There are many ways to treat disease. Vaccines are proactive, providing immunity to disease. Vaccines act like a “weakened” form of the disease, causing the body to generate antibodies that prevent illness when the real thing comes along. Vaccination is one of the main reasons why some deadly pathogens have all but disappeared. Take polio, for instance: once widespread, the disease is now rare in the Western world, and the WHO is aiming for a polio-free planet by 2018. Conversely, the unfounded phobia of vaccination has led to recent outbreaks of measles in the United States, Canada, and Mexico, including the highly publicized outbreak at Disneyland, California.

Vaccines work, but they can also have drawbacks. They can be expensive to make, requiring a combination of highly trained scientists, specialized equipment, and loads of funding. Their production can be resource-intensive and wasteful, typically requiring chicken eggs to help incubate the disease pathogens. An egg per vaccine may not seem like much, but hundreds of millions of vaccines are given each year, requiring the production of millions of nutritious eggs. Moreover, producing a vaccine can be slow, much too slow when considering the fast spread of many diseases, such as Ebola. But, surprisingly, it is the viruses themselves that hold some of the answers for speeding up vaccine production.

Viruses are icky. When a friend says, “I got a virus,” most of us take a step back, and for good reason. If you saw in detail how viruses work, you’d be more than creeped out. Ever seen a picture of a standard bacteria-targeting virus, like a bacteriophage? When these nasty critters land on a poor, unsuspecting bacterium, they insert their own genetic information into the host. The viral genes hijack the bacterial cell, take control of the cellular machinery, and use it to create more copies of the virus. And when the cell is finally filled to the brim with viral clones, the cell ruptures, spilling out hundreds of identical viruses into the world. And you thought your roommate’s mooching was bad.

In other words, a virus functions by inserting its own genes into a host genome, and then host proteins turn those viral genes into viral proteins and ultimately more viruses. The in-house enzymes can’t differentiate between viral and host genes. Moreover, the genes of viruses, bacteria, and humans are all decoded using the same universal language. This means that viruses could be engineered to deliver “good” instead of “bad” genes. For instance, viruses could be used as vectors for making and delivering antibodies to combat disease, which is exactly what scientists have in mind.

On paper, viral delivery vaccination systems and other types of genetically engineered vaccines are an upgrade to traditional egg-based vaccines. They’re fast to make — weeks not months. They’re efficient, partly because much of the vaccine genetic sequence analysis and engineering can be performed on computers using bioinformatics. And they require no eggs to incubate, no technicians to keep watch. In fact, the process is catered to automation and mass-production. Consider this: the annual flu vaccine begins production in February, well before the sniffles and coughs arrive. Specialists then get together to predict the three most common variants of the flu for next year. It’s really a whole lot of guesswork and, as such, their predictions can be hit or miss. But imagine if you could deliver an effective flu vaccine a mere week after the season begins! The effectiveness of flu vaccines would skyrocket.

Of course, there are downsides. Most importantly, control: how do we make sure that the “hijacked” cells don’t just keep pumping out antibodies? Science is still working on a functional off-switch for these other kinds of recombinant vaccines, but they’ve got an idea. Specialized vaccines provide immunity for a certain period of time before a booster shot must be reapplied. No booster, no immunity, no problem.

How far off are these vaccines? They’re already here. The Centre for Disease Prevention and Control (CDC) began research in 2013, and currently theirs is a seasonal flu vaccine that takes advantage of these kinds of methods. Vaccine approval processes take a long time, and the FDA is a mess of bureaucracy and red tape. But with the emergence of Ebola, the CDC may finally have the public support necessary to push through these developments. Many have hailed so called “viral vaccines” as the next big step in disease prevention. If anything, it shows that science is always ready to learn and find inspiration from nature.

Dennis He is an undergraduate science student at the University of Western Ontario. Stick him in a room with strangers and he’ll likely know the most about ancient Roman history, the best napping locations on campus, and how to make delicious chicken potpie. In his free time, he enjoys riding bikes downhill really, really fast. This essay resulted from a science writing internship with Prof. David Smith, Western University (www.arrogantgenome.com).

This semiotic inquiry was motivated by the limitations of the molecular biology approach. Presently, molecular and organismic biology are two diverging sciences and biosemiotics hopes to bridge these two.

And it believes that signals are the key. These signals may be chemical, visual, auditory, or tactile in nature.

Not too long ago, it was believed that the world is ordered, and causality and determinism form two important aspects of classical physics. However, chaos theory then came along. Chaos (which can be observed in deterministic systems) has important connotations in the biological realm, and is closely linked to biosemiotics as a teaching of signals and signs.

