What is Azodicarbonamide?

9 Facts About This Dangerous Food Additive

azodicarbonamide dangers

The recent revelation that Subway bread contains azodicarbonamide has gotten a lot of attention. And it should… azodicarbonamide is a dangerous industrial chemical used to make yoga mats, shoe rubber, and synthetic leather. Although there’s no reason for it to be in bread, it has in fact been used for decades as a dough conditioner. The public backlash was so great that Subway has stated it will cease to use azodicarbonamide as a food additive… although Subway stopped short of providing concrete deadlines as to when, so be aware.

So… what is azodicarbonamide? And what are the health risks associated with exposure and consumption? Because it’s used to make foamy yoga mats, please understand that it isn’t safe to consume, and the next 9 facts will explain why.

1. Azodicarbonamide is an Industrial Chemical

The primary function of azodicarbonamide is centered on the way it breaks down during processing — it creates tiny bubbles that make things “foamy.” Somewhere in the testing procedures, scientists discovered it whitened flour and acted as an oxidizing agent. Bakers, or rather “food scientists” soon concluded that it should be a standard inclusion in bread.

2. Azodicarbonamide Increases Gluten Content in Bread

Oxidizing agents like azodicarbonamide are used to increase gluten content. This is “desirable” because higher levels of gluten create stronger, more durable dough. The added convenience to processing isn’t without other risks though. Gluten has been linked to a host of gastro-intestinal, immunologic and neurologic diseases. [1] [2]

3. Azodicarbonamide Can Cause Respiratory Problems

Research has established a direct link between exposure to azodicarbonamide and the onset of asthma. [3] According to a World Health Organization (WHO) follow-up report, regular occupational exposure to azodicarbonamide can lead to asthma and allergies.  The WHO report notes many of those who developed asthma and other respiratory complications experienced symptoms within just three months of exposure. [4]

4. Azodicarbonamide is a Skin Irritant

The WHO report also noted physical exposure to azodicarbonamide caused recurring dermatitis. [4] Fortunately for those suffering, eliminating exposure caused the indications of the dermatitis to go away.  While this is good news, these results show how quickly industrial chemicals can initiate an autoimmune response.  Unfortunately, skin irritation seems to be the least of concerns…

5. Azodicarbonamide Disrupts the Immune System

In 2001, lab tests found that direct exposure to azodicarbonamide inhibited human immune cell formation and function. [5] Although “direct exposure” may be less of a common problem, the bigger problem happens when azodicarbonamide is heated up, as when it’s a bread ingredient…

6. Azodicarbonamide Creates Toxic By-Products When Heated

While azodicarbonamide is used to condition bread dough, when it’s baked, the heat causes it to break down. Two by-products can result: semicarbazide and ethyl carbamate.  Semicarbazide belongs to a family of chemicals known as hydrazines that are especially carcinogenic.  A 2003 study using animal models found that it caused free radical damage to DNA. [6] Other studies have found that semicarbazide damages human immune cells and the DNA of animals. [7]

The other half of the gruesome twosome is no better. The National Institute of Health’s Hazardous Substances Data Bank states that ethyl carbamate is a carcinogen to animals; in fact this is backed by over 200 studies. [8] [11] Research from 17 years ago confirmed that adding azodicarbonamide to bread increased ethyl carbamate levels. [12] The awful truth is that industry has known for nearly two decades that this is toxic trash and fed it to us anyway.

7. Harmful to Hormone Function

Exposure to semicarbazide can present another health risk. Animal studies have found it has a toxic impact on hormone function and the hormone-regulating organs, including the thyroid, thymus, spleen, testes, ovaries, and uterus. [9] [10] As is the case with all endocrine disrupting compounds, this stuff is poison!

8. Europe and Australia Have Banned It

While US Officials continue to claim the amount of azodicarbonamide found in most baked products poses no serious health threat, European and Australian officials have banned its use in bread.  Baby food jars were another source of exposure and officials were left without answers concerning the “safe levels” for infants. [13] Consequently, European officials disallowed its use in sealing glass jars.

9. Subway is Not the Only Violator

An NBC news piece released shortly after Subway’s bread revelation identified several other restaurants whose food contained azodicarbonamide.  These include McDonald’s, Burger King, Wendy’s, Arby’s, Jack in the Box, and Chick-fil-A. [14] Although not all bread from these restaurants may contain azodicarbonamide, is it worth the risk? Bottom line — if you want to avoid it, get in contact with the corporate big wigs who control restaurants from afar and verify they’ve made a pledge not to use any azodicarbonamide.

A Final Thought….

“Health officials” may claim this trash is safe in low doses, but who’s monitoring exposure?  And let’s face, at any level a toxin is a toxin.  If it doesn’t contribute to health, it’s taking away from it. As I’ve said for years, disease happens when toxic buildup in the body becomes too great. The best approach for encouraging good health continues to be eating a diet of natural, organic foods from trusted sources and regularly detoxifying your body.

