Keywords:
Heart -- Diseases -- Prevention.
;
Cardiovascular system -- Diseases.
;
Electronic books.
Type of Medium:
Online Resource
Pages:
1 online resource (320 pages)
Edition:
1st ed.
ISBN:
9783319152639
URL:
https://ebookcentral.proquest.com/lib/geomar/detail.action?docID=1998480
DDC:
612.17
Language:
English
Note:
Intro -- Cardiac Cytoarchitecture: Why Bother? -- Acknowledgements -- References -- Contents -- Chapter 1: Cardiac Cytoarchitecture in Health and Disease -- 1.1 Cardiomyocytes During Development -- 1.2 Cardiomyocytes in Disease -- 1.3 How to Study Cardiac Cytoarchitecture -- References -- Chapter 2: In Vitro Tools for Quantifying Structure-Function Relationships in Cardiac Myocyte Cells and Tissues -- 2.1 Structure-Function Relationships in Single Cardiac Myocytes -- 2.1.1 Myofibrillogenesis: Self-Assembly of the Contractile Apparatus -- 2.1.2 Myocyte Shape Remodeling in Development and Disease -- 2.1.3 Extracellular Matrix Regulation of Cardiac Myocyte Structure and Function -- 2.2 Structure-Function Relationships at the Intercalated Disc -- 2.2.1 Co-development of the Intercalated Disc with the Contractile Apparatus -- 2.2.2 Potential Role of the Extracellular Matrix in Pathological Intercalated Disc Remodeling -- 2.2.3 Engineering Gap Junctions -- 2.3 Structure-Function Relationships in Multicellular Cardiac Tissues -- 2.3.1 Organization and Structure In Vivo and In Vitro -- 2.3.2 Tissue Organization and Electrophysiology -- 2.3.3 Tissue Organization and Contractility -- 2.3.4 Stem Cell-Derived Cardiac Tissues: Potential Therapeutic Applications -- 2.4 Conclusions -- References -- Chapter 3: The Intercalated Disc: A Focal Point for Sarcomere Growth and Disease -- 3.1 Introduction -- 3.2 Postnatal Heart Growth -- 3.2.1 Proliferation and Hypertrophy -- 3.2.2 Morphology of Cardiomyocytes During Growth -- 3.2.3 Cardiomyocyte Connections -- 3.3 Myofibril Formation and Growth -- 3.3.1 Early Formation of Myofibrils -- 3.3.2 Evidence for Fibril Growth at the Ends of Myocytes -- 3.4 Structure of the Intercalated Disc -- 3.4.1 General Organisation -- 3.4.2 ID Membrane: Domains and Connections -- 3.4.3 The ID as Z-Disc: The Transitional Junction.
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3.5 The ID/Transitional Junction in Longitudinal Growth -- 3.5.1 Variation of ID Amplitude -- 3.5.2 Sarcomere Insertion -- 3.5.3 Mechanism of Sarcomere Addition -- 3.5.4 SR Extension and T-Tubule Addition -- 3.5.5 Lateral Growth of the ID -- 3.6 The ID in Disease -- 3.6.1 Hypertrophic Cardiomyopathy -- 3.6.2 Dilated Cardiomyopathy and the Adherens Junction -- 3.6.3 Arrhythmic Right Ventricle Cardiomyopathy and the Desmosome -- 3.6.4 Gap Junction Disorders -- 3.6.5 Brugada Syndrome and Non-junctional Domain Cardiomyopathies -- 3.7 Conclusion -- References -- Chapter 4: Dynamics of Actin in the Heart: Defining Thin Filament Length -- 4.1 Introduction -- 4.2 Major Components of the Thin Filament -- 4.3 Thin Filament Length Regulation -- 4.4 Capping Proteins: Tmod and CapZ -- 4.5 Stabilization of the Thin Filament -- 4.6 Dynamic Equilibrium Between G-Actin and F-Actin -- 4.7 Links Between Alternations in Thin Filament Components and Myopathies -- 4.8 Concluding Remarks -- References -- Chapter 5: Ca2+ Regulation of the Cardiac Thin Filament -- 5.1 Introduction -- 5.2 Ca2+-Induced Ca2+ Release -- 5.3 Sarcomere Function -- 5.4 Sarcomere Structure -- 5.5 Tropomyosin and the Steric Blocking Model -- 5.6 Troponin: The Ca2+ Switch -- 5.7 Troponin C -- 5.8 Troponin I -- 5.9 Troponin T -- 5.10 Phosphorylation -- 5.11 Ischemic Insult and the Thin Filament -- 5.12 Histidine Modified Troponin I -- References -- Chapter 6: Posttranslational Modification of the Titin Springs: Dynamic Adaptation of Passive Sarcomere Stiffness -- 6.1 The Sarcomeric Protein Titin: Regulator of Myofilament Stiffness -- 6.2 Dynamic Modulation of Titin by Phosphorylation -- 6.2.1 Z-Disk and M-Band Phosphorylation -- 6.2.2 I-Band Phosphorylation of Titin -- 6.3 Regulation of Titin Phosphorylation in Health and Disease -- 6.3.1 Altered Titin Phosphorylation in Heart Failure.