This close relationship between biology and deterministic chaos can be observed in their shared features, such as,

• complexity | interdependence, interactions
• non-equilibrium, irreversible
• sensitivity to initial conditions
• nonlinearity

The network of information and signals between organisms (as well as within a creature) unveils a nonlinear, emergent, chaotic, and unpredictable facet of biology.

Jakob von Uexküll had the idea of applying a semiotic outlook to studying organisms. He presented the notion of umwelt, which means environment in German. Unlike most ecologists, Uexküll speculated that organisms may not necessarily have the same umwelt even when they share a common environment. Umwelt here refers to a network of signs, as construed by a creature; it can therefore be viewed as a means of communication within a living system, like language. In several cases, it gets partly conveyed through chemical, acoustic, and visual cues.

The concept of umwelt is outlined by Dorion Sagan (son of Carl Sagan) in the introduction of the translated book, A Foray Into the Worlds of Animals and Humans: With a Theory of Meaning:

Unlike the reductionist approach, which treats signs and messages as metaphors that can be explained through chemical reactions, biosemiotics extends to related fields; it is open to the idea that signs might be more than just cultural commodities. Humans evolved from animals, which implies that culture does have biological origins. We also have several examples of animal behavior and psychology that suggest sign-mediated communication is a significant aspect of life, and should complement human semiotics, something which Thomas Sebeok, a semiotician, boldly suggested in the 1960s.

It is going to be exciting to see what this novel academic pursuit has store for the future, particularly how it will complement natural selection. And yet, with time, we might even discover that some of these ‘new’ visions have been latent in the works of von Baer, N. Wiener, D’Arcy Wentworth Thompson, Levi-Strauss, Stuart Kauffman, René Thom, Spemann, Waddington, Brian Goodwin, and several others. Some of these ideas include:

- systems biology | emergent properties , systems/holistic thinking
- mathematical biology
- developmental/epigenetic biology
- structuralism | in governing of species
- morphogenesis
- improving Darwinism

- mind body problem
- free will
- novel physics | poised realm
- information

Until then, the late Terry Pratchett’s words can describe our stupefaction, “No one knows the reason for all this, but it is probably quantum”.

Little more than half the size of our own moon, Pluto has always been presumed to be a dead, frozen planet only a few tens of degrees above absolute zero – literally a failed planet, officially demoted to ‘dwarf planet’ a few years ago. But could we be in for a surprise? Could the last dark corner of the solar system throw us a curveball?

NASA’s New Horizons probe has been speeding towards Pluto for almost a decade, getting a gravity assist from Jupiter in 2007 to help it cover the immense 5 billion kilometers to its target. Its cameras started to distinguish Pluto as more than just a speck of light around February of this year, but by April the images showed a hint of two blurry white polar caps, raising the intriguing possibility of ice deposits on its surface.

By early June the images were indicating not simply two polar caps but a more complex pattern of different light and dark regions including bands of lighter terrain as well as a large dark area, suggesting perhaps different geological zones, as well as a lumpy surface possibly indicative of large impact craters or maybe even a large chunk missing from one side.

Image Credit: NASA

Over the coming two weeks, the images should get much more detailed, enough to meet the primary goal of the mission to characterize the surface geology and morphology of both Pluto and its largest moon, Charon. However, travelling at 14 km/s, it will be going too fast to go into orbit around Pluto, so the plan is for it to take as many images and measurements as it can as it zips past the dwarf planet, something it will do in less than 4 minutes at around lunchtime on 14 July.

And then what? New Horizons will fly on into the Kuiper Belt, a huge region of small asteroids about twenty times wider than the asteroid belt between Mars and Jupiter. The ambition is to fly by some of these objects – but with its fuel almost gone, batteries fading and at the limit of its communications, it is pot luck what it will find. Any objects that it does encounter are likely to be no more than 50 km across, too small to see from Earth at that distance.

But Pluto is far from being the outer limit of our solar system. A handful of other dwarf planets have been found in recent years, the so-called Trans-Neptunian Objects (TNOs). TNOs range from a similar size to Pluto down to about a fifth of its diameter. The furthest, Sedna, orbits the sun a massive three times further out than Pluto. Sadly New Horizons will not reach any of them before its batteries run out, so the enigmatic worlds of the colourfully-named Eris, Makemake, Haumea, Sedna, Quaoar and Orcus will have to wait for another generation.

Other surprises have been found in the past few months. Another NASA probe, Dawn, is now in orbit around Ceres, the largest object in the asteroid belt beyond Mars, and roughly half the size of Pluto. For the most part, Ceres has looked much as you would expect an asteroid to look: a heavily cratered miniature version of our own moon. Except for one bizarre and so far unexplained feature – a series of extremely bright spots, so bright they look as though they’ve been painted on with reflective paint. Favourite theories so far are salt deposits or ice, both of which then beg the question of how they got there.

