Long time no see everyone!
It’s great to connect with everyone virtually after a while! Apologies for not posting a blog for some time. As I was spending some time with family and friends in Florida for the past week, I was unable to upload my blogs. BUT I promise I got work done over the past two weeks so let’s get into it!
For those of you who have kept up with my blogs, you will recall how I’ve been doing some research on the tumor suppressor protein p53 over the past few weeks. I intend to use this week’s blog to discuss any final notes I have on p53.
OPTIONAL: For those of you who would like to read about my earlier findings regarding p53, please use one of the links below:
As you all know, many human cancers (greater than 50%) carry loss of function mutations of p53. So, how do these mutations cause p53 to lose function?
- The DNA-binding domain is disrupted, preventing p53 from binding to DNA and activating the genes that it’s supposed to
- The tetramer is not formed at the COOH-terminal oligomerization domain preventing p53 from activating the genes it’s supposed to
- Example 1: L344P = monomeric form
- Example 2: R377C = weak tetramer
- Specific Case: p53Δc – lacks the oligomerization domain and nuclear localization signals resulting in lower pro-apoptotic activity
But some of you AP Bio students may be asking the following: if a substance within the body is non-functional, doesn’t the human body have the capability to degrade it? (i.e. apoptosis – programmed cell death)
When it comes to proteins, a process known as ubiquitination often initiates the degradation process of proteins. Unfortunately, when it comes to mutated p53, they are able to avoid degradation. Additionally, certain cancers, such as breast cancer, overexpress certain proteins that result in the rapid degradation of functional p53.
So, when it comes to my research on p53 there are some common conclusions I have come to:
- Wild-type p53 is mutated in over 50% of human cancers
- The presence of mutated p53 in cancerous patients prevents functional, wild-type p53 from actively working resulting in a lack of wild-type p53 in cancerous patients
Therefore, this is why many cancer patients require chemotherapeutics that supply them with functional, wild-type p53. The problem is that these drugs are often expensive, preventing many patients from acquiring them. Thus, my research to produce p53 using recombinant DNA technology serves the purpose of finding a way to mass produce p53 at low costs so they can be distributed easily to cancer patients around the globe.
That is all for this blog! While I often know what I’m going to be sharing next week, there are a lot of ways the following week could go. Stay tuned to find out what I will be doing. Thanks for reading, and stay tuned for another blog post coming later this week! Cheers!