Community-supported agriculture...

Ugh... two huge posts in a row. Sorry about that. Here's a shorter, less serious one.

Jenny, Chris, Minnie, and I joined together and bought a CSA farm share for the summer. For those ho don't know, CSA stands for "community-supported agriculture" and is a program that lets you buy a share of the crops produced by a local farm.

We picked the Women's Environmental Institute in North Branch, MN. Every week, they send a box full of fresh veggies to a drop of location and we pick it up. I had originally planned to take a picture of each box and post an update every week, but that just didn't happen. We're now on our 10th week and I've only photographed the first -- and smallest -- bundle of produce:



This lovely spread contains lettuce, kohlrabi, green onions, marjoram, a riot pepper plant, broccoli, and beets. All delicious. Since then, the boxes have become heavier and have included cabbage, leeks, basil, sweet corn, cauliflower, and more.

I even planted those peppers, and they're doing great. I think one of the many peppers that have sprouted is nearly ripe, and I might give it a try pretty soon.

The farm also has a salsa-making party this weekend. I think I should go.

Michelle Bachmann does a barking clown dance...

I just got done weeping for humanity listening to Michelle Bachmann talking about health care reform on MPR. Besides making a number of sweeping generalizations about how a public option will inevitably lead to gov't takeover, she also dropped a few other republican talking points poo logs golden gems:

Bachmann told Cathy Wurzer that "rationing is most definitely part of this bill... a lot of what this bill is about is having these various boards make decisions about reducing options and reducing care..." On her own website, she quotes Newt Gingrich:

"The inevitable result of this pressure to control costs will be rationing, whether it occurs during this administration or the next. At some point, the government will be forced to deny care to those who don’t meet the latest “quality-adjusted life years” cost-benefit analysis.

"So the decision on what treatment to pursue that once would have been made by you and your doctor is now made for you by a bureaucrat using a formula -- a formula to literally determine if your life is worth saving."

Apparently nobody explained to either of these two that rationing is exactly what private insurance companies already do.

Denial based on pre-existing conditions?
Excessive testing required before covering treatment?
Refusing to pay for life-saving techniques because they're "experimental"?

If health care is going to be rationed, do you want it done by a body under the control of democratic laws, or by a for-profit company that makes money by denying your care? Perhaps now is a good time to point out that insurance executives make far more money than any doctor you will ever see. And the first person to make over $1 billion in bonuses works for a health insurance company. Does anyone else see the problem with letting free market control your health care?

Here's another goodie from Bachmann's site:

There are too few shining examples of profitable and efficient government enterprise – take a gander at the failing postal service or struggling Amtrak, for example – for us to entrust the nation’s health care system to Washington’s management and oversight.

I have a couple things to point out here:
First, I'm willing to make a fairly rational guess that the USPS is failing because of the increase in electronic transfers of mail and files. If the gov't ran a newspaper that happened to be losing money, would you also say that it proves federal incompetence? Oh wait, the same thing is happening to every other paper in the country. Well, lo and behold, it's not just the USPS that's losing money. UPS is crashing, too. Private companies don't always beat out the gov't.

I'm getting away from myself. To be honest, I don't really want gov't health insurance if it looks like the post office because I don't like the post office. So let's instead look at a more appropriate comparison, such as the way gov't already manages health care.

Dr. Filice works at the Minneapolis VA Clinic, and says that it represents how all of America's citizens should be treated by the health care system.

"I think that the VA experience shows that it's possible for government to be a good player; an accountable player in that mix," Felice said.

Felice said the VA is a model that lawmakers should consider emulating as they try to overhaul the nation's health care system.

And I'm sure I don't need to point out that more than 94% of Medicare recipients are happy with their health care coverage.

Okay, so we all realize that providing a public option for the uninsured will cost money. This is true. And I hear a lot of people complain about not wanting to subsidize people's health care with taxes. Here's a newsflash for you: YOU ALREADY SUBSIDIZE CARE FOR THE UNINSURED. And you know what? It costs more than it would if they were insured.

Let me explain why this is...
Gov't health care centers, such as county hospitals, are required to provide emergency care for all patients, regardless of whether they can pay for it. If they can't pay, the hospital -- funded by your taxes -- has to cover the costs. Emergency care is exponentially more expensive than clinical care, which means the easiest way to reduce this tax burden is to provide uninsured patients access to preventive care. Allowing access to preventive care will also discourage patients from using the emergency room for non-emergency injuries.

So, do you want to reduce the cost of health care? Provide a public insurance option.

Biology 203...