– Dr. Edward F. Group III, DC, ND, DACBN, DCBCN, DABFM


  1. Pietzak M. Celiac disease, wheat allergy, and gluten sensitivity: when gluten free is not a fad.JPEN J Parenter Enteral Nutr. 2012 Jan;36(1 Suppl):68S-75S. doi: 10.1177/0148607111426276.
  2. Hernandez-Lahoz C, Mauri-Capdevila G, Vega-Villar J, Rodrigo L. [Neurological disorders associated with gluten sensitivity]. [Article in Spanish] Rev Neurol. 2011 Sep 1;53(5):287-300.
  3. Kim CW, Cho JH, Leem JH, Ryu JS, Lee HL, Hong YC. Occupational asthma due to azodicarbonamide. Yonsei Med J. 2004 Apr 30;45(2):325-9.
  4. Mr R. Cary, Dr S. Dobson, Mrs E. Ball. Azodicarbonamide. Concise International Chemical Assessment Document 16.  World Health Organization, 1999. (last accessed 2014-02-17)
  5. Tassignon J, Vandevelde M, Goldman M. Azodicarbonamide as a new T cell immunosuppressant: synergy with cyclosporin A. Clin Immunol. 2001 Jul;100(1):24-30.
  6. Hirakawa K, Midorikawa K, Oikawa S, Kawanishi S. Carcinogenic semicarbazide induces sequence-specific DNA damage through the generation of reactive oxygen species and the derived organic radicals. Mutat Res. 2003 Apr 20;536(1-2):91-101.
  7. Vlastos D, Moshou H, Epeoglou K. Evaluation of genotoxic effects of semicarbazide on cultured human lymphocytes and rat bone marrow. Food Chem Toxicol. 2010 Jan;48(1):209-14. doi: 10.1016/j.fct.2009.10.002. Epub 2009 Oct 9.
  8. NLM. METHYL CARBAMATE. (last accessed 2014-02-17)
  9. Maranghi F, Tassinari R, Lagatta V, Moracci G, Macrì C, Eusepi A, Di Virgilio A, Scattoni ML, Calamandrei G. Effects of the food contaminant semicarbazide following oral administration in juvenile Sprague-Dawley rats. Food Chem Toxicol. 2009 Feb;47(2):472-9. doi: 10.1016/j.fct.2008.12.003. Epub 2008 Dec 10.
  10. Maranghi F, Tassinari R, Marcoccia D, Altieri I, Catone T, De Angelis G, Testai E, Mastrangelo S, Evandri MG, Bolle P, Lorenzetti S. The food contaminant semicarbazide acts as an endocrine disrupter: Evidence from an integrated in vivo/in vitro approach. Chem Biol Interact. 2010 Jan 5;183(1):40-8. doi: 10.1016/j.cbi.2009.09.016.
  11. EPA. Ethyl Carbamate (Urethane). Hazard Summary-Created in April 1992; Revised in January 2000. (last accessed 2014-02-17)
  12. Dennis MJ, Massey RC, Ginn R, Parker I, Crews C, Zimmerli B, Zoller O, Rhyn P, Osborne B. The effect of azodicarbonamide concentrations on ethyl carbamate concentrations in bread and toast. Food Addit Contam. 1997 Jan;14(1):95-100.
  13. European Food Safety Authority. EFSA publishes further evaluation on semicarbazide in food.July 1, 2005. (last accessed 2014-02-17)
  14. Little, Katie. That Chemical Subway Ditched? McDonald’s, Wendy’s Use it Too. (last accessed 2014-02-17)

Bacteria may fight cancer.


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Escargot could follow the dodo, scientists warn.

France’s snails have been contaminated with the New Guinea flatworm, which could “wipe out” snail populations

Escargot, one of France’s signature dishes Photo: Alamy

 Snails, one of France’s signature dishes, could be off the menu if the country fails to stem an invasion by a slimy worm from Southeast Asia, scientists warned on Tuesday.

The warning is being sounded over a voracious species called the New Guinea flatworm.

It is already on a list of the 100 most dangerous invasive species in the world as it has a relentless appetite for native snails and earthworms in places where it has been introduced.

Workers at a botanical gardens in Caen, Normandy, called in scientific help after they spotted a strange, dark, flat-as-a-pancake worm among their greenhouse plants.

Reporting in the journal PeerJ on Tuesday, a team of French experts said DNA tests had confirmed their worst fears: Platydemus manokwari has arrived in Europe.

“This species is extraordinarily invasive,” said Jean-Lou Justine of the National Museum of Natural History. “I really hope it can be stopped at the earliest stages.”

He added: “All snails in Europe could be wiped out. It may seem ironic, but it’s worth pointing out the effect that this will have on French cooking.”

P. manokwari measures about five centimetres (two inches) long by five millimetres (a fifth of an inch) wide.

The back is black olive in colour, with a pale white belly where its mouth is located. The head is elongated, with two prominent black eyes.

It has been introduced, sometimes deliberately, in more than 15 countries and territories in the Pacific.

Biologists are alarmed by its appetite for snail.

The worm can even pursue gastropods up tree trunks – and when supplies of snails run out, it can tuck into other soil species, including earthworms.

The worm’s ancestral habitat is the mountains of New Guinea, at altitudes of 3,000 metres (10,000 feet) and above, where the temperature is moderate.

Tests have shown the worm can survive temperatures down to 10 degrees Celsius (50 degrees Fahrenheit), which gives it a good chance of surviving in temperate, snail-friendly parts of Europe.

“Platydemus manokwari represents a new and significant threat to biodiversity in France and Europe, which hosts hundreds of species of snails, some of which are endangered and protected,” said PeerJ, a publisher of peer-reviewed studies.

“It is therefore important to consider the implementation of eradication and control of this flatworm.”

P. manokwari has a distant cousin, the New Zealand flatworm (Arthurdendyus triangulatus), which has triggered an invasive-species scare in western Europe.

It has invaded the whole northern British Isles, and is blamed for big reductions in earthworms which play an essential part in aerating and fertilising the soil.

Other European countries have set in place monitoring measures in a bid to prevent it being imported through plants and agricultural products

Scientists work on backing up human brain with computers .

A new state-of-the-art headband is being developed by Tufts University scientists that could help facilitate communication between the human brain and computers.

The new technology – currently being crafted at the university’s Human Computer Interaction Lab – would be capable of scanning an individual’s brain activity, determining whether the person is mentally aware enough to handle the task at hand, fatigued, or even bored with what they’re doing.

AFP Photo / Emmanuel Dunand

According to the Boston Globe, this brain-scanning technology could potentially help humans perform a number of tasks, ranging from simple processes such as recommending movies based on individual reaction to important jobs in air traffic control. As the newspaper noted, the computer could learn “the precise moment an air traffic controller approaches mental overload, and [automatically] reassign some of his responsibilities to a fresher colleague.”

The headband does this by utilizing technology called functional infrared spectroscopy (fNIRS), which scans the amount of light being absorbed by the brain. In this way, the headband doesn’t exactly read thoughts, but since the amount of light absorbed by the brain is linked to the amount of brainpower it’s using, the device can gauge fatigue levels effectively through this measurement.

During a test run by Tufts researchers, one graduate student could manage between four and seven airplanes during a simulation, with the headband ensuring his mind wasn’t overexerted at any point in time.

If ultimately successful, computer scientist Robert Jacob and biomedical engineer Sergio Fantini hope to embed the tech in wearable products, such as Google Glass, and pave the way towards a future in which humans communicate with computers through thoughts and not tactile commands.

“Computers have gotten phenomenally better in the last 50 years — faster, more powerful — and humans haven’t,” Jacob told the Globe. “The bottleneck is now with the human, not the computer. So it’s important to put resources into communicating better with computers.”

“We’re basic researchers,” he added. “It would be delightful if these things do filter into the world, but I’d like to believe that’s not our mission. Our mission is to invent new scientific ideas and spread them, and hope they are useful to someone.”

Jacob’s team isn’t the only group looking into brain scanning technology, though. As RT reported last year, the Pentagon’s Defense Advanced Research Projects Agency (DARPA) announce it will invest $70 million to develop a new implant capable of tracking and responding to brain signals in real time.

The project, called “Systems-Based Neurotechnology for Emerging Therapies” (SUBNETS), is aimed at treating and analyzing mental disorders as they flare up in the mind. By creating an implant that can record the effectiveness of medical treatments as they’re administered, the implant could open up new avenues of treatment for patients.

Crystallizing Opportunities With Space Station Research.

In today’s A Lab Aloft, Dr. Larry DeLucas, a primary investigator for International Space Station studies on protein crystal growth in microgravity, explains the importance of such investigations and how they can lead to human health benefits.

We have many proteins in our body, but nobody knows just how many. Consider that the human genome project is more than 20,000 protein-coding genes, and many of these genes or portions of those genes combine with others to create new proteins. The human body could have anywhere from a half million to as many as two million proteins—we’re not sure. What we do know, is that these proteins control aspects of human health and understanding them is an important beginning step in developing and improving treatments for diseases and much more.

A protein crystal is a specific protein repeated over and over a hundred thousand times or more in a perfect lattice. Like a row of bricks on a wall, but in three dimensions. The more perfectly aligned that row of bricks or the protein in the crystal, the more we can learn of its nature. Today there are more than 50,000 proteins that have been crystallized and the structures of the three-dimensional proteins comprising these crystals have been determined. Unfortunately many important proteins that we would like to know the three-dimensional structures for have either resisted crystallization or have yielded crystals of such inferior quality that their structures cannot be determined.

Crystals of insulin grown in space (left) helped scientists determine the vital enzyme's structure with much higher resolution than possible with Earth-grown crystals (right). (NASA)

Crystals of insulin grown in space (left) helped scientists determine the vital enzyme’s structure with much higher resolution than possible with Earth-grown crystals (right). (NASA)

Once we have a usable protein crystal—one that is large and perfect enough to examine—the primary technique we use to determine the protein molecular structures is x-ray crystallography. When we expose protein crystals to an x-ray beam, we get what’s called constructive interference. This is where the diffracted x-rays coming from the electrons around each atom and each protein come together, providing a more intense diffraction spot. We collect hundreds of thousands, sometimes millions of diffraction spots for a protein. The more perfectly ordered the individual protein molecules are within the crystals, the more intense these spots. The higher signal to noise ratio in these strong spots creates an improved resolution of the structure, allowing us to map the crystal in detail.

Well-ordered protein crystal x-ray diffractions create sharp patterns of scattered light on film. Researchers can use a computer to generate a model of a protein molecule using patterns like this. (NASA)

Well-ordered protein crystal x-ray diffractions create sharp patterns of scattered light on film. Researchers can use a computer to generate a model of a protein molecule using patterns like this. (NASA)

Using computers, we take those diffraction spots and mathematically determine the structure of where every atom is in the protein. For example, in most protein structures we can’t even see the hydrogen atoms. We guess where they are because we know the length of a hydrogen bond. So if we see a nitrogen atom from an amino acid that we know has a hydrogen linked to it, and then at a hydrogen-bonding distance away we see an oxygen atom, then we can make an educated guess that the hydrogen is pointed towards that oxygen atom, so we position it there.

While we can grow high-resolution crystals both in space and on the ground, those grown in space are often more perfectly formed. That’s the main advantage and reason we’ve gone to space for these studies. In many cases where we could not see hydrogen crystals on the ground, we then flew that protein crystal in space and let them grow in microgravity. Because of the resulting improved order of the molecules laying down in the crystal lattice, we were able to actually see the hydrogen atoms. Usually to see the hydrogen atoms, you are talking about getting down to a resolution of one angstrom, which is not easy to do—it would take 10 million angstroms to equal one millimeter!

Another example of protein crystals grown in space (right), which are larger and more perfect than those grown on the ground (left). (JAXA)

Another example of protein crystals grown in space (right), which are larger and more perfect than those grown on the ground (left). (JAXA)

We also can look at bacteria and virus protein structures to identify how to target those proteins with drugs. Having this information is very important to pharmaceutical companies and universities. That structure provides a road map that is critical for the understanding of the life cycle of the bacteria or virus.

We’ve only done a fraction of the more important complex protein structures–I’m referring to membrane proteins and protein-protein complexes. Protein complexes are often composed of two, three or more proteins that interact together to form new macromolecular complexes that are often important in terms of disease and drug development. Membrane proteins are the targets for about 55 percent of the drugs on the market today. Scientists have determined the three-dimensional structures for less than 300 membrane protein structures thus far. However, there remain thousands more for which the structures would help scientists understand their important roles in chronic and infectious diseases.

When we see a specific region in a protein and we know exactly where every atom is, chemists can design drugs that will interact in those regions. We can take some of the drugs they design that work, but maybe not as well as we would like. We then grow new crystals of the protein with the drug attached to the protein to see exactly how it’s bound to the protein. That lets other scientists—modelers—determine very clearly how the drug interacts with the protein, information that enables them to design new, more effective compounds. This whole process is called structure-based drug design.

The International Space Station provides a unique environment where we can improve the quality of protein crystals. During the days of protein crystallization studies on the space shuttle, one of the most frustrating aspects of the microgravity experiments was the length of time it took to produce a usable crystal. This is actually part of why space-developed crystals are better—they grow much more slowly. On the shuttle you only had 10-12 days for a study, but aboard the space station you have as long as you need.

As an astronaut and scientist, I personally flew a record 14-day flight in 1992 where we studied 31 proteins. I was looking at results and planning to set up new experiments, changing the chemical conditions to optimize the crystallization. The rule for my sample selection was that the proteins had to nucleate—that means to begin to grow a crystal—and grow to full size in three days. Once I got up there, however, by the third day nothing had nucleated. I was worried, but then on the fourth day I could see little sparkles where crystals had started to grow in about half of the proteins. By mission end I was really only able to optimize the crystal growth for six of the proteins. How much longer it takes a crystal to nucleate and grow to full size was a dramatic discovery.

