Matrix metalloproteinases in the central nervous system

Matrix metalloproteinases in the central nervous system /

This book presents the reader with an understanding of the role played by matrix metalloproteinases (MMPs) in the normal and diseased central nervous system (CNS). These enzymes may be important to brain development, and may also contribute to tissue destruction, which is observed with inflammatory...

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Bibliographic Details
Online Access: Full text (MCPHS users only)
Other Authors: Conant, Katherine, Gottschall, Paul E.
Format: Electronic eBook
Language:English
Published: London : Hackensack, NJ : Imperial College Press ; Distributed by World Scientific, 2005
Subjects:
Metalloproteinases.
Metalloproteinases > Inhibitors.
Central nervous system.
Extracellular matrix proteins.
Matrix Metalloproteinases > biosynthesis
Central Nervous System > cytology
Central Nervous System > physiology
Matrix Metalloproteinases > physiology
Tissue Inhibitor of Metalloproteinases > biosynthesis
Tissue Inhibitor of Metalloproteinases > physiology
Metalloproteases
Central Nervous System
Local Note:ProQuest Ebook Central
Table of Contents:
  • Cover
  • Contents
  • Foreword
  • I.A Brief Overview
  • Chapter 1. The Matrix Metalloproteinases and Their Inhibitors Madeleine M. Handsley, Janet Cross, Jelena Gavrilovic, and Dylan R. Edwards
  • 1. Introduction
  • 2. The MMP Family
  • 3. Regulation of MMP Activity
  • 4. Endogenous Inhibitors of Metalloproteinases
  • 5. Novel Roles for MMPs
  • 6. ECM Targets in the CNS
  • 7. Generation of Matricryptic Sites in ECM Components
  • 8. Growth Factor Liberation from ECM 8220;Stores
  • 9. Chemokine Gradient Generation
  • 10. Blood-Brain Barrier Substrates for MMPs
  • 11. Conclusion
  • References
  • II. Regulation of MMP Expression
  • Chapter 2. Genetic Regulation of the Matrix Metalloproteinases and Related Proteins Tammie Roy and Elizabeth A. Milward
  • 1. Introduction
  • 2. Stimuli Triggering Alterations in MMP Gene Expression
  • 3. Alterations in Other MMPs
  • 4. Neurotransmitters
  • 5. Cell-Cell and Cell-Matrix Interactions
  • 6. Physical and Biochemical Stress
  • 7. Suppressive Factors
  • 8. Feedback Control
  • 9. Signalling Cascades Involved in Regulating MMP Gene Expression
  • 10. Genetic Elements Regulating MMP Gene Expression
  • 11. Regulation of the MMP-2, MMP-11 and MMP-14 (MT1-MMP) Genes
  • 12. Regulation of ADAMs Family Gene Expression
  • 13. Regulation of TIMP Gene Expression
  • 14. Inverse Regulation of MMPs and TIMPs
  • 15. Regulation of TIMPs Independent of MMP Inhibitory Functions
  • 16. Post-Transcriptional Regulation of MMP Expression
  • 17. Regulation of MMP Gene Expression in the Healthy Nervous System
  • 18. Neuronal Expression
  • 19. Astrocyte Expression
  • 20. Microglial Expression
  • 21. Endothelial and Other Cells
  • 22. Oligodendrocyte and Schwann Cell Expression
  • 23. Expression of TIMPs in the Nervous System
  • 24. Expression in Nervous System Development and Plasticity
  • 25. MMP Gene Regulation in Nervous System Injury and Disease
  • 26. Regulation in Nervous System Malignancies
  • 27. Regulation in Nervous System Injury
  • 28. Genetic Polymorphisms and MMP Expression
  • 29. Conclusion
  • References
  • Chapter 3. Post-Translational Modification Zezong Gu, Marcus Kaul, and Stuart A. Lipton
  • 1. Introduction
  • 2. Cysteine Switch Mechanism
  • 3. Modification of MMPs by S-Nitrosylation
  • 4. S-Nitrosylation Leads to MMP-9 Activation In Vitro
  • 5. NO-Induced Subsequent Oxidation
  • 6. Peptide Mass Fingerprinting Analysis of Cysteine Residue Post-Translational Modifications
  • 7. Structural Model of S-Nitrosylation of MMPs
  • 8. MMPs in Neurological Diseases
  • 9. Neuronal NOS-Associated Activation of MMP During Stroke
  • 10. Exogenous NO-Activated MMP-9 Induces Neuronal Apoptosis in Cerebrocortical Cultures
  • 11. MMPs Degrade Extracellular Matrix Components
  • 12. Summary
  • Acknowledgments
  • References
  • III. MMP Function
  • Chapter 4. Substrates for Metalloendopeptidases in the Central Nervous System Paul E. Gottschall, John D. Sandy, and Dieter R. Zimmermann
  • 1. Introduction
  • 2. Substrates in the Basal Lamina (Basement Membrane)
  • 3. Collagen Type IV
  • 4. Laminins
  • 5. Perlecan and Other Heparan Sulfate Proteoglycans (HSPG)
  • 6. Entactins (Nidogens)
  • 7. Substrates in the Neuropil and Perineuronal Nets
  • 8. Proteoglycans
  • 9. Hyalectans (Lecticans, Aggregating PGs)
  • 10. Expression, Localisation and Molecular/Cellular Interactions
  • 11. Proteolytic Pr.

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