Keywords:
Proteins.
;
Electronic books.
Description / Table of Contents:
This book covers ECTO-NOX, a family of cell surface-located proteins that exhibit cyanide-insensitive, timekeeping hydroquinone oxidase activity and a protein disulfide-thiol interchange activity that alternate with roles in growth, cancer and aging.
Type of Medium:
Online Resource
Pages:
1 online resource (516 pages)
Edition:
1st ed.
ISBN:
9781461439585
URL:
https://ebookcentral.proquest.com/lib/geomar/detail.action?docID=994647
DDC:
572.6
Language:
English
Note:
Intro -- ECTO-NOX Proteins -- Preface -- Contents -- Chapter 1: The ENOX Protein Family -- 1.1 The ENOX Protein Family Members -- 1.2 ENOX Proteins Are Associated with the External Cell Surface as Ecto Proteins and Are Shed into the Environment -- 1.3 Two Activities of ENOX Proteins Alternate -- 1.4 ENOX Proteins Participate Directly in the Enlargement Phase of Cell Growth -- 1.5 ENOX Proteins Are Resistant to Degradation and Tend to Form Insoluble Aggregates -- 1.6 ENOX Proteins Are Dicopper Proteins Lacking Both Iron and Flavin -- 1.7 The Oscillatory Behavior Complicates Assays of ENOX Activities -- 1.8 The Distinctive 2 + 3 Pattern of ENOX Oscillations Is a Unifying Characteristic of All Family Members -- 1.9 ENOX Proteins Differ Markedly from the NOX Proteins of Host Defense -- 1.10 ENOX Proteins Are of Low Speci c Activity -- 1.10.1 Natural Electron Donors and Acceptors for Cell Surface-Associated ENOX Proteins -- 1.10.2 Hydroquinones as Natural Electron Donors -- 1.10.3 Reduced Pyridine Nucleotides as Arti cial Electron Donors -- 1.10.4 Protein Thiols and Tyrosines as Electron Donors for arNOX Proteins and Generation of Superoxide -- 1.10.5 Aggregation and Formation of Amyloid -- 1.11 Why an External NADH Oxidase? -- 1.12 Summary -- Chapter 2: Measurements of ECTO-NOX (ENOX) Activities -- 2.1 Spectrophotometric Assay of NADH Oxidase -- 2.2 Statistical Analysis -- 2.3 Data Reduction Methods -- 2.3.1 Diode Array Instruments -- 2.4 Measurement of Hydroquinone Oxidase Activity with Reduced Coenzyme Q 10 or Phylloquinone as Substrate -- 2.4.1 Enzyme Assay for Reduced Coenzyme Q 10 Oxidase -- 2.4.2 Enzyme Assay for Reduced Phylloquinone Oxidase -- 2.5 Dissolved Oxygen Measurement -- 2.6 Estimation of Protein Disul de-Thiol Interchange Activity -- 2.7 Preparation of Scrambled RNase Substrate.
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2.8 Estimates of Protein Disul de-Thiol Interchange from Enzymatic Assay of Dipyridyl-Dithio Substrate Cleavage -- 2.9 Measurement of Trans -Plasma Membrane Redox by Reduction of Cell-Impermeable Dyes -- 2.9.1 CoQ 1 Can Function as an Intermediate Electron Carrier in WST-1 Reduction -- 2.9.2 Measurement of Plasma Membrane Electron Transport Based on WST-1 Reduction -- 2.10 Summary -- Chapter 3: The Constitutive ENOX1 (CNOX) -- 3.1 ENOX1 Function -- 3.2 ENOX1 Cloning -- 3.3 ENOX1 Characterization -- 3.4 ENOX1 Activity Requires the Presence of Copper -- 3.5 Copper Binding and Site-Directed Mutagenesis of Potential Copper-Binding Sites -- 3.6 Response to Nucleotides -- 3.7 Aggregation and Electron Microscopy -- 3.8 ENOX1 Ful lls Essential Roles in Cell Enlargement and Cellular Time-Keeping -- 3.9 ENOX1 of Human Platelets -- 3.10 Summary -- Chapter 4: Role in Plasma Membrane Electron Transport -- 4.1 Composition of the PMET -- 4.1.1 NADH Coenzyme Q Reductases -- 4.1.2 Hydroquinones -- 4.1.3 Terminal Oxidases -- 4.1.3.1 ENOX Proteins as Terminal Oxidases of PMET -- 4.1.3.2 Porin Isoform 1 or VDAC -- 4.1.3.3 57-kDa Doxorubicin-Inhibited NADH-Quinone (NADH-Ferricyanide) Reductase -- 4.1.3.4 Other Potential PMET Terminal Oxidases -- 4.2 Electron Donors and Acceptors -- 4.3 Rates of PMET -- 4.4 Energetics of PMET -- 4.5 PMET Driven Outward Proton Pumping and Alkalinization of the Cytoplasm -- 4.6 PMET Function in Electron Import -- 4.7 PMET and Growth -- 4.7.1 Cell Cycle Check Point Control of Cell Enlargement -- 4.7.2 PMET Activity and Growth Are Correlated -- 4.8 Regulation of PMET -- 4.8.1 Feedback Regulation of PMET -- 4.8.2 ENOX Cell Surface Receptor Proteins -- 4.9 PMET and Glycolysis -- 4.9.1 PMET and Glycolysis of Cancer Cells -- 4.10 PMET Links to Major Signaling Pathways -- 4.10.1 Sirtuins -- 4.10.2 Sphingolipid Rheostat.
