Wednesday, October 31, 2012

Halloween and poisoned treat rumors: What are the facts?

1920s Halloween postcard.
Via Wikimedia Commons. Public domain in USA.
Many of us probably heard the stories as kids: the razor in the apple, the poison in the Pixy Stix, the mean elderly lady who inexplicably wouldn't let children run through her flowerbeds and thus was clearly planning some dire Halloween revenge on those who did. As adults, some with children, we see these rumors in a new way, one that perhaps has us trailing our children at a respectful distance, making sure they heed our warnings to go only to the houses of people they know. (OK, I don't do that, but some parents do).

But how frequent are these acts of Halloween malevolence? Which of the most infamous rumors are, in fact, facts?

Who better to answer those questions that the queen of poison writers--that's a good thing--Deborah Blum, author of (natch) The Poisoner's Handbook: Murder and the Birth of Forensic Medicine in Jazz Age New York, one of the most lyrical, fascinating, and macabre interweavings of history, forensics, and chemistry you'll ever encounter. So, for more of that narrative craft and to sift the facts from the rumors, get thee over to Blum's blog site at Wired, where she's got the post that answers your childhood--and adult--questions about the real-life ghouls of Halloween night, including one terrible story about a father who killed his son. 

Blum writes:

This was the 1960s and even then, people told stories, warned their children, about the psychopaths out there who might drop poisoned candy into one’s hands. In the long history of the holiday, truthfully, this has almost never happened. But the very nature of Halloween – the witch at the door, the monster in the closet – lends itself to such ideas. Wasn’t there a crazy woman on Long Island in 1964, after all, who handed out arsenic to trick-or-treaters she thought too old for the candy hunt? 
It hardly mattered that as Snopes points out, she didn’t kill anyone. And her deliberate poisoning attempt seems to be an odd exception to the general goodwill of the holiday. The psychopath at the door is an urban myth.  

Monday, October 29, 2012

Frankenstorm: What is the role of climate change?

Sandy the Superstorm and her water vapor. 
Video via NOAA; hat tip to Andrew Revkin.


[First, check out this hurricane crisis map Google developed, complete with updated information on the storm's status and effects and even shelter location info.]

I've seen this question crop up a lot over the last few days--it's a natural one, I'd think, given promises of more frequent extreme weather events in association with human-driven global climate shifts: What is the role of climate change, if any, in Sandy the Frankenstorm, currently bearing down and flooding the US northeast after having killed dozens in the Caribbean on her way to US shores?

Lucky for people like me who couldn't begin to answer this question, people like Andrew Revkin at the New York Times have gathered the resources for us. Of course, the first take-home is the usual one: Nothing is straightforward here. As Revkin writes:
While the echo of Frankenstein in that Twitter moniker can imply this is a human-created meteorological monster, it’s just not that simple.
He gets into the "not simple" parts of things and cites some data (with links!) and then has been providing useful and insightful updates from meteorological experts. What it comes down to is, Sure, there's a littla the global climate change at play here--it's happening and it's global, so it's going to have some influence. But also at play are typical or at least not-wildly-unimaginable variations of weather patterns that just happen to be converging right now, right there. So a single weather event is just an anecdote in the climate context and doesn't necessarily stand as a reflection of an entire climate pattern. These patterns can emerge with warming or with cooling--and they have, over long time frames. Revkin writes:
But there remains far too much natural variability in the frequency and potency of rare and powerful storms -- on time scales from decades to centuries -- to go beyond pointing to this event being consistent with what’s projected on a human-heated planet.
In other words, this Frankstorm really is a monster built of parts--convergence of typical weather patterns and heavily populated places, roughly pieced together to some extent by human-driven climate change and animated on live radar. But Sandy the Frankenstorm is likely no more exemplary of the dire future some think it represents than poor Frankenstein's monster himself was an exemplar of humanity.

By Emily Willingham

The opinions expressed in this post do not necessarily conflict with or represent those of the DXS editors or contributors.

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FYI: For updates on this sort of analysis and what's happening with Sandy in real time, the folks at Boing Boing tweeted this list of recommended people to follow on Twitter.

Update 2:30 ET: Check out this beautiful, mesmerizing, and scary wind map, made with data on surface winds from a national database.


Monday, October 22, 2012

NOC: A whale of a mimic

Listen to this:

Get Adobe Flash player

What does it sound like to you? (Recording courtesy of the BBC.)

If you thought it sounded human, you're right. It does. But that's not a human making the sound--it's a beluga whale named NOC.