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6.3.2 Hormonal Influences on Titin Phosphorylation: Relevance for Metabolic Diseases -- 6.4 Posttranslational Modification of Titin in Response to Oxidative Stress -- 6.5 Conclusions -- References -- Chapter 7: The M-Band: Not Just Inert Glue but Playing an Active Role in the Middle of the Sarcomere -- 7.1 The M-Band Is Part of the Sarcomere Cytoskeleton -- 7.2 M-Band Function: Balancing the Forces in the Contracting Sarcomere -- 7.3 Structure of the M-Band as Studied by Electron Microscopy -- 7.4 The Myomesin Protein Family -- 7.5 Myomesin Protein Family: Dimers That Cross-Link Myosin Filaments -- 7.6 Alternative Splicing of Myomesin -- 7.7 Correlation of M-Band Appearance and Molecular Composition -- 7.8 Other M-Band Components -- 7.9 What Happens if Myomesin Is Stretched -- 7.10 Signalling from the M-Band -- 7.11 The M-Band and Disease -- 7.12 Conclusion -- References -- Chapter 8: Sarcomeric Signaling -- 8.1 Introduction -- 8.2 Mechanotransduction -- 8.2.1 Titin and Associated Signaling Pathways -- 8.2.2 Telethonin/T-Cap -- 8.2.3 Muscle Lim Protein -- 8.2.4 LRRC39/Myomasp -- 8.3 Protein Degradation and Turnover -- 8.3.1 Muscle-Specific RING Finger Proteins -- 8.3.2 F-Box and Leucine-Rich Repeat Protein 22 -- 8.3.3 Atrogin-1 -- 8.3.4 Calpains -- 8.4 Oxidative Stress -- 8.4.1 Direct Modification of Sarcomeric Proteins -- 8.4.2 Modification of Sarcomeric Proteins by ROS-Sensitive Enzymes -- 8.4.3 ROS-Induced Cleavage of Sarcomeric Proteins -- 8.5 Phosphatases and Kinases -- 8.5.1 Calcineurin and Modulators of the Calcineurin Pathway -- 8.5.2 Protein Kinase C -- 8.6 Conclusion -- References -- Chapter 9: The Nuclear Envelope in Cardiac Health and Disease -- 9.1 Introduction -- 9.1.1 Nesprins and the ONM -- 9.1.2 SUN Domain Proteins -- 9.1.3 Lamins and the INM -- 9.1.4 Nuclear Envelopathies -- 9.1.5 The LINC Complex in Cardiomyocytes.
