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HSP70/HSP40 Chaperones, involved in the Protein Quality Control System, suppressing Toxic Protein Aggregation

Eenjes, E. (2010) HSP70/HSP40 Chaperones, involved in the Protein Quality Control System, suppressing Toxic Protein Aggregation. Bachelor's Thesis, Biology.

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Abstract

Many neurodegenerative diseases are characterized by the accumulation of misfolded proteins, which results in loss of function of the particular proteins and may lead to neuronal cell death. Chaperones (HSPs) are highly involved in the protein quality control system and maintain protein homeostasis in the cell. HSP70 and its co-factor HSP40 play a major role in protein folding, refolding and degradation. The HSP70/HSP40 complex protects nascent proteins from misfolding and aggregation as well. HSP40 stimulates ATPase activity of HSP70 by increasing the rate of ATP hydrolysis. Several studies showed that overexpression of HSP70 with HSP40, in models transfected with a plasmid coding for a neurodegenerative disease, suppresses aggregate formation in vitro ( Evans et al., 2006, Kobayahi et al., 2000) and in vivo (Cummings et al., 2001, Chan et al., 2000). Overexpression of HSP40 family members alone show more or less anti-aggregation activity dependent on the protein model or which family member of HSP40 was overexpressed. DNAJB6 (MRJ), a family member of HSP40, showed anti-aggregation activity in several in vitro studies (Chuang et al., 2002). DNAJB6 suppresses toxicity in in vivo studies also (Fayazi et al., 2006). DNAJB6 together with DNAJB8 show anti-aggregation activity independent of HSP70 (Hageman et al., 2010). The anti-aggregation activity of these chaperones gives expectations for the use of chaperones for the protection against aggregation in protein misfolding disorders. This study explores the role of HSP70 and HSP40 in the protein quality control system and their anti-aggregation function in different cell models.

Item Type: Thesis (Bachelor's Thesis)
Degree programme: Biology
Thesis type: Bachelor's Thesis
Language: English
Date Deposited: 15 Feb 2018 07:31
Last Modified: 15 Feb 2018 07:31
URI: http://fse.studenttheses.ub.rug.nl/id/eprint/9154

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