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'Kiss of Death' Discoverers Get Nobel Prize
baldinux writes "Science Daily has written an article describing the cellular process of regulated protein degredation, which has landed three people the Nobel Prize in Chemistry. According to the article, this finding could greatly help researchers understand ubiquitin-mediated protein degradation, making it possible to develop drugs to treat cervical cancer, for example."
Whoa! What a loaded statement! Nothing else need be said.
how long until they patent "A process for breaking down and degrading proteins" and send cease-and-desist letters telling everyone to stop digesting ny meat they eat this instant.
Biochemists could, I presume, tailor ubiquitin to grab up undesirable proteins and still have the degradation function work.
Imagine all the diseases that come from bad proteins! This could unleash a new class of therapies.
The clearance system sounds logical. It is not. It is completely arbitrary. -- John Bolton
From the first couple of comments, it seems people don't know what the heck this is talking about. Let me explain:
The human body has a natural mechanism for recycling proteins. What nobody understood, however, was how it knew what proteins to recycle - after all, if proteins were just recycled randomly we'd all be globs of jelly.
So then these guys came along and figured it out: when the body wants to recycle a protein, it attaches another protein as a label, called ubiquitin.
The science isn't exactly new - 1980s - but it was significant, and best of all, pure research. (So you can stop with the whining about drugs)
Congrats to these guys. It really is an honor for a University to have a Nobel Laureate in their staff, and UC Irvine just got one. =]
Without a proper flamewar, Anonymous was undecided on what shell to run.
The degradation is not indiscriminate but takes place through a process that is controlled in detail so that the proteins to be broken down at any given moment are given a molecular label, a 'kiss of death', to be dramatic. The labelled proteins are then fed into the cells' "waste disposers", the so called proteasomes, where they are chopped into small pieces and destroyed.
Isn't this similar to the way OO languages are doing, create an object, use it and dispose it.
Actuall, isn't this the way we are doing things on a daily basis? It's interesting to find out that even our body is unknowingly doing almost the same process.
I recently learned (through an unpleasant personal, but not-quite-that-personal, experience) that HSV, an STD, is the "major cause of cervical cancer".
Watch out, guys. Especially watch out ladies.
-Peter
There are many, many different types of cancer. At least one for every tissue in the body. Cancers retain many of the properties of the parent tissue. Many breast cancers for instance, are estrogen dependant. So an estrogen antagonist can help shrink many breast cancers. This wouldn't work at all for skin/lung/colon/whatever cancer. I'm not sure about the specifics of cervical cancer, but it's likely there are proteins specifically expressed in cervical tissue that could be targetd for degradation by an engineered ubiquitin ligase.
Give me Classic Slashdot or give me death!
The biggest problem to developing any potential theapies from these groundbreaking discoveries is to figure out how to target particular proteins or classes of proteins. There are numerous E3 ubiquitin ligases in cells that target a varety of proteins for degradation. However, the molecular mechanisms by which this recognition takes place is still rather uncertain. The structure of the molecular interaction must be determined at atomic resolution (A difficult process which commonly uses X-ray crystallography and very, very intensive computing).
I see two methods which would lead to useful therapies:
The first is the simplest and will therefore also most likely be the first viable strategy: harnessing natural ubiquitin ligases to target and downregulate harmful proteins. This means that any therapies will be limited to natural ubiquitination processes. Humankind will find ways to make these reactions better, or ways stimulate them in diseased cells.
The second approach is de novo design. Once the structure of the target is determined, enzymes can be desgined to target it for ubiquitination/degradation. However, this requires an understanding of biochemistry far beyond what currently exists. Not only does the therapeutic enzyme have to recognize the target, but it must also catalyze the ubiquitination reaction. At this time, I do not believe that anyone has designed a functional protein-based enzyme from the ground up. This technique has greater potential, as we could target ANY protein we dislike, but we are not quite able to implement it yet.
"Me fail English, that's unpossible." --Ralphie
Targeted protein degradation has applicaitons beyond anti-cancer therapies. Alzheimer's Disease seems to be caused by the build-up of amyoloid beta protein in neurons, which is due to the failure to degrade this protein. One potential therapy is to use other ubiquitin ligases to target amyoloid beta for degradation as a method to break up protein plaques.
Similarly, antiviral potential exists as well. For example, if we could engineer ubiquitin ligases to target HIV proteases (The target of the protease inhibitor component of anti-HIV "cocktails"), we would have another method to hamper viral replication.
As with all new developments, however, there exist numerous problems that must to be overcome before we see practical and clinical results.
"Me fail English, that's unpossible." --Ralphie