Christiane Richter-landsberg

Heat Shock Proteins in Neural Cells - Neuroscience Intelligence Unit Christiane Richter-landsberg 2009 edition

Marc Notes: Includes bibliographical references and index.; Published in association with Springer Science+Business Media, New York, NY. Table of Contents: Preface -- 1. Heat Shock Proteins: Expression and Functional Roles in Nerve Cells and Glia / Christiane Richter-Landsberg -- Introduction -- Heat Shock Proteins in Nerve Cells and Glia -- Concluding Remarks -- 2. Small Heat Shock Proteins and the Cytoskeleton: Their Role in Inclusion Body Formation in Glial Cells / Christiane Richter-Landsberg, Olaf Goldbaum -- Introduction -- The Cytoskeleton in Nerve Cells and Glia -- Interaction of Small Heat Shock Proteins with Cytoskeletal Proteins -- sHSPs and Inclusion Body Formation in Glial Cells -- Concluding Remarks -- 3. The Role of Hsps in Neuronal Differentiation and Development / Kate Reed Herbert, Afshin Samali, Adrienne Gorman -- Introduction -- Hsp Expression during Development of the Nervous System -- Transcriptional Regulation of Hsp Expression during Neuronal Development and Differentiation -- Possible Roles of Hsps in Neuronal Differentiation and Development of the Nervous System -- Concluding Remarks -- 4. Heme Oxygenase as a Therapeutic Funnel in Nutritional Redox Homeostasis and Cellular Stress Response: Role of Acetylcarnitine / Vittorio Calabrese, Giovanni Pennisi, Menotti Calvani, D. Allan Butterfield, Cesare Mancuso, Anna Maria Giuffrida Stella -- Introduction -- Heme Oxygenase-1 -- HO-1, Oxidative Stress and Neurodegenerative Disorders -- Acetylcarnitine -- Conclusions and Perspectives -- 5. Heat Shock Proteins and the Regulation of Apoptosis / Una FitzGerald, Adrienne M. Gorman, Afshin Samali -- Introduction to Apoptosis -- Hsp27 and Hsp70, the Anti-Apoptotic Heat Shock Proteins -- Apoptosis, Hsps and Neurodegenerative Disorders -- Concluding Remarks -- 6. Assembly of Protein Aggregates in Neurodegeneration: Mechanisms Linking the Ubiquitin/Proteasome Pathway and Chaperones / Sha-Ron Pierre, Vita Vernace, Zhiyou Wang, Maria E. Figueiredo-Pereira -- Introduction -- Protein Degradation by the UPP -- Potential Mechanisms for the Formation of Ubiquitin-Protein Aggregates -- Subcellular Distribution of Ubiquitin-Protein Aggregates -- Concluding Remarks -- 7. The Role of Heat Shock Proteins during Neurodegeneration in Alzheimer's, Parkinson's and Huntington's Disease / Andreas Wyttenbach, Andre Patrick Arrigo -- Introduction -- Common Mechanisms Leading to Impaired Neuronal Function and Death and the Role of HSPs -- Heat Shock Proteins and Therapy -- Conclusions -- 8. Heat Shock Proteins in Multiple Sclerosis / Celia F. Brosnan, Luca Battistini, Krzysztof Selmaj -- Introduction -- The Small Heat Shock Proteins -- The HSP60 Family -- The HSP70 Family -- Concluding Remarks -- Index. Publisher Marketing: eat shock proteins (HSPs), also called stress proteins, are not only induced in response to elevated temperatures, but also as a result of various stress situations, including environmental strains, viral H infection, ischemia, anoxia and oxidative stress. These stress situations trigger cellular defence mechanisms that act as an emergency system capable of combatting the toxic consequences due to the accumulation of misfolded proteins. Heat shock proteins are involved in many physiological processes, including development and differentiation, organisation of the cytoarchi tecture by binding to cytoskeletal elements and regulation of the balance between cell death and survival. Many heat shock proteins work as molecular chaperones. In this role, they contribute to in vivo protein folding and prevent nonproductive interactions with other proteins and cellular c- ponents. In recent years it has been found that the chaperone system and the proteolytic machinery work closely together, and that proteasomal - hibition causes the upregulation of stress proteins. Impairment of the proteasomal machinery and chaperone functions lead to protein damage, which contributes to neurodegenerative disorders and to the aging process.