Astronaut Larry DeLucas, payload specialist, handles a Protein Crystal Growth (PCG) sample at the multipurpose glovebox aboard the Earth-orbiting space shuttle Columbia. (NASA)

Astronaut Larry DeLucas, payload specialist, handles a Protein Crystal Growth (PCG) sample at the multipurpose glovebox aboard the Earth-orbiting space shuttle Columbia. (NASA)

With constant access to a microgravity lab, such as the space station, I am confident that we can improve the quality of any crystal. With protein crystals it is important to note that just because we get a better structure with higher resolution, it doesn’t at all mean it’s going to lead to a drug.

The ability to grow good crystals typically involves a great deal of preparation on the ground where we first express and purify and grow the initial crystals. But if space can give you higher resolution, there’s no drug discovery program that’s going to take a lower resolution option. From the time you determine that structure and chemists work with it, the typical time frame to develop a drug is 15 to 20 years and the cost is around a billion dollars. Identifying the structure of the protein crystal is only the first step. Many times even with the structure a project goes nowhere because the drugs they develop end up being unusable. There are so many aspects to drug discovery beyond the opening act of structure mapping.

If crystals and the structure of a target protein are available, pharmaceutical and biotech companies certainly prefer to use that structure to help guide the drug discovery. After the first 18 months they’ve developed the drug candidates, they may not need to use the crystal structure again for say 10 years. During that time they are doing clinical trials and pharmacology. The majority of the money it takes to get a drug approved by the FDA is after the initial phase. If you break down what they say is about a billion dollars to develop a drug, the portion needed to get the structure up front will range from half to two million dollars—a small fraction of the whole process.

View of Expedition 28 Flight Engineer Satoshi Furukawa with the JAXA Protein Crystal Growth (PCG) investigation aboard the International Space Station Japanese Experiment Module (JEM). (NASA)

View of Expedition 28 Flight Engineer Satoshi Furukawa with the JAXA Protein Crystal Growth (PCG) investigation aboard the International Space Station Japanese Experiment Module (JEM). (NASA)

For the upcoming Comprehensive Evaluation of Microgravity Protein Crystallization investigation we focused on two things. First, we selected proteins that are of high value based on their biology. Having this information of their structure can lead to new information about structural biology—how proteins work in our body. The other major requirement for the candidates for selection was that the proteins had to have already been crystallized on Earth, but the Earth-grown crystals were not of good quality.

We are flying 100 proteins to the space station on SpaceX-3, currently scheduled for March 2014. Twenty-two of these are membrane proteins, 12 are protein complexes, and the rest are aqueousproteins important for the biology we will learn from their structures. The associated disease was the last thing we considered, as we were looking at the bigger picture of the biology. That being said, for the upcoming proteins flying you can almost name a disease: cystic fibrosis, diabetes; several types of cancer, including colon and prostate; many antibacterial proteins; antifungals; etc. There are even some involved with understanding how cells produce energy, which I suspect could lead to a better understanding of molecular energy.

Not long ago a Nobel Prize was awarded for the mapping of the ribosomes complex protein structure. This key cellular structure will also fly for study aboard the space station, because the resolution was not all that great using the ground-grown crystals. We now have the chance to learn more about how the ribosomes actually makes proteins and clarify the whole process. This is just one of the exciting projects flying in relation to protein crystal growth.

Crystallized structure of a nucleosome core particle that was grown aboard the Mir space station. (NASA)

Crystallized structure of a nucleosome core particle that was grown aboard the Mir space station. (NASA)

This space station experimentation is a double blind study. This means that all the experiment chambers are bar coded for anonymity. We also will have exact controls done with the exact same batch of proteins prepared at the same time. The crystals will grow for the same length of time, as they are activated simultaneously in space and on the ground. When the samples come down, we will perform the entire analysis not knowing which are samples grown in space versus Earth. Only one engineer will have the key to the bar codes. When we’re completely done with the analysis, then he will let us know which were from space or ground. This will allow our study to provide definitive data on the value of space crystallization.

We also wanted to ensure that our analysis looked at a sufficient number of samples, statistically speaking, to provide conclusive data. How many data sets we collect per crystal sample will depend on the quality of that crystal. Statistically the study will be relevant in terms of how many proteins we fly, as well as how many crystals we evaluate from space and ground to make the comparison.

