Data di Pubblicazione:
2014
Citazione:
Biochemical and immunological aspects of protein aggregation in neurodegenerative diseases / F. Shojaei, N. Tavakolinia, A. Divsalar, T. Haertlé, A.A. Saboury, M. Nemat-Gorgani, M.P. Abbracchio. - In: JOURNAL OF THE IRANIAN CHEMICAL SOCIETY (PRINT). - ISSN 1735-207X. - 11:6(2014), pp. 1503-1512. [10.1007/s13738-014-0491-x]
Abstract:
Protein aggregation is commonly associated with a large number of neurodegenerative disorders such as Alzheimer's disease, Parkinson's disease, Huntington's disease, and other types of pathological conditions. Misfolding and aggregation of a number of peptides and proteins have been found to occur under these conditions. In the present review, some mechanistic features of the events related to the type of structure-function relationships which may define the outcome of the abnormal conditions are discussed. The immunological responses to the aggregates and possible therapeutic strategies for prevention or control of the diseases are also reviewed. Protein aggregation and its effect on human body have become an important issue over the last two decades. Many diseases in human are related to aggregation and misfolding of different kinds of proteins; therefore, diagnosis of causes of the aggregation and their mechanisms which provoke it are important. This review describes the relations between structures and functions of already aggregated proteins, as well as proteins, which only enter initial stages of aggregation. The consequences of aggregations, which provoke many kinds of neurodegenerative disorders, are explained in details and some factors that may influence their severity are described. In addition, the immunologic responses to these aggregates are discussed. Suggestions of plausible therapies of preventing or slowing down the protein condensation diseases are presented.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
Alzheimer; Neurodegenerative; Parkinson; Protein aggregation; Chemistry (all)
Elenco autori:
F. Shojaei, N. Tavakolinia, A. Divsalar, T. Haertlé, A.A. Saboury, M. Nemat Gorgani, M.P. Abbracchio
Link alla scheda completa: