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Comment by Dr. Krishna Kumari Challa on February 11, 2015 at 8:29am

How do medical journalists treat cancer-related issues?
http://ecancer.org/journal/9/full/502-how-do-medical-journalists-tr...
Where Do Medical Journalists Find Their Sources? Direct contact with patients and doctors is favored over press releases from pharmaceutical companies, a survey of journalists reveals.
Researchers at the University of Tokyo sent self-administered questionnaires to 364 medical journalists, who described their experiences in selecting stories, choosing angles, and performing research when creating cancer-centerd news pieces. The journalists reported that they did not find pharmaceutical press releases to be helpful, preferring direct contact with physicians as their most reliable and prized sources of information. Medical journalists also report using social media and personal connections to support their research.
All journalists reported difficulties in producing accurate and interesting cancer news stories. The most commonly reported concerns were the quality of source information, difficulty in understanding technical information and a shortage of background knowledge.
As medical knowledge advances rapidly, journalists may have increasing difficulty covering cancer-related issues .
This highlights the need for responsible healthcare reporting, the team suggests, which can be attained through journalistic communication with researchers and physicians, and the willingness of healthcare professionals to explain their work carefully and clearly.
Asian Scientist Magazine : http://www.asianscientist.com/2015/02/in-the-lab/medical-journalist...

Comment by Dr. Krishna Kumari Challa on February 11, 2015 at 8:22am

Researchers have succeeded in inducing human embryonic stem cells to self-organize into a three-dimensional structure similar to the cerebellum, providing tantalizing clues in the quest to recreate neural structures in the laboratory. Their results have been published in Cell Reports.

Full details here:

 Muguruma et al. (2015) Self-Organization of Polarized Cerebellar Tissue in 3D Culture of Human Pluripotent Stem Cells.

http://linkinghub.elsevier.com/retrieve/articleSelectPrefsTemp?Redi...

Comment by Dr. Krishna Kumari Challa on February 11, 2015 at 8:17am

So you think as your original age is just 31, you are likely to live another 40-50 years without any doubt. Is your thinking right ? Not necessarily according to new research.
"DNA methylation age of blood predicts all-cause mortality in later life"
We count our age in calendar years, but our bodies may not be counting the same way. Using a biological clock that compares the aging of a person’s DNA to their actual age, University of Queensland researchers have found some clear signals to life expectancy. Professor Naomi Wray, from UQ’s Queensland Brain Institute (QBI), said the study found that people with a “biological” or DNA age greater than their true age were more likely to die younger, compared to those whose biological and true age were closely matched. “Last year, it was discovered that from a simple blood sample it is possible to predict a person’s age with a high degree of accuracy,” Wray said. “But it is not totally accurate, and some people’s predicted or ‘biological’ age is higher than their actual age and vice versa.” “Our study showed biological age really does seem to be tracking biological wear-and-tear.” The study, published in Genome Biology, used data from four independent studies that sampled almost 5,000 older people, of whom about 10 percent died in the following 14 years. Each participant’s biological age was measured from a blood sample at the outset. The research showed that those with a higher biological age compared to actual age had an increased risk of death. All four studies found the same pattern, with death linked to accelerated biological changes to DNA. Wray said the study could not look at what caused the DNA to change at an accelerated pace, nor was it an accurate predictor of death for an individual person. “However, it’s an important clue for future research in the study of cellular ageing,” she said. “What we’re seeing could be caused by environmental, lifestyle, genetic predispositions, or a combination of all these factors.” The QBI’s Dr. Allan McRae, who conducted analyses for the study, said biological ageing was measured by following DNA changes caused by a process known as methylation. “Methylation affects whether genes are turned on or off, which has important repercussions for conditions such as disease susceptibility, so it makes sense that the biological clock speeding up has impacts on how we age,” McRae said.
http://genomebiology.com/2015/16/1/25/abstract

Comment by Dr. Krishna Kumari Challa on February 11, 2015 at 8:04am

For Precision, Two Clocks Are Better Than One The optical lattice clocks use lasers to create “egg box” structures that contain single atoms, leading to unprecedented precision.
Cryogenic optical lattice clocks
http://www.nature.com/nphoton/journal/vaop/ncurrent/full/nphoton.20...

Comment by Dr. Krishna Kumari Challa on February 11, 2015 at 6:18am

Efficient solar-to-fuels production from a hybrid microbial–water-splitting catalyst system

A new way to make fuel from sunlight: starve a microbe nearly to death, then feed it carbon dioxide and hydrogen produced with the help of voltage from a solar panel. A newly developed bioreactor feeds microbes with hydrogen from water split by special catalysts connected in a circuit with photovoltaics. Such a batterylike system may beat either purely biological or purely technological systems at turning sunlight into fuels and other useful molecules.
http://www.pnas.org/content/early/2015/02/06/1424872112

Comment by Dr. Krishna Kumari Challa on February 9, 2015 at 7:12am

This sea slug ‘feeds’ on sunlight using photosynthesis

Part flora, part fauna, this pretty green sea slug has gained the ability to photosynthesise by stealing genes from the algae it feeds on.
After decades of searching, scientists have finally found direct evidence to show that the emerald green sea slug (Elysia chlorotica) takes genes from the algae it eats to perform photosynthetic processes, just like a plant. This means it can get all the energy it needs from sunlight, allowing it to survive without food for months.