It seems that however far we go in our exploration of the solar system, surprises are always in store.

The Ceres bright spots imaged by Dawn from 4,400 km. This strange group of highly reflective areas are scattered over a region 90 km across. Image credit: NASA.

How does it work?

Qi (pronounced “Chee”) wireless works on the basis of a wireless charger that uses inductive charging via a magnetic current, which transmits energy. It creates a magnetic field, which allows the device to be charged wirelessly when the charger and the gadget connect. Once the device is placed onto the flat surface of the charger, it will be charged via the invisible coil-like energy.

The only limitation is that the device must have the appropriate hardware and a chipset that supports wireless charging. In addition, companies using the wireless charger have not settled on a single standard platform for charging. Currently, there are three preferred standards in wireless charging: Qi, PMA (Power Matter Alliance), Powermat, and A4WP (Alliance for Wireless Power).

Current adoption of wireless charging

Among the industries that use wireless charging, the mobile technology department is one that has the most potential, especially since consumers are always looking for innovative solutions to solve poor battery life issues with their smartphones.

Some of today’s mobile manufacturers are maximizing Qi power in charging their latest handsets. An example of this is the Samsung and their Galaxy S6 smartphone. Since the release of their Galaxy Note 4, the company has been trying to incorporate the technology in their latest smartphones and phablets. Based on a featured post by O2 on the Galaxy S6, the handset comes with a wireless charger that promises faster charging and longer battery life. A 10-minute charge can provide up to four hours of ‘normal’ battery life, while it will only take 1.5 hours of charging to reach a full charge. Other mobile companies have also adopted Qi Wireless, such as the Nokia, LG, and several Motorola handsets.

Aside from several mobile companies, there are well-known international companies that are also showcasing wireless charging on many of their products, including Qi or Wireless Power Consortium (WPC), WiPower, PowerByProxi, and Mojo Mobility.

The future of Qi Charging

In the coming months and years, it is expected that more mobile companies will start using Qi Wireless charging. Along with mobile industries, car manufacturers and government agencies are also looking into using the technology for electric vehicles. Last year, the UK’s Highways Agency Commissions released a feasibility study that suggested that roads could be filled with dynamic wireless transfer devices to power electric cars, which is said to “support and accelerate the introduction of [electric vehicles] in the UK and elsewhere in the world.” Currently, they are still seeking engagement and support from government representatives, road user organizations, vehicle manufacturers, and local authorities regarding said project.

With the rise in the demand for more convenient, faster, and eco-friendly solutions to tech items, it is expected that more if not all tech companies will soon fully embrace Qi Wireless in their processes, products, and services. In fact, charging items at home has been introduced by IKEA on a large scale, as they are firmly behind wireless charging.

As developers continue to upgrade their technological devices to be smarter, it is only a matter of time before all tech companies adopt and introduce Qi wireless charging to their product lines. And it won’t be long before we live in a fully functioning wireless society.

William “Bill” Ja studies fruit flies to research the affects of diet on aging and longevity. He believes that “flies have long served as good models for mammals.” His recent research on flies has shown that a high protein diet can actually shorten their lives. Similar research findings have been found independently through Kwang Pum Lee, a professor at The University of Sydney, Australia; Stephen J. Simpson, also a professor at The University of Sydney, Australia; and Valter D. Longo, a professor from The Davis School of Gerontology at the University of Southern California. These scientists agree: the length of an organism’s life can be shortened by eating too much protein.

It seems ironic that we can eat too much protein when our bodies are composed mostly of protein. Hair, skin, muscles, organs are all basically protein-based parts of our biological machines. And as with any machine, it wears down through constant use. To counter this wear, we need to consume protein to rebuild and restore any loss. However, it appears that we don’t need a lot of protein for restoration.

According to the Centers of Disease Control and Prevention (CDC) a complete restoration for most of us can be achieved by eating as little as 10% of our daily caloric intake in the form of protein, which, for the average adult consuming 2000 calories per day, is about 50 grams per day (50 grams of animal-derived protein is about 2 eggs and a 4 ounce chicken breast, while 50 grams of plant-based protein is about 1 cup of oatmeal, 1 cup of soy milk, 2 slices Whole Wheat Bread, 1 cup of vegan baked beans, 1 cup of broccoli, 1 cup of brown rice, 2 Tbsp of almonds, 2 Tbsp of peanut butter and 6 crackers). So, if we eat more protein than we need, we create excess protein, and through a complicated process, excess protein can cause a wave of cell damaging free radicals.

Free radicals are molecules that carry an imbalance in their atomic structures: specifically they need an electron to regain a balanced state. To get this missing electron, free radicals will tear it from any molecule nearby, including protein molecules. When free radicals attack protein, it becomes oxidized protein. Oxidized protein is damaged protein.

