22 Sep A look into my own research project: molecular neuroscience at the faculty
For my Master’s in Neurobiology (track molecular Neuroscience) I am currently doing a research internship at the Smidt laboratory of the Swammerdam Institute for Life Sciences. Do you want to take a look in some of the research of our faculty and the good life of a researcher? Read on!
Parkinson’s disease at the molecular level
The research project I am part of, is concerned with Parkinson’s disease. The neurons of the substantia nigra, that die in the brain of Parkinson’s patients, are normally dopamine-producing neurons that are responsible for the control of body movement. The lack of dopamine causes various problems in the brain. An important enzyme in the process of dopamine production is tyrosine hydroxylase (TH), which produces L-DOPA, the precursor of dopamine. L-DOPA is currently used as a drug for Parkinson’s disease, but unfortunately it has very unpleasant side effects.
Less dopamine production: boost it!
Boosting the dopamine production in the remaining cells of the substantia nigra could help Parkinson’s disease patients, especially in an early stage. To do this, we are searching for ways to manipulate the enzymatic activity of tyrosine hydroxylase (TH) in such a way as to produce more dopamine. Another approach is to examine how TH is broken down in the cell, for example via ubiquitination. In this degradation process, a small protein called ubiquitin is attached to a protein. Ubiquitin serves as a tag that is recognized by the proteasome, which breaks the protein down into little pieces. If we find out how this works, it may be possible to prevent degradation of TH. Less degradation of TH will mean more dopamine production!
Off to the lab
One of the things I am trying to investigate in the lab is how degradation of the enzyme tyrosine hydroxylase (TH) is regulated in the cell. To look at possible proteosomal degradation of TH, I am using dopaminergic cells that are growing in petri dishes. From those cells I isolate the TH protein by using a technique called immunoprecipitation. With this technique you basically fish for TH in your sample by using an antibody as your fishhook. Once the TH in your sample is attached to the antibody, you wash away the other stuff. To visualize the fished-out TH and the possibly present ubiquitin attached to it I use Western blotting. A Western blot is a way to separate proteins through a gel, transfer them onto a membrane and eventually visualize them by using an antibody that produces light.
Why science makes you fat
The Smidt lab is a friendly and inspiring environment to work in. There are always experienced researchers in the lab that are willing to help you out or answer your questions. The weekly work meetings really force you to think critically about your own research and that of others.
During lab drinks, game nights or wine tastings, it’s time for less serious stuff or for designing an extremely creative new research approach with the help of some alcohol. Another thing I learned at the Smidt lab it that researchers eat a lot of cake: birthday cake, paper-cake and cake for accepted grant proposals (money!), but also mistake-cake (which you have to bring when you did something extremely stupid in the lab) and of course ‘resultaart’, which is a pun on the Dutch words resultaat (result) and taart (cake), so this is cake you bring when you’ve found a big result. Fortunately, running around with your beeping timer, carrying huge bottles with buffers and all the pipetting help you to burn the extra calories.
Do you want to know more about my internship experiences at SILS? Ask your questions in the comments!