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* Protein Folding and Misfolding: Neurodegenerative Diseases -- Ovadi J., Orosz F. --
Кураторы темы:* Luchkina
Операции: Хочу стать куратором* · Подписаться на тему* · Отправить страницу по e-mail · Версия для печати*
Внешний вид:* Схема · [ Стандартный ] · +Перв.сообщ.
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 Luchkina |
 06.01.2009 20:14
 Protein Folding and Misfolding: Neurodegenerative Diseases  Focus on Structural Biology кн.7 Ред. Ovadi J., Orosz F. Springer-Verlag; 2009; 277стр.; ISBN: 1402094330 The worldwide ageing of populations has brought the neurodegenerative diseases into the focus of interest. These diseases constitute large variety of pathological conditions originating from the slow, irreversible and systemic loss of cells in different regions of the brain resulting in degenerative problems with distinct clinical symptoms. The pathological behaviors are frequently associated with “proteinopathies”, the non-physiological behavior of a specific protein, affecting its processing, functioning, and/or folding. These proteins do not have stable tertiary and/or secondary structures in vivo; they enter into aberrant interactions affecting their folding state and function. A number of the diverse human neurodegenerative diseases are now recognized as conformational diseases because these are caused by aggregations of unfolded or misfolded proteins. Knowledge on the intrinsically unstructured proteins, a relatively newly recognized family of gene products as well as on the misfolded proteins produced by genetic mutations or environmental effects has been extensively accumulated in the past years. These proteins frequently cause proteolytic stress and/or enter into aberrant, non-physiological protein–protein interactions leading to sequestration of protein aggregates which are assemblies of many not-yet-identified components in addition to the deposition of well-characterized misfolded peptides and proteins. Such fate is known in the cases of Aв peptide and tau protein in Alzheimer’s disease, б-synuclein in Parkinson’s disease, the extended polyglutamine stretch of mutant huntingtin in Huntington’s disease and the prion protein in prion diseases. These protein assemblies display diverse ultrastructures such aggresomes, fibers, oligomers or amorphous structures, however, the nature of these species concerning their cytoprotective or cytotoxic effects has not been clarified yet. The understanding of the course and pathomechanism of the diseases arising from interactions of the so called malfolded proteins is crucial for finding effective therapeutic interventions. The identification of aberrant protein-protein interaction(s) playing constitutive role in aggregate formation contributes to the development of new pharmacofors that could prevent or circumvent the development of neurodegenerative disorders in human. The main focus of this issue is to review the molecular events initiated by unfolded or misfolded proteins leading to cell death via the development of pathological inclusions, with special emphasis on the macromolecular associations of the malfolded proteins into characteristic ultrastructures found in the cases of neurological disorders, some of them are shown in this issue. There are papers which uncover in details the intriguing interconnections between intrinsic disorder and human neurodegenerative diseases; the characterization of the diseases in relation to their hallmark proteins and ultrastructures. Other papers provide conceptual background of the molecular mechanism of the tendency of disordered proteins for aggregation in vitro and in vivo connected with misfolding diseases. Due to the fundamental biological importance of protein aggregates, and our poor knowledge about the molecular basis or specificity of the general phenomenon of protein aggregation, this problem will be specifically discussed. In the light of the protein based neuropathology the classification of the human neurodegenerative diseases is presented. This book also reviews the structural knowledge accumulated for well-studied and for newly discovered proteins involved in paradigmatic conformational disorders with the aim to broaden our understanding of the pathomechanisms of neurodegeneration, which is crucial for finding effective therapeutic interventions that could prevent or circumvent the development of neurodegenerative disorders in humans. |
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Pupis гость |
 06.01.2009 20:18
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