Because our cells are made of protein, they too can become damaged through oxidation, the results of which may lead to heart disease, cancer, and diabetes. According to these researchers, if we constantly ingest more protein than we need, a lifespan shortened by disease may be in store for us.

Kwang Pum Lee, reporting his research results in the peer-reviewed Proceedings of the National Academy of Sciences, fed fruit flies a variety of meals with different ratios of proteins and carbohydrates, namely 1:2, 1:4, and 1:16, (the 1s on the left side of the colon represent 1 calorie of protein, while the 2, 4, and 16 on the right side of the colon represent calories of carbohydrates). When Lee fed his fruit flies high protein diets, the 1:2 and 1:4 ratios, their median life span was 25.5 days and 35.9 days, respectively. When Lee fed a third group a low protein, 1:16 diet, the flies achieved a median life span of 56.7 days.

Bill Ja, reporting in the journal Experimental Gerontology, repeated close variations of Lee’s experiments with similar results. Bill also found that a low protein, 1:16 diet, achieved the longest lifespan. According to Bill Ja, “the high carb ratio diet is indeed better” for longevity.

Stephen Simpson, publishing in the peer-reviewed journal Cell Metabolism, arrived at similar results, but with mice. He fed 858 mice one of 25 diets that differed in their ratios of protein, carbohydrate, and fat content. The interactions between the nutrients were complicated. To help penetrate the complexity, Stephen utilized Geometric Framework (GF) – a statistical tool that made it possible “to disentangle the individual and interactive influences of multiple nutrients.”

By applying GF to the interactions between proteins, carbohydrates, and fats, Stephen discovered: “the longest median survival occurred in cohorts of mice on the lowest ratio diets, and there was a clear correlation between the ratio and lifespan. Median lifespan increased from about 95 to 125 weeks (approximately 30%) as the protein-to-carbohydrate ratio decreased.” Stephen concluded that “lifespan was greatest for animals whose intakes were low in protein and high in carbohydrate.”

The results obtained by the researcher, Valter D. Longo, who also published in Cell Metabolism, agreed with the preceding studies, except this time humans were the focus. Valter studied the diets of 6,381 adults ages 50 and over. The participants were part of the largest nutrition survey in the United States, the NHANES III. The size and scope of the survey gave Valter the statistical power to confidently say that people “aged 50–65 reporting high protein intake had a 75% increase in overall mortality and a 4-fold increase in cancer death risk.” Dr. Longo defined a high protein diet as a diet that consisted of eating 20% or more of one’s daily caloric intake in the form of protein.

To demonstrate the complexity of nutrition, Valter also found that people over the age of 65 actually do better on a high protein diet as more protein seems to help counter the natural frailty that occurs with older bodies. By eating extra protein, an elderly person can build bodily reserves to help weather the storms of age-related diseases. For adults 65 and younger, eating 20% or more of daily caloric consumption in protein appears, however, to stress bodies that are already fine tuned for optimal health by virtue of being youthful and in the prime of life.

It’s actually pretty easy to eat over 20% of daily caloric consumption in protein, especially with protein rich animal-based proteins. 20% of daily caloric consumption in protein for the average diet that would be over 100 grams of protein per day. 100 grams of protein in a day would look like this: 2 eggs (25g) for breakfast, 4 ounces of chicken breast for lunch (25g), and a 6 ounce steak (50g) for dinner. Even if we switched out the steak for 4 ounces of turkey or fish for dinner, we would still be at 95 grams of protein for the day. Throw in a cup of ice cream (because we were so good) to add another 5 grams would again make an even 100 grams for a high protein day.

According to these researchers a high protein diet, for most of us, appears to be too much of a good thing. So, what can we do about it? The simplest thing would be to eat less meat. According to the American Heart Association, nuts, greens, and beans and many other plant-based based protein sources can adequately fill our daily protein needs and, according to Valter Longo, plant-based protein actually appears to be healthier than meat-based protein. When controlling for the effect of plant-based protein, he found there was no change in the association between plant-based protein intake and mortality, which indicated to him “that high levels of animal proteins promote mortality.” Valter goes on to conclude that “a diet in which plant-based nutrients represent the majority of the food intake is likely to maximize health benefits in all age groups.”

So while most of us aren’t ready to chuck our ground chuck to pursue a vegan diet, it may be worth our time to pay attention to the latest discoveries in nutrition research. It’s also worth mentioning that the presented researchers are part of the same broad intellectual query started in the 1940s when it was discovered that by eating a minimal amount of calories per day, lab animals lived longer. Recent refinements to the theory have pointed to protein restriction as the life extending factor, not calorie or even carbohydrate restriction. Indeed, they agree more years will probably be granted to those rebellious folks who eschew high protein, low carbohydrate diets for low protein, high carbohydrate options, at least until they’re 65 and older.

