter 3: Probing Selenoprotein Translation by Ribosome Profiling
3.1 Introduction
3.2 Translational Control of Gene Expression Revealed by Ribosome Profiling
3.3 Application of Ribosome Profiling to Investigate Selenoprotein Biosynthesis
3.3.1 Selenocysteine Incorporation Efficiency
3.3.2 Ribosome Occupancy Near the UGA-Sec Codon and in the 5′ UTR
3.4 Conclusion: Insights Gained, Limitations, and Future Directions
References
Chapter 4: Pathways in De Novo Biosynthesis of Selenocysteine and Cysteine in Eukaryotes
4.1 Introduction
4.2 Sec Biosynthesis
4.2.1 Discoveries That Provided the Foundation for Sec Biosynthesis
4.2.2 Step 1: Aminoacylation of tRNA[Ser]Sec
4.2.3 Step 2: Phosphorylation of the Serine Moiety
4.2.4 Step 3: Generation of Selenophosphate, the Active Selenium Donor
4.2.5 Sec Synthesis
4.3 De Novo Synthesis of Cys and Cys/Sec Replacement In Vitro and In Vivo
4.3.1 In vivo Studies
4.3.2 In Vitro Studies
4.4 Concluding Remarks
References
Chapter 5: Prokaryotic Selenoprotein Biosynthesis and Function
5.1 Introduction
5.2 Selenocysteine
5.3 Selenoprotein Synthesis in Bacteria
5.3.1 Sec Biosynthesis and Incorporation in E. coli
5.3.2 Selenoprotein Synthesis in Other Bacteria
5.4 Selenoprotein Synthesis in Archaea
5.5 Selenoproteins of Prokaryotes
5.5.1 Predicted Selenoproteins
5.5.2 Formate Dehydrogenase
5.5.3 Hydrogenase
5.5.4 Glycine Reductase
5.5.5 Proline Reductase
5.5.6 Methionine Sulfoxide Reductase
5.5.7 Seleno(mono)phosphate Synthetase
5.5.8 Formyl-Methanofuran Dehydrogenase
5.5.9 Heterodisulfide Reductase
5.5.10 HesB-Like Selenoprotein
5.5.11 Benzoyl-CoA Reductase
5.6 Concluding Remarks
References
Chapter 6: The Role of Selenium in Human Evolution
6.1 Introduction
6.2 Diet and Natural Selection
6.3 Worldwide Availability of Se
6.4 Genetic Variation in Human Se-Related Genes
6.5 Human Adaptation to Dietary Se
6.6 Adaptation to Se Deficiency in China
6.7 Genes That May Be Important for Adaptation to Se Deficiency
6.8 Concluding Remarks
References
Chapter 7: The Chemistry of Selenocysteine in Proteins
7.1 Selenocysteine in Chemical Protein Synthesis
7.2 Selenocysteine in Oxidative Protein Folding
7.3 SEP15 and SELM in In Vivo Protein Folding
7.4 Concluding Remarks
References
Chapter 8: Evolution of Selenophosphate Synthetase
8.1 Introduction
8.2 SPS Supports Diverse Se Utilization Traits in Prokaryotes
8.2.1 Bacteria
8.2.2 Archaea
8.3 SPS in Eukaryotes
8.3.1 Emergence of SPS1 Genes in Metazoa
8.4 Concluding Remarks
References
Chapter 9: Structure and Mechanism of Selenocysteine Synthases
9.1 Introduction
9.2 The Structure and Architecture of the Bacterial SelA
9.3 The Structure of the Archaeal and Eukaryotic SepSecS
9.4 Divergent Active Sites of Selenocysteine Synthases and a Conserved Catalytic Mechanism
9.5 Future Directions
References
Chapter 10: Mechanism, Structure, and Biological Role of Selenocysteine Lyase
10.1 Mammalian Selenium Metabolism
10.2 Identification of SCLY in Mammals and Bacteria
10.3 Orthologous Genes in Various Organisms
10.4 Homology to NifS-type Cysteine Desulfurases
10.5 Structure and Open-Close Conformational Change
10.6 Catalytic Mechanism
10.7 Discrimination Between Selenium and Sulfur
10.8 Biological Role
References
Part II: Selenoproteins, Their Occurrence and Function
Chapter 11: Eukaryotic Selenoproteomes
11.1 Introduction
11.2 Computational Tools for Selenoprotein Identification
11.3 Mammalian Selenoproteins
11.3.1 Glutathione Peroxidases
11.3.2 Thyroid Hormone Deiodinases
