Ordelman, Valeska, V (2021) The role of zDHHC proteins in cancer. Master's Thesis / Essay, Biomedical Sciences.
|
Text
mBMS_2021_OrdelmanV.pdf Download (506kB) | Preview |
|
Text
toestemming.pdf Restricted to Registered users only Download (579kB) |
Abstract
S-acylation is a form of reversible post-translational modification. S-acylation, in other words, palmitoylation, is the attachment of a palmitate group via a thioester bond to the thiol group of a cysteine. Palmitoylation, is a process that is moderated by zDHHC (zinc finger domain containing aspartate-histidine-histidine-cysteine) enzymes. Palmitoylation of proteins affects the protein in several ways, it gives rise to alterations in the secondary structure which leads to altered functions of the proteins. In line with the important functions of palmitoylation, malformations in zDHHC proteins are likely to play a role in human diseases, including cancer. zDHHC proteins can either act as oncoproteins or as tumor suppressor proteins and in addition, some of them have been shown to have value as prognostic markers. Studies have shown that most of the zDHHC proteins seem to act as oncoproteins, with tumor suppressor functions for only 5 of the 23 zDHHC proteins. However, there is often a lack of functional evidence to confirm these observations. For zDHHC4, zDHHC6, zDHHC10, zDHHC12, zDHHC22, and zDHHC24 there is currently not enough data to support a role in cancer. Additionally, for zDHHC8 , zDHHC11, and zDHHC20 studies showed some controversial results when it comes to the classification of these proteins as oncoproteins or tumor suppressor proteins. Current knowledge on the role of zDHHC proteins in cancer development is far from complete. So, future research is needed to cr
Item Type: | Thesis (Master's Thesis / Essay) |
---|---|
Supervisor name: | Berg, J.H.M. van den |
Degree programme: | Biomedical Sciences |
Thesis type: | Master's Thesis / Essay |
Language: | English |
Date Deposited: | 28 Apr 2021 08:42 |
Last Modified: | 28 Apr 2021 08:42 |
URI: | https://fse.studenttheses.ub.rug.nl/id/eprint/24313 |
Actions (login required)
View Item |