References

• Bruce et al., High carbohydrate-low protein consumption maximizes Drosophila lifespan, Exp Gerontol. 2013 Oct;48(10):1129-35
• Solon-Biet et al., The ratio of macronutrients, not caloric intake, dictates cardiometabolic health, aging, and longevity in ad libitum-fed mice, Cell Metab. 2014 Mar 4;19(3):418-30
• Levine et al., Low protein intake is associated with a major reduction in IGF-1, cancer, and overall mortality in the 65 and younger but not older population, Cell Metab. 2014 Mar 4;19(3):407-17
• Lee et al., Lifespan and reproduction in Drosophila: New insights from nutritional geometry, Proc Natl Acad Sci U S A. 2008 Feb 19;105(7):2498-503
• CDC, Nutrition for Everyone: Proteins
• American Heart Association, Vegeterian diets,

While having dinner one night, cancer researchers Michael Lisanti and Federica Sotgia asked their eight-year-old daughter Camilla how she would treat patients with cancer. Her answer, in an impatient attempt to move to a more interesting conversation topic, was to take on the disease with antibiotics. As a youngster who had experienced the typical sore throats that come with childhood, this was a logical suggestion. Antibiotics target parasites and bacterial infections, but Camilla was on to something when she innocently stereotyped cancer as an infectious disease.

Cancer research trends have been moving toward the study of stem cells. These are a small number of cells from each tissue in the body that generate further cell division and differentiation, providing replacements for adult cells that are short lived. Cancers possess their own stem cells that facilitate the production of bulk cells present in tumors.

Despite the research trends, drug companies are lagging behind. According to Lisanti, most drug companies manufacture pharmaceuticals that target bulk cancer cells, not their stem cells. “They’re digging in the wrong hole,” he asserts. The relapse of tumor growth after remission in many patients provides evidence for this theory. Cancer stem cells are more resistant to traditional radiation and chemotherapy treatments, though scientists don’t completely understand why. Radiation and chemotherapy may initially prevail, but the resilient stem cells fight back vehemently, producing more aggressive cancer lines.

Cancer stem cells and Camilla’s provocative response inspired Lisanti and his research team at the University of Manchester to completely rethink cancer therapy. They decided to approach cancer treatment through the perspective of commonalities between cancer stem cells rather than differences. “This goes against what people in the field were saying,” said Dr. Lisanti. “[Many believed] each cancer needs its own biomarkers and genetic mutations.” While there is merit to understanding the integral details of each cancer type, it can prove laborious and extremely costly to develop such target specific treatments.

Mitochondria, a component found in all cancer stem cells, were the link Lisanti fixed upon to tie cancer and infectious diseases together. These organelles, or membrane bound bodies, are found inside most cells and perform numerous functions. They are needed to produce chemical energy from nutrients, control cell growth and death, and provide instructions for cell specialization. But for Lisanti, the most interesting aspect of mitochondria is that they very likely evolved from bacteria that were engulfed by primitive cells millions of years ago. Consequently, mitochondria and bacteria are very similar both in structure and function.

One of the known side effects of antibiotics in medical literature is fatigue, the result of their well tolerated toxicity toward mitochondria in healthy cells. This frequently documented symptom supported Lisanti’s hypothesis that harnessing this toxic effect for a therapeutic use against the mitochondria in cancer stem cells could work. Furthermore, the differing mutations among the cancer types would not be an issue since the antibiotics would target an analogous component in all the stem cell varieties.

Lisanti also knew about a group in Italy that had promising results researching the treatment of bacterial associated cancers. Researchers at the San Raffaele Scientific Institute in Italy were successful in treating lymphomas of the eye caused by chlamydial infections using an antibiotic. Patients participating in their clinical trial experienced significant tumor shrinkage and resistance to recurrent cancer growth following the antibiotic therapy.

Lisanti chose an array of cancers to test, growing them in a lab and then harvesting their stem cells. “We tried really hard to make our research not work,” he said. In an effort to build a robust study, he selected twelve different cancer lines from eight tumor types, including those specific to the breast, prostrate, skin, and brain. To test his antibiotic theory, the tried and true antibiotics from each of five classes were used to attempt the suppression of stem cell replication and expansion. The results were significant across the board, showing a decrease in mitochondrial function with treatment from each drug.

However, doxycycline was the study’s clear winner. Doxycycline, a member of a broad spectrum group of antibiotics referred to as the tetracyclines, has enjoyed sustained success for over forty years in treating bacterial and parasitic infections. Although certain types of bacteria have developed resistance against it, doxycycline remains a strong player in the fight against strains that cause acne and many types of respiratory and sexually transmitted diseases. It is this same antibiotic that had been successful treating chlamydial related lymphoma in Italy.

