The role of misfolded proteins in neurodegenerative diseases pathology

Belačić, Katarina (2016) The role of misfolded proteins in neurodegenerative diseases pathology. Bachelor's thesis, Faculty of Science > Department of Biology.

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Abstract

In order to fulfill their various biological roles, proteins must fold into precise three-dimensional structure. Failure to fold properly can either cause a loss of normal function, mislocalization, improper degradation, structural alterations that establish novel toxic functions and/or acumulation of protein aggregates inside or outside the cell. Many pathological conditions are fundamentally rooted in the protein folding problem. Recent evidence indicates that diverse neurodegenerative diseases for a common cause and pathological mechanism have misfolding, aggregation and acumulation of proteins in the brain resulting in neuronal apoptosis. The aim of this report was to review the existing knowledge of the molecular mchanisms and causes of protein misfolding and aggregation, cell methods for combating this problem, its role in neurodegeneration and the potential targets for therapeutic intervention in neurodegenerative diseases. Neurodegenerative diseases are associated with the acumulation of misfolded proteins inside and outside of the neuronal and glial cells in the central nervous system. Three hypothesis have been proposed to explain how protein misfolding and aggregation might be associated with neurodegeneration: the loss-of function hypothesis, the gain-of toxic function hypothesis and the brain inflammation hypothesis. Despite impressive progress in understanding the pathogenesis of neurodegenerative diseases, none of this disorders can be successfully treated.

Item Type: Thesis (Bachelor's thesis)
Supervisor: Gruić-Sovulj, Ita
Date: 2016
Number of Pages: 41
Subjects: NATURAL SCIENCES > Biology
Divisions: Faculty of Science > Department of Biology
Depositing User: Palma Dizdarevic
Date Deposited: 11 May 2017 08:11
Last Modified: 11 May 2017 08:11
URI: http://digre.pmf.unizg.hr/id/eprint/5511

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