| Description |
1 online resource |
| Contents |
Cover -- Title Page -- Copyright Page -- Dedication -- Contents -- About the Authors -- Preface -- Acknowledgments -- Chapter 1 -- Chemical Basis of Lipid Biochemistry -- 1.1 -- Introduction -- 1.2 -- Chemistry background -- 1.3 -- Molecular interactions -- 1.4 -- Solubility in water: what is it? -- 1.5 -- Lipid biochemistry -- 1.5.1 -- Definition -- 1.5.2 -- Biochemistry of Fatty Acids -- 1.5.3 -- Biochemistry of Saturated Fatty Acids -- 1.5.4 -- Biochemistry of Unsaturated Fatty Acids -- 1.5.5 -- Glycerolipids -- 1.5.6 -- Sphingolipids -- 1.5.7 -- Sterols -- 1.6 -- Biochemical diversity of brain lipids -- 1.7 -- A key experiment: lipid analysis by thin layer chromatography -- References -- Chapter 2 -- Brain Membranes -- 2.1 -- Why lipids are different from all other biomolecules -- 2.2 -- Role of structured water in molecular interactions -- 2.3 -- Lipid self-assembly, a water-driven process? -- 2.4 -- Lipid-lipid interactions: why such a high specificity? -- 2.4.1 -- Melting Temperature of Lipids -- 2.4.2 -- The Molecular Shape of Lipids -- 2.5 -- Nonbilayer phases and lipid dynamics -- 2.6 -- The plasma membrane of glial cells and neurons: the lipid perspective -- 2.7 -- Key experiments on lipid density -- References -- Chapter 3 -- Lipid Metabolism and Oxidation in Neurons and Glial Cells -- 3.1 -- General aspects of lipid metabolism -- 3.2 -- Cholesterol -- 3.3 -- Sphingolipids -- 3.3.1 -- Biosynthesis of Ceramide in the Endoplasmic Reticulum -- 3.3.2 -- Biosynthesis of Sphingomyelin in the Golgi -- 3.3.3 -- Glycosphingolipids -- 3.3.4 -- Sphingolipid Messengers -- 3.4 -- Phosphoinositides -- 3.5 -- Phosphatidic acid -- 3.6 -- Endocannabinoids -- 3.7 -- Lipid peroxidation -- 3.8 -- Key experiment: Alzheimer's disease, cholesterol, and statins: where is the link? -- References -- Chapter 4 -- Variations of Brain Lipid Content |
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4.1 -- Brain lipids: how to bring order to the galaxy -- 4.2 -- Variations in brain cholesterol content -- 4.2.1 -- Cholesterol and Aging -- 4.2.2 -- Brain Cholesterol and Neurodegenerative Diseases -- 4.3 -- Variations in brain ganglioside content -- 4.3.1 -- Ceramide Variability -- 4.3.2 -- Sugar Head Group Variability -- 4.4 -- Variations in myelin lipids -- 4.5 -- Impact of nutrition on brain lipid content -- 4.6 -- Key experiment: the GM1/GM3 balance and Alzheimer's disease -- References -- Chapter 5 -- A Molecular View of the Synapse -- 5.1 -- The synapse: a tripartite entity? -- 5.2 -- Role of gangliosides in glutamate clearance -- 5.3 -- Neurotransmitters and their receptors: what physicochemical properties reveal -- 5.4 -- A dual receptor model for serotonin -- 5.5 -- A dual receptor model for anandamide -- 5.6 -- Control of synaptic functions by gangliosides -- 5.7 -- Control of synaptic functions by cholesterol -- 5.8 -- Key experiments: debunking myths in neurosciences -- References -- Chapter 6 -- Protein-Lipid Interactions in the Brain -- 6.1 -- General aspects of protein-lipid interactions -- 6.2 -- Annular versus nonannular lipids -- 6.3 -- Interactions between membrane lipids andcytoplasmic domains -- 6.4 -- Interactions between membrane lipids andtransmembrane domains -- 6.4.1 -- Back to First Principles -- 6.4.2 -- Cholesterol-Binding Domains -- 6.4.3 -- Interaction of TM Domains with Sphingolipids -- 6.5 -- Interactions between membrane lipids andextracellular domains -- 6.5.1 -- The Sphingolipid-Binding Domain (SBD) -- 6.5.2 -- Recognition of Membrane Cholesterol by Extracellular Proteins -- 6.6 -- Chaperone effects -- 6.7 -- Conclusions -- 6.8 -- Key experiment: the Langmuir monolayer as a universal tool for the study of lipid-protein interactions -- References -- Chapter 7 -- Lipid Regulation of Receptor Function |