I noticed my buddy Andrew has a link to this blog on his website, complete with a large title of "SCIENCE". I figure with such a kind endorsement, I really ought to post something about science. So let me tell you a bit about some recent experiments I've been doing.

Western Blot

Hopefully you remember the leukemia studies I'm working on. I've been busy trying to characterize these cancers, and today I'm going to describe a very powerful tool for doing that called Western blot. Before I discuss Western blotting, let me start with a related procedure called the Southern blot. I happen to be running both Western and Southern blot experiments, but the Southern is arguably more confusing, so I'll save the details for another day. But I mention it now because it was the first of the "blot" experiments to be invented.

Southern blot is unexcitingly named after its inventor, Dr. E. Southern. He developed a way to detect and quantify particular sequences of DNA in cells. Before long, the technique was altered to detect RNA, and was named "Northern blot" -- not because there's a Dr. Northern, but because of the play on Dr. Southern's name. Eventually, variations and combinations of the procedures led to Western, Eastern, and Southeastern blots as well.

The Western blot is the one I'll focus on today, and it too resembles the Southern and Northern blots, but it specifically detects protein instead of DNA or RNA. In my experiments, I'm interested in how leukemia differs from normal cells. If I can identify abnormal levels or actions of key proteins, they can potentially be used as treatment targets down the road. I won't get into extreme details, but let's say I think these cancer cells lack an important regulatory protein we'll call protein X (pX). pX restricts the action of other growth proteins, and thus without pX, the growth proteins go crazy. To test my hypothesis (that the cancer cells lack pX), I'll employ the Western blot to measure the levels of the protein.

Remember my post about antibodies, and how there can be an antibody specific for any possible protein? Western blotting takes advantage of this specificity by spreading out all the proteins in a tissue, and probing them with antibodies. Here's how it's done:

I start by making a soup of protein from my cells of interest. Specifically, I'm looking at protein in pre-B lymphocytes, but you can use any cell you want. I extract the proteins by breaking open the cells with a particular buffer solution. One problem with this is that the insides of cells also contain enzymes called proteinases that degrade proteins, and breaking the cells open exposes the two, and your proteins break down. To prevent this from happening, I add proteinase inhibitors to the solution.

After isolating the proteins, I treat them with reducing and denaturing techniques to uncouple and unfold the complex shapes proteins have. Incidentally, one of the reducing agents is beta-mercaptoethanol -- a chemical that smells so ridiculously awful, the bottle has a warning the says it is toxic because of the smell (think stinkbombs). Next, I separate the protein on an acrylamide gel by putting the samples at one end of the gel and running an electrical current through. The negative charge on proteins causes them to migrate toward the positive pole in the current, and as they move through the gel, they separate based on size (large proteins move more slowly through the gel than small proteins).

Now the proteins are spread all over the gel, but I can't really do much with them. If I want to analyze them, I need to get them out of the gel by transferring them to a special membrane. This is done in almost the same way as I made them migrate trough the gel, except this time, I use the electrical current to move them up and out of the gel. So if I put the membrane on the surface of the gel and apply the current, the proteins will lift out and stick to the membrane in the same pattern as they were before (sort of like lifting a drawing off of paper with Silly Putty). Now I have my proteins spread out by size, stuck to the membrane, and I can manipulate it however I like.

Now comes the "blot" of Western blot. I cover the membrane with a primary antibody for pX. In theory, it will bind only to pX, but proteins are notoriously sticky, and will bind to anything they can get their grubby little alpha-helices on. To prevent this, I give them a bunch of irrelevant dummy proteins to play with -- essentially "blocking" the nonspecific binding of sticky proteins. That leaves the antibody free to find pX. In the laboratory, we accomplish this by using a state-of-the-art protein compound called powdered milk.

Okay, I've covered the membrane with antibodies, and they have bound to my protein of interest, pX. Unfortunately I don't have a way to see where the antibodies have bound. Now I have to come in with a secondary antibody to find the primaries. This secondary antibody has a "marker" or "flag" stuck on the end that lets me see it. This flag can be a couple different things, such as a bioluminescent molecule, radioactive material, or -- in my case -- a fluorochrome. A fluorochrome is a molecule that emits light at a certain wavelength when stimulated by a different wavelength, thereby rendering the antibody detectable. Like this:



On the left of the picture is a "ladder" of known standard protein sizes, so I can confirm my protein is the right size. It just so happens that pX is ~62 kDa (kilodaltons), and as you can see, the more total protein I start with (10, 20, or 40 ug), the more pX I can detect.

And that, folks, is how a Western blot works.