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4.10.3 NADH Modulation of PTEN Provides Link of PMET to Ras-Raf-Mek-Erk, PI3-AKT-mTOR and NF- k B -- 4.10.4 AMP-Activated Protein Kinase -- 4.10.5 Hypoxia -- 4.11 NAD + Homeostasis -- 4.12 Summary -- Chapter 5: Role in the Enlargement Phase of Cell Growth -- 5.1 Cell Enlargement Linked to ENOX Activities -- 5.2 ECTO NADH Oxidase of Liver Plasma Membranes Stimulated by Hormones and Growth Factors -- 5.3 ECTO NADH Oxidase of Rat Hepatoma Plasma Membrane Constitutively Activated and No Longer Growth Factor or Hormone-Responsive -- 5.3.1 Thiol Reagents -- 5.4 Relationship to Growth -- 5.4.1 Plants -- 5.4.1.1 Turgor Pressure Is Not the Driving Force of Cell Enlargement in Plants -- 5.4.1.2 ECTO-NOX Proteins as Drivers of Cell Enlargement -- 5.4.1.3 Cell Enlargement of Plant Tissue Explants Oscillates with a Temperature-Independent Period Length of ca. 24 min -- 5.4.1.4 The Period Length of Cell Enlargement Is Independent of Temperature -- 5.4.1.5 Cell Enlargement Is Restricted to the Protein Disul de-Thiol Interchange Portion of the ENOX Cycle -- 5.4.2 Vertebrate Cells -- 5.4.2.1 Role of ENOX Proteins in Vertebrate Cell Enlargement -- 5.4.2.2 Cell Enlargement and Cell Cycle Control -- 5.4.2.3 Results with ENOX2 Overexpression -- 5.5 Pathological Implications -- 5.5.1 Apoptosis -- 5.6 Physical Membrane Displacements -- 5.7 ATP- and p97 AAA-ATPase-Dependent and Drug-Inhibited Vesicle Enlargement Reconstituted Using Synthetic Lipids and Recombinant Proteins -- 5.8 Summary -- Chapter 6: Roles as Ultradian Oscillators of the Cells Biological Clock -- 6.1 Time Keeping Properties -- 6.2 Molecular Studies -- 6.3 Studies with Deuterium Oxide -- 6.4 The Role of Copper -- 6.5 The Copper Clock -- 6.6 EXAFS Investigations -- 6.7 Oscillations Inherent in the Structure of Water -- 6.8 Period Length Determined by Ionic Radius of Liganded Cation.