Shh. The beluga is listening.
Credit: via Wikimedia Commons.
Dolphins have been trained to mimic people, but the fellow in this recording apparently picked up human-sounding lingo on his own. Researchers describe his acquisition as self taught. According to this BBC story, the way the white whale pulls it off isn't easy--he had to really work at it in a pretty un-beluga-like way to get his voice so much lower than the normal beluga vocalization. You can listen to the typical beluga talk, which sounds like a dyspeptic piglet trapped by a creaky door here. It sounds. Ed Yong at Not Exactly Rocket Science tells us these whales are sometimes called "sea canaries" but that they usually sound like children in the distance.

To me, this human mimicry sounds like nothing as much as men on a fishing boat, hollering at each other over the wind, just as they might sound to ears underwater. In fact, the way the researchers found NOC, according to the BBC story, was when a diver surfaced, thinking he'd heard someone tell him to get out. 

What do you think it sounds like?

Friday, October 19, 2012

100 Years

By Adrienne M. Roehrich, Chemistry Editor
Photo of the author with her 100 year old grandmother 10-1-2012


100 is such a nice round number. 

Should I start with a disclaimer? I'm a chemist, not a biologist. Perhaps I should leave a post on centenarians to the biologists, but I have a vested interest in the topic. On October 1 of this year, my grandmother turned 100, so I've been a little obsessed with living until 100. In the United States, an estimated 1 in 4400 people reach the age of 100 and the highest number worldwide. The next highest number of centenarians reside in Japan, with a rate of 1 in 3500 people. 

The question is, why do these people live so long? This is a highly studied question. When one delves into the literature, as with most questions, there is no simple answer and often studies conflict with each other. There are different modes of study: some scientists study those who have become centenarians to try to determine what they have done to reach this rare milestone while other scientists work in theories, then animal models to study what pathways lead to longevity.

Studies have found that healthy centenarians in some areas have high levels of vitamin A and vitamin E1 and higher red blood cell glutathione reductase and catalase activities.2,3 But the presence of higher levels of these vitamins and glutathione reductase is not present in all centenarians, and the mere presence of these high levels does not necessarily indicate longevity.

 
Molecules that may or may not help longevity


You may have heard exclamations about antioxidants or calorie restriction. While antioxidants (the aforementioned vitamin A and vitamin E) are known to protect the body from the harmful effects of free-radicals, which occur in the normal processes of the body, evidence does not support that simply adding more antioxidants to the diet will slow aging. There are studies also showing that calorie restriction may have beneficial effects in terms of markers of aging in some animals, but many animals that are commonly used as human models do not extend longevity under calorie restriction, and such a course of action may have deleterious effects. The safety and benefits of long-term calorie restriction is currently unknown. Scientists are working towards answering these questions. 

Genetics plays an important role. The best predictor of a person reaching 100 is having a sibling live past 100. Variations in genes abound, but other than children of long-lived parents living longer, specifics are elusive. Oddly, being born in the Fall (September through November) is linked with a higher likelihood of becoming a centenarian.4 And functional independence for a longer period of time (past the age of 90) was found to be strongly correlated to centenarians. 90% of the participants in the New England Centenarian study were found to have been so.

Hormones are integral to our body function and have been studied for their potential pathways in longevity. Testosterone has been focused on, and lately a study of Korean eunuchs gave a higher rate of centenarians, 3 in 81 individuals. Due to the wide variability of the amount of testosterone produced by individuals, whether more or less testosterone exposure is beneficial or deleterious is unknown. 

What causes aging? This question is so important the National Institutes of Health (NIH) has devoted National Institute on Aging, the leading research institute on aging. A summary in more detail than I have gone into here is given on the NIH NIA’s site about preventing aging

If we look at the cellular level, scientists discovered that complete copying of DNA is dictated by telomeres and the enzyme telomerase, which earned 3 scientists the Nobel Prize in Physiology and Medicine in 2009. The unique DNA sequence in the telomeres protects chromosomes from degradation. When telomeres are shortened, cells age. Eventually, the telomeres will shorten, and cells will age and die. Unfortunately, extending telomeres or increasing the activity of telomerase enzyme does not help anti-aging, it contributes towards the growth of cancerous cells. 

A conversation with Dr. Mark D Johnson on twitter gave me these neat facts: Complete natural Homo sapiens LifeSpan = 120 years! All mammals except humans, bonobos, and chimpanzees, live six times their growth cycle. We grow within 20 years. That means natural mammal lifespan of 120. 