“There is no way on earth that genes from an alga should work inside an animal cell”. And yet here, they do. They allow the animal to rely on sunshine for its nutrition. So if something happens to their food source, they have a way of not starving to death until they find more algae to eat.

Scientists have known for over 40 years that the emerald green sea slug takes chloroplasts - organelles found in plant and algal cells that facilitate photosynthesis - from the yellow-green algae it eats, called Vaucheria litorea. Referred to as ‘kleptoplasty’, this process allows the chloroplasts to continue photosynthesising in their new sea slug home for up to nine months after transferring from the algae. By photosynthesising, the sea slug produces lipids when the energy from the sunlight is combined with water and carbon dioxide, which gives it all the nourishment it needs, no additional food required.
But exactly how the emerald green sea slug manages to maintain these organelles in working order for so long has proven to be a complex puzzle - one that was not made easier by an experiment completed by researchers at the University of Dusseldorf in Germany in 2013. The team gave their emerald green sea slugs a drug that completely halted any photosynthetic activity in their cells, but the slugs still managed to survive for 55 days, without any food. They ended up a little smaller and paler, so food wouldn’t have gone astray if they were offered it, but it was proof that the organelles they 'stole' from their last algae meal were somehow still working for them.
"In order to photosynthesise, the chloroplasts inside an alga depend on many genes in the alga’s own nucleus and the proteins for which they code. Tearing chloroplasts out of algal cells and asking them to make food inside a slug’s gut is like expecting the bottom half of a blender to puree some carrots sans the blade and glass jar.”

So where are these genes that the chloroplasts depend on? Reported in The Biological Bulletin, fluorescent DNA markers were used to track the genes from the algae as they made their way into the genetic material of both juvenile and adult emerald green sea slugs. And for the first time, the research team watched as these genes produced an enzyme that’s critical to the proper photosynthetic function of the chloroplasts.

“This paper confirms that one of several algal genes needed to repair damage to chloroplasts, and keep them functioning, is present on the slug chromosome. The gene is incorporated into the slug chromosome and transmitted to the next generation of slugs.”

So while the young emerald green sea slugs still need to feed on the algae to get their supply of chloroplasts, the genes they need to turn these chloroplasts in to little photosynthetic machines have already been passed down to them from their parents.

"Importantly, this is one of the only known examples of functional gene transfer from one multicellular species to another, which is the goal of gene therapy to correct genetically based diseases in humans.
Sources: The Marine Biological Laboratory Blog, Scientific American, Smithsonian.com

Comment by Dr. Krishna Kumari Challa on February 9, 2015 at 7:03am

Comment by Dr. Krishna Kumari Challa on February 9, 2015 at 6:48am

We are close to eradicating the second disease ever from the planet, the first one is small pox, now we have our sights set on Guinea worm disease.

There are only 126 cases of Guinea worm left in the world before the parasite is gone from humans forever. It is caused by the Guinea worm parasite, Dracunculiasis, and just happens to be one of the most horrible conditions. The Guinea worm infects people who drink water contaminated with its larvae, and it now only exists in four countries in Africa. But that wasn't always the case. In 1986, there were 3.5 million cases of infection reported across Africa and Asia.
A war was declared on the parasite by Carter Centre Foundation - and 30 years later, they are almost won. Thanks to their program, which uses filter technology and education to help disrupt the life cycle of the Guinea worm, the center has announced that there are now only 126 cases left of the parasite.
The life cycle of the Guinea worm is pretty terrifying in itself - once it's infected a host, the larvae develops into a pale worm that can stretch up to one metre long . This growth period lasts for around 12 months, during which time the host might not even know they're infected. And then a painful blister will suddenly appear somewhere on the host's body - usually the foot or another sensitive region. That's when the worst part begins - the worm starts to emerge out of its host's skin over an agonising 30-day period. In an attempt to ease this pain, the infected human often lays down in water to try to wash the worm out of their body or sooth the wounds - but this actually allows the worm to lay its eggs and start the whole cycle again.
The Carter Centre realised that although the disease was widespread, the fact that it was only caused by one parasite meant that it, effectively, could be stopped. They then worked with communities to explain the parasite's life cycle, and to keep them away from water while their worms exited their bodies.

But most importantly, they developed a simple and cheap straw filter to help eliminate parasites from drinking water. The "pipe filter" as it's called, involves a small piece of steel mesh inside a plastic drinking tube, and it ensures that the water being drunk is free of the tiny worms.

Of course, the parasites aren't gone just yet, and it's hard to know just how long it will take before we can say the disease is gone for good.

But it's inspiring to think that, simply by using education and very basic technology, we can stop a devastating disease in its track!

http://www.theatlantic.com/health/archive/2015/01/carter-center-gui...