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6.9 Spectral Evidence for Disequilibrium of ortho : para Spin States in Liquid Water That Oscillate -- 6.10 Other Mechanisms Proposed for ortho / para Conversions and Departures from Their Equilibrium Ratio of 3:1 -- 6.11 The 24-min Period Has Properties of a Carrier Wave Generated from the Basic Underlying ortho - para Water Oscillations? The Heart Rate Model -- 6.11.1 Growth Oscillations of Elongating Pollen Tubes -- 6.12 Phasing of the Rhythm -- 6.12.1 EMF Sets the Copper Clock -- 6.13 A Mechanism to Explain How Oscillations of Redox Potential of Aqueous Solutions Become Synchronous and Remain So -- 6.14 ENOX Clock and Cancer -- 6.15 Are ENOX Oscillators Linked to the Drivers of the Circadian Clock and How Are They Linked? -- 6.16 Why Oscillate? A Consequence of Active Sites in Metalloproteins? -- 6.17 Summary -- Chapter 7: Other Potential Functional Roles of ENOX Proteins -- The principal functional roles of ENOX proteins are in plasma membrane electron transport (Chapter 4), in growth (Chapter 5) and in cellular time keeping (Chapter 6). In this chapter indications for other possible functional roles of ENOX proteins in diverse cellular processes are considered. 7.1 Cell Cycle Control -- 7.2 Gene Regulation -- 7.3 Endomembrane Function, Membrane Displacements, Vesicle Budding -- 7.3.1 Membrane Budding -- 7.3.2 Energy Requirements for Physical Membrane Displacement -- 7.4 Endocytosis and Autophagy -- 7.5 Host Defense -- 7.6 pH Control -- 7.7 Lipid Oxidation -- 7.7.1 arNOX Inhibitors and Prevention of Coronary Artery Disease -- 7.8 Life Extension and Calorie Restriction -- 7.9 Control of Apoptosis and Cell Survival -- 7.10 Neurodegenerative Disorders -- 7.11 Memory -- 7.12 Gametogenesis -- 7.13 Role in Viral Pathogenesis.
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7.13.1 ENOX2 Inhibitor (−)-Epigallocatechin-3-Gallate Blocks Virus Infections Alone and in Combination with Capsicum Vanilloids and Other Green Tea Catechins -- 7.13.1.1 HIV and FIV -- 7.13.1.2 Other Viruses -- 7.13.2 Brefeldin A and Antitumor Quassinoids -- 7.14 Summary -- Chapter 8: ENOX2 (tNOX) and Cancer -- 8.1 ENOX2 Discovery -- 8.2 ENOX2 Activity -- 8.2.1 Biochemistry -- 8.3 Sequence -- 8.4 Structural Properties -- 8.5 ENOX2 Presence and Cancer -- 8.5.1 ENOX2 Autoantibodies Generated in Cancer Patients -- 8.5.2 ENOX2 Gene Present in Genome as a Single Copy -- 8.5.3 ENOX2 Lacks Intrinsic Membrane-Binding Motifs -- 8.5.4 ENOX2 Has Properties of a Prion and Is Protease Resistant -- 8.6 ENOX2 Has Characteristics of an Oncofetal Protein -- 8.7 Transgenic Mouse Strain Overexpressing ENOX2 -- 8.8 Alternative Splicing as Basis for Speci c ENOX2 Localization to the Cell Surface -- 8.8.1 Full-Length ENOX2 MRNA Identical to That of Cancer Cells Exists in Human Non-cancer Cells and Tissues -- 8.8.2 Full-Length 71 kDa ENOX2 Protein Not Translated -- 8.8.3 Cancer-Speci c Expression of ENOX2 -- 8.8.4 Splice Variants of ENOX2 Were Found in Cancer Cells -- 8.8.5 Expression of Exon 4 Minus and Exon 5 Minus Forms of ENOX2 in COS Cells -- 8.8.6 Delivery of 34 kDa ENOX2 Protein to the Plasma Membrane -- 8.8.6.1 Evidence for ENOX2 in Golgi Apparatus -- 8.8.7 Mutation of Met 231 Blocked Expression of the Exon 4 Minus Splice Variant -- 8.8.8 Subcellular Localization of E4m ENOX2-EGFP and Full-Length ENOX2-EGFP Fusion Proteins -- 8.8.9 Regulation of ENOX2 Expression -- 8.9 hnRNP F Splicing Factor Directs Formation of the Exon 4 Minus Variant of ENOX2 -- 8.10 Summary -- Chapter 9: Age-Related ENOX Proteins (arNOX) -- 9.1 arNOX Discovery -- 9.2 Measurement of Superoxide Formation by arNOX -- 9.3 Characteristics -- 9.4 arNOX Cloning.
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9.5 Characterization of Recombinant arNOX Proteins.
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