Astronaut Nicole Stott works with the high-density protein crystal growth (HDPCG) apparatus aboard the International Space Station. (NASA)

Astronaut Nicole Stott works with the high-density protein crystal growth (HDPCG) apparatus aboard the International Space Station. (NASA)

The microgravity environment is so beneficial because it allows the crystals to grow freely. Without the gravitational force obscuring the crystal molecules, as seen on Earth, the crystals can reveal their full form. We are giving all of these protein crystals the chance to grow to their full size in aquiescent environment. This is a very important investigation, not only because of the high number of proteins we are flying, but the statistical way we will evaluate them. Based on the results of the study, we will know if PCG in space is worth continuing.

Once the crystals come back to Earth, it will take at least one year to complete the full analysis. However, we will likely know that we’ve got some exciting results within the first three months. To publish something, it will be at least a year to complete the analysis, as we will have about 1,400 data sets to analyze. These results will determine the future of microgravity protein crystallization.

Cecal Volvulus Imaging

The plain abdominal radiograph is usually the key to the diagnosis of cecal volvulus. In axial torsion, the image may show a markedly distended loop of large bowel with its long axis extending from the right lower quadrant to the epigastrium or left upper quadrant, the most common site to which the cecum is displaced (see the image below). Depending on the initial bowel position and the length of mobile right colon, the distended cecum may be seen anywhere in the abdomen.

Plain supine abdominal radiograph from an 81-year-

Plain supine abdominal radiograph from an 81-year-old man presenting with abdominal pain and vomiting. The radiograph shows a markedly distended loop of bowel 15-cm in diameter with its axis running from the right lower quadrant to the mid abdomen. This loop of bowel represent a twisted cecum with the caput cecum directed medially (arrows). The haustra within the cecum (C) are effaced. Note the proximal dilated loop of small bowel. The distal colon shows little if any air. At surgery a cecal volvulus was confirmed.

Despite the varying positions of the distended cecum, the plain radiographic features of a cecal volvulus are characteristic, and the caput cecum can typically be identified (see the first image below). The colonic haustral pattern is generally maintained, although some effacement may be present if superimposed ischemia is present. When shorter segments of the colon and cecum are involved, the distended cecum may be found in the normal location (see the second image below).

A 53-year-old woman presented with clinical featur

A 53-year-old woman presented with clinical features of intestinal obstruction. This plain supine radiograph was performed on the day of admission. It shows a large air-filled viscus (15 cm in diameter), with the axis running from the mid abdomen to the left hypochondrium. No haustra are seen in the air-filled viscus (short arrow). Note that the right iliac fossa is empty (long arrow), but formed feces intermingled with air are noted in part of the ascending colon. The air can be traced up to the rectum. At this stage, no firm radiologic diagnosis was entertained, although the working clinical diagnosis was partial bowel obstruction.This plain supine radiograph was obtained 24 hours

This plain supine radiograph was obtained 24 hours after the radiograph in the previous image (from a 53-year-old woman who presented with clinical features of intestinal obstruction). The position of the air filled viscus has changed and suggests that the air-filled viscus is mobile. The viscus now looks much more like a cecum. The caput cecum is directed toward the right iliac fossa. The twist is outlined by air (arrows).

In most patients, obstruction is almost complete; thus, the distal colon is usually empty and the small bowel is frequently distended. Occasionally, a long-axis torsion may be associated with signs of incomplete obstruction. Rarely, small-bowel loops are identified to the right of the distended cecum and ascending colon. The ileocecal valve may possibly be identified, and on occasion, the point of torsion may be outlined by gas, as an area of conelike narrowing.

In the cecal bascule form of volvulus, the distended air-filled cecum is located more centrally. With this variant, the ileum can passively twist with the cecum, and small bowel is not obstructed. If the appendix is filled with gas and in an unusual location attached to a distended cecum, the diagnosis can be made readily.

Single contrast barium enema examination is generally adequate for the evaluation of cecal volvulus. A double-contrast barium enema study does not confer any significant advantage, because no fine detail is necessary to make the diagnosis. The administration of glucagon is often necessary, because patients may have considerable colonic spasm and find it difficult to retain the contrast agent.

The barium enema study shows a nondilated distal colon to the point of twist (see the following images). If the obstruction is not complete, some barium may trickle past the site of obstruction, and the twist may be visualized in more detail. If the twist occurs along the transverse axis, the obstruction appears relatively smooth, and no spiral twist is usually seen. In a cecal bascule, a rounded termination of the barium column may be seen. This, when seen near a distended gas-filled viscus, should alert the radiologist to the diagnosis of a volvulus.