Comment by Dr. Krishna Kumari Challa on February 9, 2015 at 6:18am

New type of chemical bond discovered : vibrational bond.
This vibrational bond seems to break the law of chemistry that states if you increase the temperature, the rate of reaction will speed up. Back in 1989, a team from the University of British Columbia investigated the reactions of various elements to muonium (Mu) - a strange, hydrogen isotope made up of an antimuon and an electron. They tried chlorine and fluorine with muonium, and as they increased the heat, the reaction time sped up, but when they tried bromine (br), a brownish-red toxic and corrosive liquid, the reaction time sped up as the temperature decreased.

Perhaps, thought one of the team, chemist Donald Flemming, when the bromine and muonium made contact, they formed a transitional structure made up of a lightweight atom flanked by two heavier atoms. And the structure was joined not by van der Waal’s forces - as would usually be expected - but by some kind of temporary ‘vibrational’ bond that had been proposed several years earlier.
"In this scenario, the lightweight muonium atom would move rapidly between two heavy bromine atoms, 'like a Ping Pong ball bouncing between two bowling balls,' Fleming says. The oscillating atom would briefly hold the two bromine atoms together and reduce the overall energy, and therefore speed, of the reaction.”
"Fundamental Change in the Nature of Chemical Bonding by Isotopic Substitution"
http://onlinelibrary.wiley.com/doi/10.1002/anie.201408211/abstract
The research team watched as the light muonium and heavy bromine formed a temporary bond. “The lightest isotopomer, BrMuBr, with Mu the muonium atom, alone exhibits vibrational bonding in accord with its possible observation in a recent experiment on the Mu + Br2 reaction.
Accordingly, BrMuBr is stabilised at the saddle point of the potential energy surface due to a net decrease in vibrational zero point energy that overcompensates the increase in potential energy.”

In other words, the vibration in the bond decreased the total energy of the BrMuBr structure, which means that even when the temperature was increased, there was not enough energy to see an increase in the reaction time.

While the team only witnessed the vibrational bond occurring in a bromine and muonium reaction, they suspect it can also be found in interactions between lightweight and heavy atoms, where van der Waal’s forces are assumed to be at play.

"The work confirms that vibrational bonds - fleeting though they may be - should be added to the list of known chemical bonds

Comment by Dr. Krishna Kumari Challa on February 9, 2015 at 6:01am

Tuna keep their hearts warm in cold depths - how this is done?
It may be a little odd sounding, but tuna are very cold hearted creatures. No, they aren't unnecessarily cruel or stoic in life. Instead, they just can literally have cold hearts, with the organ somehow able to keep functioning even when deep-diving chills it to temperatures that would stop a human heart. Now researcher think they know how the fish is capable of this amazing feat.

Bluefin tuna have increasingly been spotted in East Greenland waters, and scientists are mystified as to what is driving this northward movement.
Bluefin Tuna Mysteriously Move to East Greenland Waters
The Pacific Bluefin tuna, a fish popular among sushi eaters, is verging on the brink of extinction as the global food market places
Sushi Eaters Push Bluefin Tuna Towards Extinction

"Tunas are at a unique place in bony fish evolution" researcher Barbara Block at Stanford University explained in a recent statement. "Their bodies are almost like ours - endothermic (warm blooded/bodied), but their heart is running as all fish at ambient temperatures. How the heart keeps pumping as the fish moves into the colder water is the key to their expanded global range."

As detailed in a new study published in the journal Proceedings of the Royal Society B, Block and her colleagues looked to bluefin tuna to learn more about this fascinating ability. A top predator of the Pacific Ocean, the bluefin are renown for their epic migrations, traveling far in search of prey and diving chillingly deep - up to 1000 meters below the ocean surface.

"When tunas dive down to cold depths their body temperature stays warm but their heart temperature can fall by 15°C within minutes," added Holly Shiels, from the University of Manchester. "The heart is chilled because it receives blood directly from the gills which mirrors water temperature. This clearly imposes stress upon the heart but it keeps beating, despite the temperature change. In most other animals the heart would stop."

Shiels, Block, and Manchester researcher Gina Gali reportedly used electromagnetic tags to monitor bluefins in their lengthy migration from the waters of Japan all the way to the Californian coast. The tags allowed them to measure the depth at which each fish swam on its journey, its internal body temperature at any one point, and the ambient water temperature surrounding it. This data was then reapplied in lab simulations using single tuna heart cells to see how they beat.

The trio found out that rushes of adrenaline during dives helped keep essential calcium circulating in the tunas' hearts, which kept them pumping their chilled blood.

"We were recording the fish swimming down into colder depths only to resurface quickly into the warmer surface waters, a so called 'bounce' dive," said Block. " From work at sea and in the lab we now know the fish hearts slow as they cool and as they resurfaced it sped up. Our findings suggest adrenalin, activated by the stress of diving, plays a key role in maintaining the heart's capacity to supply the body with oxygen."

Now the researchers are wondering if this is a new and unique mechanic among only tuna, or if other species have taken on this adaptation as well.

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