11.3.3 Thioredoxin Reductases
11.3.4 Methionine-R-Sulfoxide Reductase 1 (MSRB1)
11.3.5 15 kDa Selenoprotein (SEP15)
11.3.6 Selenophosphate Synthetase 2 (SEPHS2)
11.3.7 Selenoprotein P (SEPP1)
11.3.8 Selenoproteins W (SelW, SEPW1) and V (SELV)
11.3.9 Selenoproteins T (SELT), M (SELM) and H (SELH)
11.3.10 Selenoproteins O (SELO) and I (SELI)
11.3.11 Selenoprotein K (SELK) and S (SELS)
11.3.12 Selenoprotein N (SEPN1)
11.4 Additional Selenoproteins in Eukaryotes
11.5 Selenoprotein Functions
11.6 Selenoproteomes
11.7 Applications of Selenoproteome Analyses to Biology
11.7.1 Genetic Code Supports Targeted Insertion of Two Amino Acids by One Codon
11.7.2 High-Throughput Identification of Catalytic Redox-­Active Cysteine Residues
11.8 Analyses of Ionomes
11.9 Concluding Remarks
References
Chapter 12: Prokaryotic Selenoproteins and Selenoproteomes
12.1 Introduction
12.2 Computational Identification of Selenoproteins in Prokaryotes
12.3 Prokaryotic Selenoproteins
12.4 Comparative Genomics of Selenoproteomes in Prokaryotes
12.5 Concluding Remarks
References
Chapter 13: Functional Genomics of Selenoproteins and Se-responsive Pathways
13.1 Introduction
13.2 Selenium Metabolism and Transport
13.3 The Effects of SNPs on the Sec Incorporation Machinery
13.4 Genetic Variants Affecting Redox-Active Selenoproteins
13.4.1 Genetic Variants in GPX4
13.4.2 Genetic Variants in GPX1
13.4.3 Genetic Variants in TXNRDs
13.5 Genetics of Endoplasmic Reticulum Selenoproteins
13.6 Perspectives
References
Chapter 14: Selenium Regulation of the Selenoprotein and Non-selenoprotein Transcriptomes in a 
14.1 Introduction
14.2 Animal Models for Se Regulation of Selenoprotein Transcripts
14.3 Se Regulation of Conventional Se Biomarks
14.4 Se Regulation of Selenoprotein Transcripts in Rats
14.5 Se Regulation of Selenoprotein Transcripts in Mice
14.6 Se Regulation of Selenoprotein Transcripts in Turkeys
14.7 Se Regulation of Selenoprotein Transcripts in Chickens
14.8 Se Regulation of Selenoprotein Transcripts in Caenorhabditis elegans
14.9 Overall Selenoprotein Transcript Regulation
14.10 Se Regulation of Non-selenoprotein Transcripts in Rodents
14.11 Se Regulation of Non-selenoprotein Transcripts in C. elegans
14.12 Se Regulation of Non-selenoprotein Transcripts in Avian Species
14.13 Molecular Biomarker Panels
References
Chapter 15: 77Se NMR Spectroscopy of Selenoproteins
15.1 NMR Spectroscopy of Biological Macromolecules
15.2 Selenium’s NMR Properties
15.3 77Se Isotopic Enrichment of Proteins for NMR Studies
15.4 Identification of Chemical Species by 77Se NMR
15.5 The Connectivity of Diselenide Bonds
15.6 Measurements of Sec pKa in Selenoproteins and Selenopeptides
15.7 Conformational Preferences and Dynamics of Sec
15.8 77Se NMR Sensitivity to the Local Environment
15.9 Data Interpretation
15.10 Concluding Remarks
References
Chapter 16: Thioredoxin Reductase 1 as an Anticancer Drug Target
16.1 Introduction
16.2 The Multiple Roles of the Thioredoxin System in Cancer
16.3 The Interplay Between Thioredoxin Reductase and Nrf2
16.4 Impact of Thioredoxin Reductase Targeting in Cancer and Its Potential for New Anticancer Th
16.5 Potential Beneficial Effects of TrxR1 Drug Targeting for Anticancer Therapy
16.5.1 Nrf2 Activation, with Increased Detoxifying Protection Against Carcinogens and Inhibited I
16.5.2 Direct and Specific Cancer Cell Killing Effects Due to Their Increased Reliance upon TrxR
16.5.3 Impaired Proteasome Function Linked to TrxR1 Inhibition
