Molecular Chaperones in Health and Disease
Molecular chaperones are involved in a wide variety of essential cellular processes in living cells. A subset of molecular chaperones have been initially described as heat shock proteins protecting cells from stress damage by keeping cellular proteins in a folding competent state and preventing them from irreversible aggregation. Later it became obvious that molecular chaperones are also expressed constitutively in the cell and are involved in complex processes such as protein synthesis, intracellular protein transport, post-translational modification and secretion of proteins as well as receptor signalling. Hence, it is not surprising that molecular chaperones are implicated in the pathogenesis of many relevant diseases and could be regarded as potential pharmacological targets. Starting with the analysis of the mode of action of chaperones at the molecular, cellular and organismic level, this book will then describe specific aspects where modulation of chaperone action could be of pharmacological and therapeutic interest.
Molecular Aspects of the Stress Response
We are extremely happy to present the reader this book containing a summary of a well-known research field, the phenomenon of cellular stress defense from two new angles: networks and membranes.
Heat Shock Proteins and the Brain : Implications for Neurodegenerative Diseases and Neuroprotection
Neurodegenerative disorders such as Alzheimer’s disease, Huntington’s disease, Parkinson’s disease and amyotrophic lateral sclerosis have been termed ‘protein misfolding disorders’ that are char- terized by the neural accumulation of protein aggregates. Manipulation of the cellular stress response involving the induction of heat shock proteins offers a the- peutic strategy to counter conformational changes in neural proteins that trigger pathogenic cascades resulting in neurodegenerative diseases. Heat shock proteins are protein repair agents that provide a line of defense against misfolded, aggregati- prone proteins. Heat Shock Proteins and the Brain: Implications for Neurodegenerative Diseases and Neuroprotection reviews current progress on neural heat shock proteins (HSP) in relation to neurodegenerative diseases (Part I), neuroprotection (Part II), ext- cellular HSP (Part III) and aging and control of life span (Part IV).
Fundamentals of Protein Structure and Function
This book serves as an introduction to the fundamentals of protein structure and function. Starting with their make up from simple building blocks called amino acids, the 3-dimensional structure of proteins is explained. This is followed by an introduction into enzymology and modern concepts of enzyme kinetics, taking into account the physiological and medical significance of this often neglected topic.
Lysosomes
This book summarizes the current state-of-the art knowledge about this unique organelle. It addresses the biogenesis of this compartment, the transport of lysosomal proteins, the role of the lysosomal membrane in lysosomal stability and transport, the function of lysosomal proteases and hydrolases, lysosomal storage disorders, and new concepts on how to treat these diseases.
Chromatin and Disease
It is more evident now than ever before that dynamic organization of human genome into nucleoprotein structure, chromatin confers the unique regulatory mechanisms for most of the cellular phenomena, which include replication, transcription, DNA repair, recombination and also apoptosis. The dynamic nature of the chromatin is regulated by chromatin modifications (epigenetic alterations), remodeling, histone chaperones and functional interactions of different chromatin interacting n- histone proteins. Dysfunction of this highly inter connected machineries disturb the cellular homoeostasis, and thereby causes several diseases. As we advance in our knowledge of chromatin function and also disease mechanisms in more details, their causal relationship is becoming more evident. This has lead to the identification of chromatin function as target for new generation therapeutics.
Chaperones
Molecular chaperones interact with virtually every newly synthesized protein. Their role is not limited to this, as an increasing number of protein-protein interactions are found to be mediated by molecular chaperones. They reside in large complexes, in every cellular compartment, and to some extent even outside cells. These proteins are of interest to a large number of scientists, not only to those interested in protein biosynthesis, but also in relation to protein transport, organelle biogenesis, and cell stress.
Cell Stress Proteins
This comprehensive volume, written by experts in the field, provides a current understanding of the molecular properties of the heat shock proteins and their roles in health and disease. Cell Stress Proteins includes advances in several aspects of stress protein research, with chapters ranging from basic studies of the role of heat shock proteins in protein folding to reviews examining the breakdown of stress protein regulation during disease. It also provides analysis of the biochemical and molecular properties of heat shock proteins which can be utilized in evaluating their role in human physiology and pathology. Cell Stress Proteins is an ideal book for researchers, clinicians, physicians, and graduate students in the fields of biochemistry, cell biology, microbiology, immunology, and genetics.