Overall, the contributing factors towards ageing and longevity are deemed to be complicated and there is no short-order anti-aging remedy.

Turning more towards my own field of expertise, the Maillard Reaction, a chemical reaction that makes cooked food tasty, also turns 100. Obviously, the actual chemical reaction goes back longer than 100 years - to when amino acids began to react with sugars at elevated temperatures. However, the French chemist Louis-Camille Maillard first reported the nature of these reactions in 1912.5 Maillard chemistry not only describes the molecules in baked bread, grilled veggies, and brewing of beer, but also other molecules as products, so many that chemists did not study Maillard chemistry in detail until World War II. Nearly 60 years ago, African American chemist John E. Hodge reported a mechanism for the Maillard reaction6

Hodge’s Flowchart of the Maillard Reaction

Products of the Maillard reaction range from molecules that are both welcome and abhorrent. The usually enjoyed flavor and aroma of roasted coffee is a product of the Maillard reaction, as is the char on the surface of grilled food which is considered to be carcinogenic. 

Roasted Coffee Beans, photo by Adrienne Roehrich
Grilled Yams, photo by Adrienne Roehrich


Do you know someone or something that has reached the anniversary of 100 years on this earth? 


References:
(1) Mecocci, P.; Polidori, M. C.; Troiano, L.; Cherubini, A.; Cecchetti, R.; Pini, G.; Straatman, M.; Monti, D.; Stahl, W.; Sies, H.; Franceschi, C.; Senin, U. Free Radical Biology and Medicine 2000, 28, 1243.
(2) Klapcinska, B.; Derejczyk, J.; Wieczorowska-Tobis, K.; Sobczak, A.; Sadowska-Krepa, E.; Danch, A. Acta Biochimica Ponoica 2000, 47, 281.
(3) Andersen, H. R.; Jeune, B.; Nybo, H.; Neilsen, J. B.; Andersen-Randberg, K.; Grandjean, P. Age and Ageing 1998, 27, 643.
(4) Journal of Aging Research 2011, 2011.
(5) Maillard, L.-C. Comp. Rend. 1912, 66.
(6) Hodge, J. E. Journal of Agricultural and Food Chemistry 1953, 1, 928.


Wednesday, October 17, 2012

Breast cancer screening and treatment, especially in younger women

[Editor's note: I was on Twitter, as usual, a couple of days ago, and started seeing tweets with the hashtag #SSCAbc. They contained information that I, an avid consumer of science and medical information, don't normally see addressed in breast cancer stories, including for young women with breast cancer and how to talk to children about having breast cancer. I've aggregated some of those tweets below, but you can read more at the hashtag here, which represents the Seattle Cancer Care Alliance, whose representatives were conducting the Twitter session.]

Monday, October 15, 2012

Aren't you curious?



