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Abstract
Conformational Protein Diseases (CPDs) comprise over forty clinically and pathologically diverse disorders in which specific altered proteins accumulate in cells or tissues of the body. The most studied are Alzheimer's disease, Parkinson's disease, Huntington's disease, amyotrophic lateral sclerosis, prion diseases, inclusion body myopathy, and the systemic amyloidoses. They are characterised by three dimensional conformational alterations, which are often rich in β- structure. Proteins in this non-native conformation are highly stable, resistant to degradation, and have an enhanced tendency to aggregate with like protein molecules. The misfolded proteins can impart their anomalous properties to soluble, monomeric proteins with the same amino acid sequence by a process that has been likened to seeded crystallization. However, these potentially pathogenic proteins also have important physiological actions, which have not completely characterized. This opens up the question of what process transforms physiological actions into pathological actions and most intriguing, is why potentially dangerous proteins have been maintained during evolution and are present from yeasts to humans. In the present paper, we introduce the concept of mis–exaptation and of mis–tinkering since they may help in clarifying some of the double edged sword aspects of these proteins. Against this background an original interpretative paradigm for CPDs will be given in the frame of the previously proposed Red Queen Theory of Aging.
Keywords: Exaptation, tinkering, neurodegenerative diseases, prions, protein conformation, protein aggregation, aging
Current Protein & Peptide Science
Title:A New Interpretative Paradigm for Conformational Protein Diseases
Volume: 14 Issue: 2
Author(s): Luigi Francesco Agnati, Diego Guidolin, Amina S. Woods, Francisco Ciruela, Chiara Carone, Annamaria Vallelunga, Dasiel Oscar Borroto Escuela, Susanna Genedani and Kjell Fuxe
Affiliation:
Keywords: Exaptation, tinkering, neurodegenerative diseases, prions, protein conformation, protein aggregation, aging
Abstract: Conformational Protein Diseases (CPDs) comprise over forty clinically and pathologically diverse disorders in which specific altered proteins accumulate in cells or tissues of the body. The most studied are Alzheimer's disease, Parkinson's disease, Huntington's disease, amyotrophic lateral sclerosis, prion diseases, inclusion body myopathy, and the systemic amyloidoses. They are characterised by three dimensional conformational alterations, which are often rich in β- structure. Proteins in this non-native conformation are highly stable, resistant to degradation, and have an enhanced tendency to aggregate with like protein molecules. The misfolded proteins can impart their anomalous properties to soluble, monomeric proteins with the same amino acid sequence by a process that has been likened to seeded crystallization. However, these potentially pathogenic proteins also have important physiological actions, which have not completely characterized. This opens up the question of what process transforms physiological actions into pathological actions and most intriguing, is why potentially dangerous proteins have been maintained during evolution and are present from yeasts to humans. In the present paper, we introduce the concept of mis–exaptation and of mis–tinkering since they may help in clarifying some of the double edged sword aspects of these proteins. Against this background an original interpretative paradigm for CPDs will be given in the frame of the previously proposed Red Queen Theory of Aging.
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Cite this article as:
Francesco Agnati Luigi, Guidolin Diego, S. Woods Amina, Ciruela Francisco, Carone Chiara, Vallelunga Annamaria, Oscar Borroto Escuela Dasiel, Genedani Susanna and Fuxe Kjell, A New Interpretative Paradigm for Conformational Protein Diseases, Current Protein & Peptide Science 2013; 14 (2) . https://dx.doi.org/10.2174/1389203711314020006
DOI https://dx.doi.org/10.2174/1389203711314020006 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
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