16.5.4 Impaired Angiogenesis upon TrxR1 Inhibition
16.5.5 Nrf2 Activation and/or Trx1 and Trx80 Secretion Yielding Increased Anti-Tumoral Immune Syste
16.6 Potential Cancer-Promoting Effects of TrxR1 Drug Targeting
16.6.1 Impaired p53 Function Due to TrxR1 Insufficiency
16.6.2 Increased Cancer-Promoting Mutagenesis Due to Increased ROS Levels after TrxR1 Targeting
16.6.3 Increased Growth- and Cancer Promoting Protein Phosphorylation Cascades and/or other Signali
16.6.4 Nrf2 Activation in Cancer Cells, with Increased Cancer Cell Robustness
16.7 Concluding Remarks
References
Chapter 17: Basics and News on Glutathione Peroxidases
17.1 Introduction
17.2 The Glutathione Peroxidase Reaction
17.3 Diversification Within the GPx Family
17.3.1 Structure and Substrate Specificity
17.3.2 Diversified Biological Roles
17.4 Concluding Remarks
References
Chapter 18: Glutathione Peroxidase 4
18.1 Introduction
18.2 Gene Structure
18.3 Protein Structure
18.4 Enzymatic Activity
18.5 Kinetics
18.6 Catalytic Mechanism
18.7 Functions
18.8 Genetic Diseases and Polymorphisms
18.9 Male Fertility
18.10 Inflammation
18.11 Cell Death and Survival
18.12 Metabolic Diseases
18.13 Viral Diseases
18.14 Conclusions, Unresolved Questions, and Perspectives
References
Chapter 19: The 15 kDa Selenoprotein: Insights into Its Regulation and Function
19.1 Introduction
19.2 SEP15 Structure and Function
19.3 Biological Function of SEP15
19.4 Human SEP15 Polymorphisms and Cancer
19.5 Concluding Remarks
References
Chapter 20: Selenoprotein K and Protein Palmitoylation in Regulating Immune Cell Functions
20.1 Introduction
20.2 Protein Palmitoylation
20.3 The Role of SELK-Dependent Palmitoylation in Regulating the Stability and Function of CD36
20.4 The Role of SELK-Dependent Palmitoylation in Regulating the Function of the IP3R
20.5 How Does SELK Contribute to Protein Palmitoylation?
20.6 Concluding Remarks
References
Chapter 21: Selenoprotein M: Structure, Expression and Functional Relevance
21.1 Discovery and Structure
21.2 Expression
21.3 Role in Neuroprotection
21.4 Characterization of the Selm Knockout Mouse
21.5 Involvement in Cancer
21.6 Concluding Remarks
References
Chapter 22: Selenoprotein P and Selenium Distribution in Mammals
22.1 Introduction
22.2 Selenoprotein P (Sepp) Is a Plasma Selenium Transport Protein
22.3 Lipoprotein Receptor-Related Proteins as Endocytic Receptors Involved in Sepp Uptake
22.4 Mouse Models of Modified Sepp, Lrp2 or Lrp8 Expression
22.4.1 Classical Gene Targeting
22.4.2 Isoforms of Sepp
22.4.3 Sepp in the Liver
22.4.4 Sepp in the Brain
22.4.5 Sepp in the Kidney
22.5 Regulation of Sepp Expression
22.6 Comparison of Experimental Concepts with Clinical Data
22.7 Concluding Remarks
References
Chapter 23: Selenoprotein T: From Discovery to Functional Studies Using Conditional Knockout Mice
23.1 Introduction
23.2 Structure, Subcellular Localization and Activity
23.3 Tissue-Distribution and Regulation of Gene Expression
23.4 Function
23.4.1 Role in Ca2+ Regulation and Cell Adhesion
23.4.2 Role in Brain
23.4.3 Role in Pancreas
23.4.4 Role in Liver
23.5 Concluding Remarks
References
Chapter 24: Biochemistry and Function of Methionine Sulfoxide Reductase
24.1 Introduction
24.2 Methionine Oxidation
24.3 Methionine Sulfoxide Reductase Families
24.4 Functions of Methionine Sulfoxide Reductase
References
Part III: Dietary Selenium and Its Impact on Human Health