The success of doxycycline in the initial cancer stem cell research provided a strong foundation for further clinical studies. The possible ramifications of its success are striking, both in terms of economics and the lack of side effects common to most cancer drugs. A three week course of doxycycline can cost as little as five dollars, making it accessible to patients around the world. Furthermore, doxycycline is already an FDA approved drug, a factor that could expedite future clinical trials.

Further research is needed to validate the treatment of cancer as an infectious disease, including the potential development of personal resistance to the antibiotic. Despite that concern, this study showed that there may be several viable antibiotic options if resistance to one arises. More extensive testing against a greater range of cancer types is warranted as well. However, the work of Lisanti’s team, thanks to the serendipitous suggestion from an eight-year-old girl, offers a potentially powerful addition to our cancer fighting arsenal.

References

• Interview with Dr. Michael Lisanti, University of Manchester, England
• “Chlamydophila Psittaci Eradication With Doxycycline As First-Line Targeted Therapy for Ocular Adnexae Lymphoma: Final Results of an International Phase II Trial” by A. Ferriri, et al. Journal of Clinical Oncology, August 20, 2012 vol. 30 no. 24 2988-2994
• “Antibiotics that target mitochondria effectively eradicate cancer stem cells, across multiple tumor types: Treating cancer like an infectious disease.” by Lamb, R., Ozsvari, B., Lisanti, C., Tanowitz, H., Howell, A., Martinez-Outschoorn, U., Sotgia, F., & Lisanti, M. (2015). Oncotarget, 6(7), 4569-4584

Releasing so much methane all at once jump-starts what has been, so far, a fairly slow and steady climate warming process. What makes this scenario particularly worrisome is that methane is a much more potent greenhouse gas than CO₂ – between 20 and 100 times more effective at warming the planet’s surface depending on whose estimates you believe. The net result of this nightmare scenario, also known as the clathrate gun hypothesis, is a rapid acceleration in global warming along with all the consequent bad effects for humankind.

Methane hydrates are found in subsea deposits in many parts of the world’s oceans including shallower areas of the Arctic Ocean as well as onshore in permafrost, but until recently this ‘arctic methane timebomb’ hypothesis that there could exist a tipping point at which gradual warming might suddenly trigger a mass release was just that, still a hypothesis.

But four years ago, a joint US-Russian expedition observed fountains of methane bubbles rising from the seafloor of the East Siberian Arctic Shelf. Last summer, a Swedish expedition found a whole lot more, with plumes up to a kilometre wide and methane concentrations 100 times the background concentration. More recently they have been observed offshore Svalbard in the Norwegian arctic too.

Methane bubbling to the surface in a lake in the Yamal permafrost. Image credit: Siberian Times and Vasily Bogoyavlensky

If that wasn’t enough, two years ago mysterious craters began appearing in the permafrost of the Yamal Peninsula, also in the Russian arctic. Just one or two at first, but last month twenty more were found in a survey of satellite images. The most credible explanation so far is that they are sinkholes that have filled with methane released from the surrounding permafrost, until the pressure build-up makes them explode outwards.

So is the arctic methane timebomb prophecy becoming a reality? Are we on the verge of climate calamity?

Unlike the near-universal agreement that humanmade CO₂ is responsible for global warming, scientific opinion is sharply divided over whether catastrophic release of methane from the arctic is likely or even possible.

Carolyn Ruppel of the USGS Gas Hydrates Project concluded a recent Nature review article on the subject by saying ‘catastrophic, widespread dissociation of methane gas hydrates will not be triggered by continued climate warming at contemporary rates (0.2^oC per decade; IPCC 2007) over timescales of a few hundred years. Most of Earth’s gas hydrates occur at low saturations and in sediments at such great depths below the seafloor or onshore permafrost that they will barely be affected by warming over even 103 years’, and made it even clearer in a follow-up TV interview by saying bluntly that the clathrate gun hypothesis was ‘nearly impossible’.

One of the Yamal Craters. Image credit: Siberian Times and Vasily Bogoyavlensky.

Others have supported this view by pointing out that if hydrates are so unstable one would expect to find high concentrations of methane during past global warm periods in records of past atmospheric composition, such as polar ice cores – yet no such correlation has been consistently observed.

On the other hand, computer simulations of warming seafloor gas hydrates have demonstrated that they can undergo rapid dissociation over timescales as short as decades, and the recent observations from the East Siberian Arctic unquestionably do show that significantly increased amounts of methane are being released as the arctic warms, although it is estimated to be still only 0.5 million tonnes per year.