Source: IFLS
By Courtney Williams, DXS contributor
Recently my on-line science pal Emily J. Willingham asked on Facebook,
“You are a consumer of science. As one, what bothers you about how science is offered to you? What questions do you have? How do you consume scientific information? How do you use it?”
She’s going to be blogging on the Forbes network, see her here, and I’m guessing this was the impetus for that particular set of questions.I had much to say in answer to her questions.
One of my biggest pet peeves is that the most sensational headlines are used- even if they are entirely inaccurate scientifically. For example the recent news about small pox and breast cancer. Headlines like, “New smallpox virus could ‘cure’ breast cancer, studies reveal.” How many ways is that wrong?  Well, it’s not smallpox the researchers were using, it’s a vaccinia virus, which is in the same family as the smallpox virus. Big difference. For instance, there wasn’t a global effort to eradicate cowpox- another vaccinia family member. Just because the viruses are related doesn’t mean they are the same thing. Also, what’s with the quotation marks around cure?Maybe because it’s not actually a cure, not even a treatment, just an interesting experiment done in mice- but cure (even in quotes) makes for a better headline. [If you want to learn about the real science behind that crappy headline, here's the original paper- "Vaccinia Virus GLV-1h153 Is Effective in Treating and Preventing Metastatic Triple-Negative Breast Cancer"]
Articles rarely cite their scientific sources- i.e. linking to the actual journal article they are writing about. For instance, the craptastic example above where the ‘journalist’ (how’s that for quotation marks?) not only failed to link to the original article, he didn’t even mention the journal it was published in, when it was published, or any other info (other than the lead author’s name) that would help a reader find the journal article or additional info on it.
As for sources, it's important to distinguish for the reader between peer reviewed journal articles and mere opinion pieces on blogs. Take for instance the blog post I wrote about here that appeared on the website of Psychology Today. Many news outlets picked it up and touted it as research that showed it was dangerous to let your infant ‘cry it out’ when really it was just a post (poorly researched, lacking citations, and full of unsupported conjecture and opinion) on the blog of a psychologist. A blog post is NOT the same thing as a peer reviewed journal article. Please journalists, know this!
Another gripe, accuracy is sacrificed for the sake of brevity, which completely defeats the purpose of sharing the science. See above yet again about smallpox as a ‘cure’ for breast cancer.
Another problem I have is the way the media handles funding sources for research studies- they always matter, it’s imperative that scientists report any conflicts of interest that funding sources might prove to be. However, they are not always a sign that researchers are ‘in cahoots’ with the companies that fund them. For instance, would you trust RJ Reynolds to fund unbiased research on smoking and cancer? Probably not. Thus, if at the end of a research article you see a company with a known bias and the findings support their assertions, you are right to be skeptical. However, sometimes the funding merely means a company paid for work to be done, regardless of the outcome. For instance, a pharma company that partners with an academic lab on basic science and published the results in a peer reviewed journal. Or, a drug company that funds the clinical trials for it’s drugs. That’s just the way it works- who else would fund the trial if not the manufacturer? If those types of studies are published in peer reviewed journals, they have been vetted to that extent. Further, with clinical trials, the Federal Drug Administration (FDA) oversees all those trials to help ensure they are unbiased and protect the patients involved as well as the public as a whole. The media seems unable to distinguish.
As for how I generally consume science/scientific information? It’s usually as follows- hear about it on the radio or read a lame article via Yahoo News/Strollerderby/The Stir/etc., assume the author is either full of bologna, got the science partly/mostly wrong, had their more level-headed title replaced by an editor, is totally biased, etc., then I track down the original research article, and possibly seek out commentaries on the work from reliable sources (SciAm blogsDouble X Science, fellow scientists, etc.).
What about how I use it? Well, obviously I’m a scientist, so I ‘use’ science/scientific information professionally every single (work) day to try and cure (no quotation marks) and/or treat cancer. In my personal life, science helps me make healthcare decisions for myself and my family, decide which products to buy or to avoid, answer questions about the natural world when my toddler asks, as  material to blog about and use to dispel misconceptions held by myself and others.
However, a lot of the time I don’t necessarily even use the science I consume. Sometimes I just want to know it. I’m curious.
Pretty frequently people ask me, “How do you know that?” or “Why do you even know that?” I’m not sure how to answer. If it’s a medical question, a lot of the times the answer is, “Well, I have that body part and I want to know how it works.” Or, “Well, I’m taking that medicine, so I looked up how it works.” People forget that science is the basis of everything- it’s how everything works or came to be.  While others seem to find it odd that I’m always looking up the science behind was I see/do/hear about, I find it odd that other don’t seem to question enough.
You’re taking that medicine, you’re having that surgery, you’re using that product right now- don’t you wonder how/why it works? Why aren’t you wondering?
Where’s your curiosity? Don’t you just want to know why the sky is blue? How did you came to be? Why are roses red and violets blue?
Aren’t you curious?
The opinions in this article do not necessarily reflect or conflict with those of the DXS editorial team and its contributors.---------------------------------------------
Courtney Williams is a scientist, wife, and mother (in no particular order). She works in the oncology department of a biotech company in the burbs of NYC. She blogs about marriage, motherhood, and science at http://mommacommaphd.wordpress.com/.

Friday, October 12, 2012

An antibody therapy for hemophilia A?


Example of an antibody. The interesting bits are purple,
as so many interesting things are.
Image credit and license info, via Wikimedia Commons.

By Jeffrey Perkel, DXS tech editor

Last night on TV I caught an ad for Humira, Abbott Laboratories’ prescription medication for a series of conditions including rheumatoid arthritis, psoriatic arthritis, and Crohn’s disease.

The ad noted that, like all drugs, this medication actually has two names, its brand name (Humira), and its generic name, adalimumab. That suffix, -mab, indicates that Humira is a monoclonal antibody, a large protein normally produced by your immune system’s B cells to recognize and eliminate proteins and pathogens that are not “self.” In particular, Humira recognizes, binds, and inactivates the protein called “tumor necrosis factor,” or TNF, which is implicated in various autoimmune disorders.