Chapter 25: Selenium: Dietary Sources, Human Nutritional Requirements and Intake Across Populations
25.1 Introduction
25.2 Geographic Distribution and Production
25.3 Dietary Sources
25.4 Human Se Requirements and Patterns of Consumption
25.5 Availability, Absorption and Metabolism
25.6 Se Intake and Se Status
25.6.1 Se Status Across Geographic Locations
25.6.2 Se Deficiency
25.6.3 Selenosis/Se Toxicity
25.7 Concluding Remarks
References
Chapter 26: Human Clinical Trials Involving Selenium
26.1 Introduction
26.2 Successful Prevention of Endemic Diseases Linked to Se Deficiency
26.3 Clinical Trials for Biomarker Identification of Se Status
26.4 Se and Cancer Prevention
26.5 Se and Cancer Treatment
26.6 Se in Sepsis
26.7 Se in Thyroid Disease
26.8 Viral Infections
26.9 Pregnancy
26.10 Concluding Remarks
References
Chapter 27: Status of Dietary Selenium in Cancer Prevention
27.1 Evidence for a Selenium-Mediated Antitumorigenesis
27.1.1 Emergence of Evidence
27.1.2 Clinical Trial Results
27.2 Mechanisms of Selenium Antitumorigenicity
27.2.1 Roles of Selenocysteine-Containing Selenoproteins
27.2.2 Roles of other Selenium-Associated Proteins
27.2.3 Roles of Selenium-Metabolites
27.2.3.1 Effects of Selenium-Metabolites on Tumor Cells
27.2.3.2 Mechanisms Underlying Selenium-Antitumorigenesis
Redox Cycling
Modification of Protein-Thiols
Methionine Mimicry
27.3 Evidence for Tumorigenic Actions of Selenoproteins
27.4 Risks of Supranutritional Se Intakes
27.5 Concluding Remarks
References
Chapter 28: Selenium in HIV/AIDS
28.1 Introduction
28.2 Se and Immunity
28.3 HIV, Antiretroviral Treatment, Oxidative Stress and Se
28.4 Observational Studies of Se Deficiency and HIV
28.5 Se Supplementation in HIV
28.6 Clinical Trials of Supplementation in HIV-Positive Patients that Included Se in the Experim
28.7 Concluding Remarks
References
Chapter 29: Genetic Variations in the Genes for Selenoproteins Implicate the Encoded Proteins in
29.1 Introduction
29.2 The Types of Genetic Variations to Consider
29.3 Glutathione Peroxidase 1 (GPX1)
29.4 The 15 kDa Selenoprotein (SEP15)
29.5 Glutathione Peroxidase 4 (GPX4)
29.6 Thioredoxin Reductases (TXNRD)
29.7 Selenoprotein S (SELS)
29.8 Selenoprotein P (SEPP1) and Its Impact on Other Selenoproteins
29.9 Concluding Remarks
References
Chapter 30: Is Adequate Selenium Important for Healthy Human Pregnancy?
30.1 Introduction
30.2 Pre-eclampsia
30.2.1 Observational Studies of Se and Pre-eclampsia
30.2.2 Se Supplementation in Pregnancy
30.2.3 How Might Se Lower the Risk of Pre-eclampsia?
30.3 Miscarriage
30.4 Preterm Birth
30.4.1 How Might Se Affect the Risk of Preterm Birth?
30.5 Autoimmune Thyroid Disease
30.5.1 How May Se Affect the Risk of Autoimmune Thyroid Disease in Pregnancy?
30.6 Insulin Resistance
30.7 Concluding Remarks
References
Chapter 31: The Epidemiology of Selenium and Human Health
31.1 Introduction
31.2 Cancer
31.3 Cardiovascular Disease
31.4 Diabetes
31.5 Thyroid Disease
31.6 Neurological Disease
31.7 Concluding Remarks
References
Chapter 32: Sex-Specific Differences in Biological Effects and Metabolism of Selenium
32.1 Selenium Metabolism in Female and Male Animals
32.2 Sex-Specific Regulation of Selenoprotein Expression
32.3 Sexual Dimorphic Findings in Clinical Studies
32.3.1 Cancer
32.3.2 Infectious Diseases and Sepsis
32.3.3 Autoimmune Thyroid Disease
32.3.4 Cardiovascular System
32.4 Sexual Dimorphic Risk/Benefit Ratio of Se Supplementation
32.5 Concluding Remarks

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