Such gradual releases of methane from melting ice both on-land and subsea are to be expected as the climate warms, however that’s missing the point. The doomsday scenarios require not a gradual release but a rapid, catastrophic one – and as much as the climate pessimists may wish for it, there isn’t much hard evidence for such a scenario … yet.

There is no question that the arctic will play a key role in the future climate change of the planet, in fact it’s already happening thanks to the rapidly shrinking summer pack ice cover and the resulting change in albedo, leading to a warming of the Arctic Ocean and hence changing weather patterns. The resulting ‘wavier’ jet stream is thought to be the cause of the recent spate of more severe winter weather events in North America. But the jury is still out on whether runaway methane release is likely to add to the problem too.

The fundamental concept used in solar sailing is also not new, as Maxwell had shown us in the 1860’s that light exerts pressure. The light particles (photons) can therefore move the sail by transferring momentum to it, as long as the sails have a reflective surface for easy illumination. Since there is no shortage of photons from sunlight in space, a constant pressure is created on the sail that provides a constant acceleration to the spacecraft.

The force experienced by a conventional rocket is greater than a spacecraft propelled by solar sails. However, the constant acceleration produced on the solar-sail spacecraft increases its velocity over time. For this reason, it is imagined as the fabled tortoise in the space race.

Nonetheless, it must be noted that while the deployment of a solar sail should be possible in space, it is challenging to release a purely sunlight driven kite-like spacecraft directly from a low Earth orbit. A second rocket would typically be necessary to launch the sail.

Solar sails were considered by NASA in the 1970s. However, it was technologically too risky at the time. Later, NASA revisited solar sails with its partner, Able Engineering, and successfully demonstrated the deployment of solar sails in a vacuum environment during their testing period from April to May 2004. The same year, NASA and L’Garde, Inc., deployed their solar sail system successfully, and Japanese Aerospace Exploration Agency (JAXA) launched two large solar sails and deployed them through space.

The Planetary Society planned to launch its solar sail, Cosmos 1, in 2005. If the mission had been successful, it would have been the first of its kind to put a solar sail into orbit. Unfortunately, the launch vehicle did not reach its orbit due to a rocket failure.

JAXA launched IKAROS (Interplanetary Kite-craft Accelerated by Radiation Of the Sun) in 2010, the world’s first interplanetary spacecraft powered primarily by solar sails. IKAROS completed its mission six months after its launch in December 2010 when it passed by Venus; it was reported to be still alive in 2012.

A giant solar sail called the Sunjammer was due to be launched in January 2015 but it was cancelled last year. However, solar sails have been making the news again lately because the solar-sail spacecraft, LightSail-1 (formerly known as NanoSail-D), developed by the Planetary Society, will be tested in May 2015; a second LightSail spacecraft is expected to launch in 2016. These solar sail projects, in addition to the much-awaited James Webb Space Telescope of 2018, should make the next few years quite exciting.

Endothelial cells live on the inner surface of your blood vessels where they create a gas called nitric oxide. This gas is basically a chemical command that says, “Relax!” to the smooth muscles surrounding your blood vessels (all your blood vessels have tiny muscles embedded in their walls). When the smooth muscles receive the command to relax they, like a fist opening, allow the blood vessels to expand wider, letting more blood flow through. More blood means more oxygen for your muscles, especially when you’re doing things like climbing stairs, playing tennis, or dancing the night away. The key to all these vigorous activities is generous amounts of nitric oxide.

To make nitric oxide, your endothelial cells need arginine, a protein manufactured within your body and found in most common foods. Whether eaten or manufactured, arginine enters your endothelial cells, where it is converted into nitric oxide. But the story does not end here. There is an impostor lurking in your blood called asymmetric dimethylarginine, or ADMA for short.

ADMA is a naturally occurring waste product that can cause problems. How? From your endothelial cells’ point of view, ADMA looks like arginine. In fact, ADMA not only looks like arginine, it’s actually more attractive to your endothelial cells than arginine itself! As a consequence, arginine is often supplanted by ADMA, which may enter the endothelial cell, but much like you cannot squeeze blood from a turnip, no nitric oxide can be made from ADMA. If this happens too often, you simply won’t have enough nitric oxide to command the blood vessels to relax, which means not enough oxygen for your muscles and definitely no energy for dancing.

To prevent this from happening, your body creates a protective molecule called Dimethylargininase, DDAH for short, which destroys ADMA. ADMA’s numbers are kept low when you have enough DDAH. This system generally works well but it has a weakness: DDAH is vulnerable to the attacks of free radicals, which are like tiny magnets in your body that float along until they bump against other molecules and viciously tear them apart. Fortunately, you have molecules designed to be safely torn apart called anti-oxidants. These are plentiful when you eat fresh fruits and vegetables, like blueberries and broccoli.

