WAY overdue....sorry folks

Current location: 30 minutes from Spooner, WI, sitting on the patio overlooking the lake, celebrating Amuricuh day (the 4th). Considering the last post was well over a month ago, it may be well to admit that I'm not ready for the responsibility of having a dog, despite wanting one. So this is way overdue, but I've got a lot to talk about (even some science!) - here we go!

The last month has been absolutely INSANE. Fun, busy but absolutely INSANE. The CliffsNotes version, more or less in chronological order:

1. First lab rotation begun and finished
2. Fully moved into the new house
3. New roommate (Erich)
4. Trivia nights on Mondays
5. Eric Clapton live at Summerfest
6. Bought my first car
7. Ramani's engagement!
8. 4th of July reunion with the old roommates (and Kelly and Kim joined us, too!)

So, much has been going on. The big news is the first lab rotation:
I spent about 5 weeks in Dr. Park's lab in the department of biochemistry, studying the MAP Kinase (MAPK) pathway in cancer. Essentially, this is a series of proteins that are responsible for activating the ones below them, creating a chain reaction when the cell is properly stimulated. This translates into instructions for the cell to either replicate, stop dividing (senescence) or die (apoptosis). As one can imagine, this is hugely important in cancer, as the name of the game is get cells that are rapidly multiplying to senesce or, better yet, die. One of the big questions in the field is how this pathway can signal these opposing outcomes with the same machinery and activation. Think about it this way: you have one light switch and by flipping it you can either turn on a fan in one corner or turn on the light overhead. The lab recently found that one of the key proteins in the pathway, ERK, has both catalytic and, interestingly, non-catalytic functions, which may explain why this is possible.

So where do I fit into all of this? Well, I spent the last 5 weeks investigating the function of a drug that is currently in use clinically to induce cell death. They have found the drug to already be very effective in inducing apoptosis in cells that have a mutation in the RAF protein. However, in cancer where this mutation is not present, the drug causes the cells to hyper-proliferate (ruh roh, Shaggy!). So my job was to see if we can use this drug on RAF-normal cells. This is a fancy way of saying I cultured up tons of cells, treated them with the drug, collected protein samples and measured what happened to protein function in the MAPK pathway. Here is an example of some pretty neat biochemistry and ingenuity: how do you separate all of one protein from literally tens of thousands in a total protein sample? Well, it's actually pretty simple, and we do it every day in the lab. First, the cells are broken apart with detergent, allowing us to access the proteins inside. These proteins are then placed into a gel much like Jell-O (but not for eating) and separated by size using electrical charge. So, now the proteins are all spaced out, big huge ones at the top, small ones at the bottom, and everything else between. This sample is then transferred to another apparatus where the proteins are pulled out of the gel and put onto a membrane using, again, electrical charge. Now here is where things get really neat. For anyone who has ever been sick (i.e., all of you), your body developed antibodies for whatever it was that made you sick. Essentially, these antibodies recognize the proteins that are expressed on the outside of the bug you had. Somewhere, someone got a really good idea - these antibodies are VERY good at recognizing a VERY specific protein sequences. So, what if you inject protein, say ERK, into a rabbit? It will develop antibodies that are specific to just ERK! Collect a blood sample from the rabbit, separate the antibodies, and viola, you have an antibody for that protein that you can apply to the membrane! And, it gets even better! So now you have a whole sheet of proteins on the membrane, and all the ERK proteins have antibodies stuck to them. Now get another antibody, say from a goat, that targets rabbit antibodies. While you're at it, add a light-emitting molecule to the antibody and you'll be able to see the proteins on a long exposure camera or undeveloped film. Pretty neat, hey?

So that was 5 weeks, and there are some results that do look a bit promising. It's up to Johnathan, the next rotation student (and fellow MSTPer + past BTRL member) to pick up the project and make it shine. So, good luck to him, hope I didn't leave too big a mess for you, buddy.

So what else? Well, the house is all set up (whew!) and we're getting along great. Back to family dinners with the roommates and FIFA World Cup games on the weekends. Getting back into a rhythm of things, and it's good.

Of course, the really big news is that my sister, Ramani, is engaged! Emmanuel came to Milwaukee earlier this month to spend a weekend and popped the question...she said YES! Needless to say, we're all very excited and wish them the best. Stay tuned for more details and dates.

So that's it for now. And yes, this post was written on the 4th and published on the 17th. I know I'm behind, but whatever. I'll fill you in on Gauld Lab (new rotation) happenings in a short bit. But this should be enough (er, overload) for now.