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7.1 -- Specific lipid requirement of membrane proteins -- 7.2 -- Nicotinic acetylcholine receptor -- 7.3 -- Cholesterol- and ganglioside-binding domains in serotonin receptors -- 7.4 -- Cholesterol- and GalCer-binding domains insigma-1 receptors -- 7.5 -- GM1-binding domain in high-affinity NGF receptor -- 7.6 -- Phosphoinositide binding to purinergic receptors -- 7.7 -- Key experiment: transfection of membrane receptors: what about lipids? -- References -- Chapter 8 -- Common Mechanisms in Neurodegenerative Diseases -- 8.1 -- Amyloidosis: a brief history -- 8.2 -- Protein structure -- 8.3 -- Protein folding -- 8.4 -- Intrinsically disordered proteins (IDPs): the dark side of the proteome -- 8.5 -- Lipid rafts as platforms for amyloid landingand conversions -- 8.6 -- Amyloid pores -- 8.7 -- Amyloid fibrils -- 8.8 -- Common molecular mechanisms of oligomerization and aggregation -- 8.9 -- Therapeutic strategies based on lipid rafts -- 8.10 -- A key experiment: common structure of amyloid oligomers implies common mechanism of pathogenesis -- References -- Chapter 9 -- Creutzfeldt-Jakob Disease -- 9.1 -- Prion diseases -- 9.2 -- PrP: structural features, biological functions, and role in neurological diseases -- 9.3 -- The mechanism or prion replication: a great intuition and an intellectual journey of an imperturbable logic -- 9.4 -- Role of lipid rafts in the conformational plasticity of PrP -- 9.5 -- Conclusion of the investigation: who is guilty, who is innocent? -- 9.6 -- Key experiment: adenine is a minimal aromatic compound that self-aggregates in water through s-s stacking interactions -- References -- Chapter 10 -- Parkinson's Disease -- 10.1 -- Parkinson's disease and synucleopathies -- 10.2 -- a-Synuclein -- 10.3 -- Intracellular a-synuclein binds to synaptic vesicles and regulates vesicle trafficking, docking, and recycling |
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10.4 -- a-Synuclein is secreted, extracellular, and taken up by several brain cell types -- 10.5 -- a-Synuclein: a multifaceted protein with exceptional conformational plasticity -- 10.6 -- How a-synuclein interacts with membrane lipids -- 10.7 -- Oligomerization of a-synuclein into Ca2+-permeable annular channels -- 10.8 -- Electrophysiological studies of oligomeric a-synuclein channels -- 10.9 -- Cellular targets for a-synuclein in the brain: the lipid connection -- 10.10 -- Conclusion of the investigation: who is guilty, who is innocent? -- 10.11 -- Key experiment: pesticides and animal models of Parkinson's disease -- References -- Chapter 11 -- Alzheimer's Disease -- 11.1 -- Alzheimer's disease: a rapid survey, from 1906 to 2014 -- 11.2 -- The amyloid paradigm -- 11.3 -- The calcium hypothesis of Alzheimer's disease -- 11.4 -- Amyloid pores: b, a, or both? -- 11.5 -- Cholesterol -- 11.6 -- GM1 -- 11.7 -- Lipid rafts: matrix for APP processing andfactory for Ab production -- 11.8 -- Gender-specific mechanisms -- 11.9 -- Conclusions of the inquiry -- 11.10 -- Key experiment: a blood-based test to predict Alzheimer's disease? -- References -- Chapter 12 -- Viral and Bacterial Diseases -- 12.1 -- Overview of brain pathogens -- 12.2 -- Pathogen traffic to the brain -- 12.2.1 -- Rabies Virus: A Traveler to the Brain via Retrograde Axonal Routes -- 12.2.2 -- HIV: Strategies for Crossing the Blood-Brain Barrier -- 12.2.3 -- Listeria Monocytogenes -- 12.3 -- Overview of brain pathogens -- 12.3.1 -- Bacteria -- 12.3.1.1 -- N. meningitidis -- 12.3.1.2 -- H. influenzae -- 12.3.1.3 -- S. pneumoniae -- 12.3.2 -- Viruses -- 12.3.2.1 -- Enteroviruses -- 12.3.2.2 -- JC Virus -- 12.3.2.3 -- Herpes Viruses -- 12.4 -- Key experiment: what is a virus receptor? -- References -- Chapter 13 -- A Unifying Theory -- 13.1 -- Why do we need a unifying theory? |
