Uloga pogrešno smotanih proteina u razvoju neurodegenerativnih bolesti

undergraduate thesis

• Title (english): The role of misfolded proteins in neurodegenerative diseases pathology
• Author: Katarina Belačić
• Mentor: Ita Gruić-Sovulj (mentor)
• Granter: University of Zagreb; Faculty of Science; (Department of Biology); Zagreb
• Defense date and country: 2016, Croatia
• Scientific / art field, discipline and subdiscipline: NATURAL SCIENCES; Biology

Abstract

Kako bi protein mogao izvršavati svoju biološku funkciju, on se mora pravilno smotati, odnosno zadobiti pravilnu trodimenzionalnu strukturu. Ako dođe do pogrešnog smatanja proteina kao posljedica može biti gubitak funkcije tog proteina, kriva lokalizacija unutar stanice, nepravilna razgradnja pogrešno smotanog proteina, promjena strukture kojom protein dobiva nova toksična svojstva i/ili akumulacija proteinskih agregata unutar ili izvan stanice. Mnoga patološka stanja kao izvor imaju problem pri smatanju proteina. Rezultati nedavnih istraživanja ukazuju da je mogući zajednički uzrok i patološki mehanizam različitih neurodegenerativnih bolesti pogrešno smatanje, agregacija i akumulacija proteina u mozgu koja rezultira apoptozom neurona. Cilj ovog završnog rada bio je istražiti postojeća saznanja o molekularnim mehanizmima i uzrocima pogrešnog smatanja i agregacije proteina, stanični odgovor na pogrešno smatanje i agregaciju proteina, uloga pogrešnog smatanja i agregacije proteina u neurodegeneraciji i potencijalnih ciljnih meta za terapiju neurodegenerativnih bolesti. Neurodegenerativne bolesti su povezane s akumulacijom pogrešno smotanih proteina unutar i izvan neurona i glija stanica u centralnom živčanom sustavu. Postavljene su tri hipoteze koje nastoje objasniti povezanost pogrešnog smatanja i agregacije proteina s neurodegeneracijom: hipoteza gubitka funkcije, hipoteza toksičnosti i hipoteza upale mozga kao posljedice pogrešnog smatanja i agregacije proteina. Unatoč velikom napretku u razumijevanju patogeneze neurodegenerativnih bolesti, dosada niti jedna nije izlječiva.

Abstract (english)

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.

• Keywords: proteini; neurodegenerativne bolesti
• Keywords (english): proteins; neurodegenerative diseases
• Language: croatian
• URN:NBN: urn:nbn:hr:217:976053
• Study programme: Title: Molecular Biology; Study programme type: university; Study level: undergraduate; Academic / professional title: sveučilišni/a prvostupnik/prvostupnica (baccalaureus/baccalaurea) molekularne biologije (sveučilišni/a prvostupnik/prvostupnica (baccalaureus/baccalaurea) molekularne biologije)
• Type of resource: Text
• File origin: Born digital
• Access conditions: Open access
• Created on: 2017-12-22 10:56:12