This unprepared barium enema examination was obtai

This unprepared barium enema examination was obtained 12 hours after the first supine plain radiograph from a 53-year-old woman who presented with clinical features of intestinal obstruction. The image shows a nondilated colon. The barium-filled colon can be traced back to the right iliac fossa where there is a bird-beak cutoff (solid arrow). The dilated cecum lies in the epigastrium .where there is an air fluid level (open arrow). Note that the barium has not entered the cecum

Right oblique image from a barium enema examinatio

Right oblique image from a barium enema examination in from a 53-year-old woman who presented with clinical features of intestinal obstruction. This image shows a bird-beak appearance (arrow). At surgery, a cecal volvulus was confirmed.Left: Plain abdominal radiograph from a 48-year-ol

Left: Plain abdominal radiograph from a 48-year-old woman showing a massively distended and medially displaced proximal ascending colon and cecum. The cecal pole is now lying in the left upper abdominal quadrant (C). At least 2 or 3 haustrations are seen in the distended large bowel, which is consistent with cecal volvulus. No air fluid levels were demonstrated in this case. Right: A single contrast barium study of the same patient showing free barium flow through the sigmoid colon in to the mid ascending colon. The proximal ascending colon and the cecum are void of barium due to obstruction at the level of the mid ascending colon

.A post evacuation film from the same 48-year-old p

A post evacuation film from the same 48-year-old patient as in the previous images. This image shows a medially pointed end column of the barium (beak sign) in the mid ascending colon. Distally the large bowel is distended with gas and represents the cecal volvulus.

As little barium as possible should be allowed to flow proximal to the site of obstruction, because flooding the bowel proximal to the obstruction site might precipitate a complete obstruction. When the barium enema is administered, overdistention should also be avoided, because this can lead to perforation. An attempt should always be made to reduce the volvulus. This reduction may be achieved during colonic filling by barium, but reduction occasionally occurs during barium evacuation. With an intermittent volvulus, the barium enema results may be normal, but a postevacuation radiograph may reveal the twist.[9, 11]

Degree of confidence

Plain radiographic findings can be diagnostic of a cecal volvulus in most patients. In others, the findings on the plain images only suggest the diagnosis, and barium enema examination is necessary to confirm the diagnosis.

False positives/negatives

Rarely, the dilated displaced cecum and ascending colon in the left upper quadrant may be confused with a normal or abnormally distended stomach. A redundant looplike cecal volvulus may be confused with a sigmoid volvulus. In the presence of a double obstruction of the colon (left colon obstruction associated with a cecal volvulus), evaluation of the right colon may not be possible, and the diagnosis of volvulus must be based on plain radiographic findings alone.

Facebook reportedly in talks to buy drone manufacturer

Social network could use high-altitude craft as part of it’s internet.orginitiative, providing internet access to developing markets.

Facebook is reportedly in talks to buy Titan Aerospace, makers of solar-powered, high-altitude drones that can stay aloft for up to five years at a time.

It’s thought that the social network is interested in using the aircraft to provide internet access in developing markets as part of its internet.org initiative.

This project, launched by Mark Zuckerberg last August in partnership with companies including Nokia and Qualcomm, aims to cut the cost of internet access across the world and connect “the next five billion people” to the web.

Reports from TechCrunch suggest that Facebook is interested in buying the drone manufacturer for $60 million and would begin by building 11,000 Solara 60 aircraft to provide internet access in Africa.

Titan Aerospace, a private company with research and development facilities in New Mexico, unveiled its Solara 50 and Solara 60 unmanned aerial vehicles last year, marketing them as extremely cheap alternatives to satellites.

The craft can be launched at night powered by an internal battery and once airborne use solar panels embedded into their 160-foot long wingspan to power them. The aircraft have a mission range of over 4 million kilometres and operate at an altitude of 65,000 feet.

This places them well above commercial airliners flying at around 30,000 feet, as well as regulated air-space in the US (the FAA’s jurisdiction goes up to 60,000 feet) while the high altitude also means that they are out of reach of turbulence, sitting in a calm atmospheric area known as the tropopause.

Speaking to Fortune magazine last year, Titan Aerospace chief electrical engineer Dustin Sanders said that the company wanted to create a “single-million-dollar-per-aircraft platform” as opposed to the billions involved in launching a satellite.

“The operation cost is almost nothing,” said Sanders “You’re paying some dude to watch the payload and make sure the aircraft doesn’t do anything stupid.”

If Facebook does follow through on this acquisition it would put them into direct competition with Google’s own ‘Project Loon’, a similar initiative that aims to provide internet via a network of high-altitude weather balloons.

The Solara 50 drone.

Both Facebook and Google’s projects have been criticized in the past for disguising commercial goals as altruism. Microsoft founder Bill Gates was among those who spoke out, noting last year in an interview with Businessweek that “when a kid gets diarrhea, no, there’s no website that relieves that.”

Facebook’s interest in providing even slow internet to new parts of the world would also complement its recent acquisition of WhatsApp, a simple mobile messaging service that uses relatively small amounts of data to replace SMS and MMS text messaging.

While a ‘drone project’ might sound like a significant development for Zuckerberg’s social network, it’s worth remembering that the price being mooted for Titan Aerospace ($60 million) is a fraction of what the company paid for WhatsApp ($19 billion).