There are dozens of monoclonal antibody drugs on the market now, including the breast cancer therapeutic Herceptin (trastuzumab), Remicade (infliximab) for autoimmune disorders, and Rituxan (rituximab) for non-Hodgkin lymphoma.(*) In most cases, by binding specific proteins, either in solution or on cell surfaces, these molecules either inactivate proteins (as in the case of TNF), target the cell for death, or block inappropriate cell signaling (as in Herceptin). Other antibody designs use the antibody as a "guided missile," targeting drug or radioisotope "warheads" to cancerous cells. 

On Sept. 30, though, a team of Japanese researchers at Chugai Pharmaceutical, reported an example of a new kind of antibody application, and it’s pretty slick.

The paper concerns a novel treatment concept for hemophila A, an X-linked recessive bleeding disorder that affects about 1 in 10,000 men. It is caused by a lack of a clotting protein called factor VIII (FVIII), and the typical treatment is “prophylactic supplementation” of the missing protein.

There are three problems with that treatment, as the paper notes. First, FVIII is expensive. It also must be administered frequently and intravenously, which is especially difficult for pediatric patients and “negatively affects both the implementation of and adherence to the supplementation routine.” But perhaps most significantly, in about 30% of cases the body recognizes the recombinant FVIII as “non-self” or “foreign,” and develops antibodies (“inhibitors”) to inactivate it, rendering the treatment ineffective.

To circumvent that problem, the Chugai team developed what is called a “bispecific antibody” to replace FVIII. So what is a bispecific antibody?

In cartoon form, antibodies resemble the letter Y, with antigen-binding regions at the tip of either branch. In a normal antibody, those two binding regions are identical, such that each antibody can bind two copies of the same protein molecule.

A standard monoclonal antibody has two binding arms, each recognizing the same antigen (protein target).
Source: Wikipedia, http://en.wikipedia.org/wiki/Antibody

A bispecific antibody, though, has two different binding domains, one for each of two proteins, such that it can effectively act as a scaffold to bring two proteins – or the cells they are attached to – together. The only bispecific currently on the market, Trion Pharma’s Removab, acts to couple immune system T cells and macrophages to tumors.

A bispecific antibody, Trion's Removab.
Source: Wikipedia, http://en.wikipedia.org/wiki/Bispecific_monoclonal_antibody

Chugai’s scientists developed a bispecific antibody that does something different. Their antibody, called hBS23, links two other clotting factors, FIXa and FX, thereby mimicking the function and architecture of the missing FVIII without actually administering it.

FVIII activates FX in the presence of FIXa. hBS23 is a bispecific antibody that replaces FVIII.
(c) 2012 Nature Publishing Group [Nature Medicine, doi:10.1038/nm.2942]

In test tube clotting assays, hBS23 was about 14-times less catalytically efficient than FVIII itself, yet could nevertheless induce clotting, even in cases where the plasma contained inhibitors against FVIII. (Recombinant human FVIII had no effect in those latter cases.) In a non-human primate model of hemophilia A, hBS23 prevented development of anemia and reduced internal bleeding comparable to FVIII itself.

Significantly, hBS23 lasts a long time in the primate bloodstream – with an IV half-life of 14 days and comparable subcutaneously bioavailability – yet seems unlikely to elicit inhibitory antibodies of its own. That subcutaneous activity is significant, as regular subcu administration should be more easily tolerated than an IV.

Based on the these studies, and some simulations, the authors predict that "once weekly dosing of 1 mg per kg body weight of hBS23 would show a continuous hemostatic effect in humans."  

Of course, that's just a prediction. The proof of the pudding is in the eating, as they say, and only time will tell how hBS23 will fare in people. But don’t look for it on pharmacy shelves any time soon. Clinical trials take time, and further optimization of the antibody design is likely required. Still, the team is obviously upbeat about their strategy’s potential:

“A long-acting, subcutaneously injectable agent that is unaffected by the presence of inhibitors could markedly reduce the burden of care for the treatment of hemophilia A.”

For more details, you can read the report here.

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We've also got a partner post for you, an antibody explainer by our very own Jeanne Garbarino. Be sure to check it out! 


*Fun fact: If you’ve ever wondered about how drugs get their generic names, they are conferred by the US Adopted Names Council. The names have a kind of prefix/stem structure, linking a manufacturer-supplied but meaningless prefix (adalimu–) with a specific stem (eg, –mab) that denotes the drug class or activity. There are literally hundreds of stems, including –coxib (COX2 inhibitors), –vir (antivirals), and –stat (enzyme inhibitors); for a complete list, click here.

