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Christiane Richter-Landsberg
University of Oldenburg
Oldenburg, Germany

About this book

Heat 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 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 cytoarchitecture 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 components. In recent years it has been found that the chaperone system and the proteolytic machinery work closely together, and that proteasomal inhibition 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.

The brain is the most sensitive target for traumatic events. Many disorders of the nervous system are caused by intracellular or extracellular deposits of protein aggregates. Stress responses in the brain, as monitored by the induction of heat shock proteins, occur in distinct regions and affect nerve cells and glia in a cell-type-specific manner. Hence, stress proteins may serve as biomarkers and provide diagnostic tools that allow us to identify stress specificity and localize pathological processes. Their critical involvement during neurodegeneration in brain disorders, such as Alzheimer’s, Parkinson’s and Huntington’s diseases, and multiple sclerosis, makes them promising candidates for therapeutic intervention and drug development.

Table of contents

1. Heat Shock Proteins: Expression and Functional Roles in Nerve Cells
and Glia
Christiane Richter-Landsberg

2. Small Heat Shock Proteins and the Cytoskeleton: Their Role in Inclusion
Body Formation in Glial Cells
Christiane Richter-Landsberg and Olaf Goldbaum

3. The Role of Hsps in Neuronal Differentiation and Development
Kate Reed Herbert, Afshin Samali and Adrienne Gorman

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 and Anna Maria Giuffrida Stella

5. Heat Shock Proteins and the Regulation of Apoptosis
Una FitzGerald, Adrienne M. Gorman and Afshin Samali

6. Assembly of Protein Aggregates in Neurodegeneration: Mechanisms Linking
the Ubiquitin/Proteasome Pathway and Chaperones
Sha-Ron Pierre, Vita Vernace, Zhiyou Wang and Maria E. Figueiredo-Pereira

7. The Role of Heat Shock Proteins during Neurodegeneration in Alzheimer’s,
Parkinson’s and Huntington’s Disease
Andreas Wyttenbach and André Patrick Arrigo

8. Heat Shock Proteins in Multiple Sclerosis
Celia F. Brosnan, Luca Battistini and Krzysztof Selmaj