Plant may help floppy baby syndrome.

Professor Tom Gillingwater
The researchers hope better versions of quercetin can be created that are more effective than the naturally-occurring chemical

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A chemical found in plants could help improve the lives of babies with a rare muscle disease, a study has found.

Edinburgh University scientists hope the quercetin extract will pave the way for new treatments to ease the symptoms of incurable spinal muscular atrophy.

The disease, known as floppy baby syndrome, leaves children with little or no control of their movements.

One in 6,000 babies are affected by the condition, and about half with the most severe form will die by the age of two.

Edinburgh University experts found evidence that quercetin, found in some fruits, vegetables, herbs and grains, could help prevent damage to nerves associated with spinal muscular atrophy (SMA).

The chemical targets the build-up of a specific molecule inside cells, called beta-catenin, that is responsible for some of the symptoms of the condition.

Tests of a purified form of the extract on zebrafish, flies and mice led to a significant improvement in the health of nerve and muscle cells.

Prof Tom Gillingwater, of Edinburgh University, said: “This is an important step that could one day improve quality of life for the babies affected by this condition and their families.

“There is currently no cure for this kind of neuromuscular disorder so new treatments that can tackle the progression of disease are urgently needed.”

It is hoped better versions of quercetin can be created that are more effective than the naturally-occurring chemical.

Silk screws used to repair fractures.

Silk screws

The screws were made from silk spun by the silk worm
Screws made from 100% silk have been used to repair broken bones in research that could transform surgery.

US scientists say metal fixtures can potentially be replaced with plates and screws made from the natural fibre, which will eventually dissolve in the body.

So far the technique has only been tested on rodents.

Silk was once used to make sutures, but more recently has been used in modern medical implants.

“Start Quote

We envision a whole set of orthopaedic devices for repair based on this – from plates and screws to almost any kind of device you can think of where you don’t want hardware left in the body”

David KaplanTufts University

In the new research, a team of medical engineers at Tufts University, Massachusetts, made screws from medical grade silk using specially designed moulds.

The silk material can be cut to different sizes on a machine.

The screws were implanted into the hind limbs of rats, where they functioned successfully for four to eight weeks.

By the end of the study, the silk had started to dissolve.

The low stiffness of silk, which is similar to that of bone, and its ability to break down in the body, make it a promising bioengineering material compared with traditional metal plates and screws, the researchers say.

Lead researcher Dr David Kaplan told BBC News: “The future is very exciting. We envision a whole set of orthopaedic devices for repair based on this – from plates and screws to almost any kind of device you can think of where you don’t want hardware left in the body.”

He added: “They don’t interfere with X-rays, they don’t set off alarms and they don’t cause sensitivity to cold.”

Recently, German researchers coated silicone breast implants with a thin layer of bioengineered silk proteins.

Preclinical studies suggest the coating reduces or prevents painful reactions.

New magnetic material discovered

A highly sensitive magnetic material that could transform computer hard drives and energy storage devices has been discovered.

The metal bilayer needs only a small shift in temperature to dramatically alter its magnetism – a tremendously useful property in electronic engineering.

Computer hard disk

“No other material known to man can do this. It’s a huge effect. And we can engineer it,” said Ivan Schuller, of the University of California, San Diego.

He presented his findings at the American Physical Society meeting in Denver.

The material combines thin layers of nickel and vanadium oxide, creating a structure that is surprisingly responsive to heat.

“We can control the magnetism in just a narrow range of temperature – without applying a magnetic field. And in principle we could also control it with voltage or current,” said Prof Schuller.

“At low temperatures, the oxide is an insulator. At high temperatures it’s a metal. And in between it becomes this strange material,” he said.

Although it’s too early to say exactly how it will be used, Prof Schuller sees an obvious opportunity in computing memory systems.

“A problem with magnetic memory is reversibility – you want it to be reversible but also stable.

“Today’s best systems are heat-assisted, but they use lasers, which involves a lot of heat. But with this new material, you barely need to heat it by 20 degrees (Kelvin) to get a five-fold change in coercivity (magnetic resistance),” he told the conference.

Another potential use is in electricity networks. Prof Schuller envisions a new type of transformer which can cope with sudden surges in current – such as during a lightning strike or a power surge.

But he points out that new phenomena such as this often lead to entirely unexpected technologies.

He gave the example of giant magnetoresistance – a discovery that radically miniaturised hard drives in digital devices, and won the 2007 Nobel prize.

“Without it, that computer you’re writing on would not work,” he told the meeting.

“So if you want to find the next transformative technology, this is the type of research you do. We don’t know what the best application is yet,” he said.

“I’m not saying it’s going to solve world’s energy crisis but it’s certainly going to help us.”