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13.2 -- Bacteria, viruses, and amyloids converge at brain membranes -- 13.3 -- Glycosphingolipids and cholesterol in brain membranes: "un pas de deux" -- 13.4 -- Geometric aspects of glycolipid-protein andcholesterol interactions -- 13.5 -- Why two lipid receptors are better than one? -- 13.6 -- When cholesterol plays two roles -- 13.7 -- Structural disorder as a common trait of pathogenicity -- 13.8 -- Key experiment: probes to study cholesterol and/or glycolipid-dependent mechanisms -- References -- Chapter 14 -- Therapeutic Strategies for Neurodegenerative Diseases -- 14.1 -- Proteins involved in brain diseases considered asinfectious proteins -- 14.2 -- How to prevent the interaction of pathogenic proteins with brain membranes -- 14.3 -- How to prevent the insertion of pathogenic proteins into brain membranes -- 14.4 -- How to block amyloid pore formation -- 14.5 -- A universal ganglioside-binding peptide -- 14.6 -- A universal squatter of cholesterol-binding sites -- 14.7 -- Could anti-HIV drugs also be considered for thetreatment of neurodegenerative diseases? -- 14.8 -- Conclusions -- 14.9 -- A key experiment: PAMPA-BBB, a lipid-based model for the blood-brain barrier96 -- References -- Glossary -- Subject Index |
| Summary |
Lipids are the most abundant organic compounds found in the brain, accounting for up to 50% of its dry weight. The brain lipidome includes several thousands of distinct biochemical structures whose expression may greatly vary according to age, gender, brain region, cell type, as well as subcellular localization. In synaptic membranes, brain lipids specifically interact with neurotransmitter receptors and control their activity. Moreover, brain lipids play a key role in the generation and neurotoxicity of amyloidogenic proteins involved in the pathophysiology of neurological diseases. The aim of this book is to provide for the first time a comprehensive overview of brain lipid structures, and to explain the roles of these lipids in synaptic function, and in neurodegenerative diseases, including Alzheimer's, Creutzfeldt-Jakob's and Parkinson's. To conclude the book, the authors present new ideas that can drive innovative therapeutic strategies based on the knowledge of the role of lipids in brain disorders |
| Bibliography |
Includes bibliographical references and index |
| Notes |
Online resource; title from PDF title page (EBSCO, viewed May 18, 2015) |
| Subject |
Brain -- Diseases -- Alternative treatment
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Lipids.
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Lipids
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Brain -- physiology
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lipid.
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MEDICAL -- Physiology.
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SCIENCE -- Life Sciences -- Human Anatomy & Physiology.
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Lipids
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| Form |
Electronic book
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| Author |
Yahi, Nouara, author
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| ISBN |
9780128004920 |
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0128004924 |
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0128001119 |
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9780128001110 |
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