The Amazing Antibody and its Therapeutic Potential


NYC Campaign to alert the authorities if you see
something  suspicious.  Antibodies are like the citizens
that tell our body that something fishy is going down.

By Biology Editor, Jeanne Garbarino

There is a campaign sponsored by NYC’s Metropolitan Transit Authority (MTA) encouraging citizens to speak up if they see any activity or persons acting in a suspicious manner.  Plastered all over buses, subways, and commuter rails are posters with the following message: If you see something, say something.  This type of imagery reminds me very much of our own biological warning system programmed to, in essence, “speak up” should a suspicious character of the microscopic kind make it’s way into our bodies.  It is through our immune response that our bodies “say something” in the event of infection. 
At the very crux of the immune response are tiny proteins called antibodies, which are basically like the citizens that report any suspicious activities.  Antibodies often travel in the blood stream, and upon crossing paths with a foreign invader (bacteria, virus, etc.), an antibody will flag it down and alert the “local authorities” of the body (aka immune cells). 
For many years, scientists have been studying antibodies and their role in the immune response, revealing many aspects surrounding their structure and function.  And through these studies, we have figured out how to use antibodies in ways that go beyond the immune system.  For instance, antibodies against human chorionic growth hormone, or hCG, are the essential ingredients in home pregnancy tests.  More recently, scientists have, in many ways, harnessed the power of antibodies for pharmaceutical uses.  A very popular example of this is the drug Remicade, which is used to treat severe autoimmune diseases like rheumatoid arthritis and Crohn’s Disease.   But, what exactly are antibodies and how do they work?
Well, I am glad I asked me that question.

As I mentioned, antibodies are proteins that we make.  Specifically, they are produced by specialized immune cells called B-cells, which are the main players during our humoral immune response.  B-cells will either secrete an antibody, which can then float around the circulatory system, or the antibody can remain attached to the outside of the B-cell.  If there is something “foreign” in our bodies, such as a virus or bacterium, antibodies will recognize and attach itself to the invader, which is scientifically referred to as an antigen.  When an antibody attaches to an antigen, it signals to our body to get rid of it.  Amazingly, each antibody can only recognize 1 antigen, which is why we need so many different types of antibodies!     
To get a better idea of how antibodies work, it is important to learn their basic structure.  Antibodies are ‘Y’ shaped proteins, and have both constant and variable regions.  The constant region is the same among all antibodies within a specific class (there are several different classes), where as the variable region is the portion of the antibody that is designed to recognize a specific antigen.      
To better explain this, consider the antibody to be a lacrosse stick.  The “stick” part is the constant region, and the mesh part is the variable region.  Now consider the lacrosse ball to be the antigen (i.e. bacterium or virus).  Only the lacrosse ball that is a triangle can fit into the lacrosse stick with the triangle-shaped mesh pocket.  The same is true for the circle.  And so on.  Once the ball fits into the mesh, meaning, once the antibody binds the antigen, a cascade of events is set off, essentially sounding the alarm.  Under normal, healthy circumstances, we take care of the antigen and the infectious agent is removed. (Note: there are different classes of antibodies and each class has it's own "stick" part.)
A basic analology for how antibodies work.
Building off our understanding of how antibodies work, scientists have been able to develop monoclonal antibody therapy, which is the use of specific antibodies to stimulate an immune response against a disease.  For instance, we now use monoclonal antibody therapy to combat a variety of cancers by injecting cancer patients with antibodies designed to recognize specific components on the surface of tumor cells.  This helps signal to the body that it should turn on the immune response and get rid of the tumor cells. 
The list of conditions where monoclonal antibody is a potential therapy is growing, and includes a variety of autoimmune diseases and cancers, post-organ transplant therapy, human respiratory syncytial virus (RSV) infections in children, and most recently hemophilia A.  Also being explored is the use of monoclonal antibody therapy for addiction, which could essentially revolutionize how we can help people kick extremely difficult habits (i.e. cocaine or methamphetamine).
Despite the thousands of tedious and repetitive assays I’ve done using antibodies in my own laboratory, I know that I can never lose sight of how amazing these little proteins are. 

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This post is a mental appetizer for another post on monoclonal antibodies by DXS tech editor, Jeffrey Perkel. His post specifically discusses the potential use of monoclonal antibody to treat the X-linked blood disorder, hemophilia A.  Read about it here.