Some familiar advice might go like this: eat plenty of fruits and vegetables. This gives your free radicals lots of anti-oxidants to tear apart, instead of tearing apart your DDAH. By saving your DDAH, ADMA is culled. With ADMA kept under control, adequate amounts of arginine reaches your endothelial cells where it’s transformed into nitric oxide. Nitric oxide, in turn, commands the smooth muscles around your blood vessels to relax, allowing more blood flow. With increased blood flow more oxygen is delivered to your muscles and when you have well oxygenated muscles, you have the energy to dance all night long.

This article appeared in the Spring 2014 issue of Current Exchange Magazine.

Most labs have equipment that was hacked together by clever souls. Those range from custom-made PC cards to the plate colony replicators, made from just few pieces of common-use items. Whenever I come across custom-built equipment, my mind fills with excitement when I think of all the creativity that went into it, a creativity that should be commonplace in the scientific environment. This goes against all current trends, however, since most of molecular biology is reduced to kit-based science, which makes it more difficult—especially for scientists in training—to understand the underlying biology. Let’s not forget that the greatest discoveries in molecular biology happened by hacking something together to achieve something new; just think of the proverbial Hershey blender.

What stemmed from these thoughts was the realization that when starting up the lab, one need not necessarily buy all the equipment; rather, labs could simply print what they need. It is no longer surprising to life science researchers how expensive enzymes and other molecular biology products are. A price of $200 per 100µL of enzyme lies on the cheap side of the spectrum. What is surprising is how this pricing also extends to mundane lab necessities such as Western blot boxes, tube racks and pipette holders.

While some high prices are understandable due to the limited production run, other price increases seem to come straight from the moon. Consider the magnetic racks used for magnetic bead separation. Those are simply Eppendorf tube racks with permanent magnets fitted to them. Not exactly high tech, but this item carries the price of $500 if not more, and all for a product that is dwarfed in complexity by many a child’s toys. Although you could use a magnet if tight on budget, a more ergonomic solution is preferred for everyday work. Hence, the racks are here to stay and become a highly coveted item in laboratories with few resources.

This is where the 3D printer solution comes into play to print your own equipment. But how do you justify its purchase? Simple: Print five items and you’ve already recuperated the cost of the printer. Of course, you must still order magnets (eight pieces, $1 each) and do some simple assembly but it’s worth the trouble.

A quick search in the standard repository of printable things produces examples of many useful objects, like electrophoretic boxes (just add platinum wire), gel combs, magnetic racks, pipette hangers and holders, ice box solutions, etc. You can even find parts for a functional tabletop spindown microcentrifuge! Although additional parts and assembly are required, you are again getting a $500 item for much less.

With examples like this, an idea came to mind. What if we could put together several useful 3D designs to make a ‘lab seed’ for starting scientists? New faculty who are just getting started could simply manufacture what they need.

This is a great idea, but is it realistic? From our experience, we were pleasantly surprised by the performance of the printer we purchased. We would stand by the printer, watching in awe as the object emerged as per the specification of our design. What came later, however, was an even greater surprise: the printed object’s hardness combined with its low weight. This is due to the internal structure produced by the printer, which occupies only 10% to 15% of the internal volume (and resembles a honeycomb). Interestingly, the level of the infill can be regulated to produce objects which are more solid and durable.

As for the object’s finish, while it is potentially watertight, the surface has a rough appearance as it is composed of plastic extruded from the nozzle and the machine has no way of smoothing it out. This can be rectified by rubbing some acetone or sand paper across the surface. The plastic filament is relatively cheap, with 2 lb spools priced at $50, and there is a selection of colors and properties to choose from. It is possible to print transparent or flexible objects, or even dissolvable ones for use in particularly difficult models that require support. The possibilities are endless and the modeling software can be surprisingly easy to use nowadays, with Google Sketchup being the leading example.

We are still far from push-the-button-and-forget consumer model. Although the print process is automatic, you still need to process the design file even if you downloaded it. This process translates the 3D model into the series of commands for the printer. Next you need to transfer the file to the printer’s SD card, level the working area and start the print. Additional calibration and filament maintenance is sometimes required, so some practice is needed to run things smoothly. There are additional problems that may manifest themselves during your printing adventures, such as the clogging of the printing head, unexpected power losses which stop your print, uneven shrinking of the plastic or sagging of overhanging parts. About half the time, we got exactly what we expected, while most of the problems were addressed by revising the design or experimental conditions. Of course, creating your own design requires more work.

In summary, the time for obtaining a 3D printer for your lab is right around the corner. It can justify its cost in a stunningly short time and with a relatively small investment of curiosity and some persistence.