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9.2 The Role of the NE in Cardiac Disease -- 9.3 Mechanistic Insights into NE-Associated Cardiomyopathy -- 9.3.1 Mechanical Efficiency and Structural Instability -- 9.3.2 Mechanosignalling and Gene Regulation -- 9.3.3 Intercalated Disc Disorganisation -- 9.3.4 Autophagy and Related Signalling Mechanisms -- 9.3.5 Mitogen-Activated Protein Kinase Signalling -- 9.3.6 Other Signalling Pathways Deregulated by Perturbations to the NE -- 9.4 Premature Ageing and Cardiomyopathy -- 9.4.1 Therapeutic Potential -- 9.4.2 Prelamin A and `Premature Cardiac Senescence´ -- 9.5 Summary -- References -- Chapter 10: AMP-Activated Protein Kinase: A Metabolic Stress Sensor in the Heart -- 10.1 Evolving Physiological Roles -- 10.2 Molecular Structure -- 10.3 Localization -- 10.4 Activation -- 10.5 Regulation -- 10.6 Cardiac Signaling in Health and Disease -- 10.7 Pharmacological Activation -- 10.8 Concluding Remarks -- References -- Chapter 11: How Cardiac Cytoarchitecture Can Go Wrong: Hypertrophic Cardiomyopathy as a Paradigm for Genetic Disease of the He... -- 11.1 Introduction -- 11.2 Complexity Beyond One Mutation, One Gene, One Phenotype -- 11.3 Hypertrophic Cardiomyopathy -- 11.3.1 Clinical Features and Therapeutic Options -- 11.3.2 Genetics of HCM -- 11.3.2.1 Sarcomeric HCM Mutations -- 11.3.2.2 Mutations in Non-contractile Proteins Causing HCM -- 11.3.2.3 Phenocopies of HCM and Mitochondrial Disease -- 11.3.3 Pathomechanisms of HCM -- 11.4 Next-Generation Sequencing: `Opening Pandora´s Box´? -- References -- Chapter 12: Cardiac Cytoarchitecture: How to Maintain a Working Heart-Waste Disposal and Recycling in Cardiomyocytes -- 12.1 Cellular Degradation Systems -- 12.1.1 The Ubiquitin-Proteasome System -- 12.1.2 Autophagy/Lysosome -- 12.1.3 Proteases -- 12.1.3.1 Matrix Metalloproteinases -- 12.1.3.2 Cathepsins -- 12.1.3.3 Calpains -- 12.1.3.4 Caspases.
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12.1.3.5 Mitochondrial Proteases -- 12.1.4 Chaperones and Heat-Shock Proteins -- 12.1.5 Cooperativity Between Degradation Systems -- 12.2 Roles of Degradation Systems in the Heart -- 12.2.1 Balance Synthesis/Degradation -- 12.2.2 Protein Quality Control and the ERAD System -- 12.2.3 The Role of Substrate-Ubiquitylation Beyond Degradation -- 12.2.4 Cardiac-Specific Adaptations of the Degradation Machineries -- 12.2.5 The Cardiac Degradation Process -- 12.3 E3-Ligases with Cardiac Roles -- 12.3.1 MuRF Protein Family -- 12.3.2 Cullin-Type E3-Ligases -- 12.3.2.1 Regulation -- 12.3.2.2 Cullin1-Atrogin1 -- 12.3.2.3 Other Cullin-1 Substrate Adaptors -- 12.3.2.4 Cullin-2 -- 12.3.2.5 Cullin-3 -- 12.3.2.6 Cullin-4 -- 12.3.2.7 Cullin-5 -- 12.3.2.8 Cullin-7 -- 12.3.3 Other RING-Type E3-Ligases -- 12.3.3.1 Parkin -- 12.3.3.2 IAPs -- 12.3.3.3 Nrdp1/RNF41 -- 12.3.3.4 MDM2, MDM4/MDMX -- 12.3.3.5 Cbl -- 12.3.4 HECT-Type E3-Ligases -- 12.3.4.1 Nedd4 E3-Ligases -- 12.3.4.2 Ube3a/E6AP -- 12.3.5 U-Box-Type E3-Ligases -- 12.3.5.1 Ube4A -- 12.3.5.2 PRP19 -- 12.3.5.3 CHIP (C-Terminus of HSP70-Interacting Protein) -- References.
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