Machine Keeps Human Liver Alive And Functioning Outside The Body For 24 Hours

This could double the amount of livers available for transplant and save thousands of lives. Livers for everyone! 

A new machine can keep human livers warm and functioning outside the body for 24 hours before successfully transplanting them, a team of Oxford scientists announced last week. The breakthrough could double the number of livers available for transplant.
Livers are normally kept on ice to slow down their metabolism, a risky process that only buys doctors about 14 hours of time before they need to be transplanted. More than 2,000 livers are tossed every year because of oxygen deprivation or damage endured in the cold preservation process, according to the CEO of OrganOx, the company created around the new device. In the U.S. and Europe, there are about 30,000 patients awaiting new livers, many of whom will die before they can get one.

Staying Alive:  Oxford University

The machine, developed by biomedical engineering professor Constantin Coussios and Peter Friend of the Oxford Transplant Centre, keeps the liver alive at normal body temperature through perfusion, or supplying it with oxygenated red blood cells. While connected to the device, the liver regains its normal color and produces bile just like it would in the human body. The team has been working on the technology since 1994.
Two successful transplants at King's College Hospital in London last month indicate the device could become the go-to method for liver transplants, increasing the amount of time livers could be preserved for transport. The livers were only kept alive for 10 hours in those transplants, but the researchers say their other experiments have shown the machine to work for periods up to 24 hours.

Living Liver:  Oxford University

Having a little wiggle room in the timeframe could allow doctors to assess how well the organ is working and maximize the likelihood of a successful transplant.
Coussios and Friend plan to run a pilot with 20 patients, and pending success, have the machine on the market by 2014.

The Fastest DNA Sequencer

DNA sequencing has revolutionized medicine and biomedical research. For example, DNA analysis can tell doctors which drug might work best against a particular cancer. But current technology usually sequences only short stretches of DNA and can take hours or days. To sequence anything longer than a few hundred base pairs, scientists mince up thousands of copies of the target DNA, sequence all the fragments, and use software to painstakingly reconstruct the order of the DNA bases by matching overlap within fragments. A new approach, called nanopore sequencing, can handle long strands of DNA at once, eliminating the need for overlap analysis. As a result, nanopore sequencers could be cheaper, faster, and more compact than other DNA sequencers. They can also accurately sequence stretches with many repeating base pairs. The MinION from Oxford Nanopore Technologies connects to a USB port. Soon, anyone with $1,000 and a computer will be able to sequence DNA.

1) Drop the DNA sample on a chip.
Researchers place pretreated samples—blood from a patient or purified DNA, for example—into a small port. Within the device is a silicon chip with many thin membranes studded with tiny pores.

2) Unzip the DNA.
An enzyme shuttles the DNA to the membrane’s nanopore. It then unzips the twin strands of DNA and feeds one end into the pore. The pore is a set of proteins arranged in a ring and derived from bacteria. The inner diameter of the pore is a couple of nanometers wide: 100,000 times thinner than a human hair.

3) Block the ion current.
Electrodes send an ionic current, a flow of ions, through the open nanopore. As a group of a few DNA bases—the As, Ts, Cs, and Gs—threads through the neck of the pore, it blocks the ions and interrupts the current. A sensor records the electrical disturbance.

4) Determine the sequence.
Software in an attached computer analyzes the electrical signal recorded for every group of bases. Because each combination of bases blocks the current in a distinctive fashion, the software can deduce the identity and sequence of the individual bases in the group. As the DNA strand feeds through the pore, the software stitches together the sequence of bases on the entire strand.

5) Check for errors.
The device can determine the sequence of a single strand of DNA, but for greater precision, it can also read the complementary strand. Once the first strand of the DNA ratchets through the pore, a small stretch of DNA called a hairpin structure acts as a tether to draw the matching half into the pore as well.

STATS

Price: Less than $1,000
DNA Read Length: 70,000 base pairs
Human Genome Size: 3 billion base pairs

9 Reasons To Avoid Sugar As If Your Life Depended On It

The harmful effects of sugar go way beyond empty calories.
Added sugar is so unhealthy that it is probably the single worst ingredient in the modern diet.
Here are the top 9 reasons to avoid sugar as if your life depended on it (it does).

1. Added Sugar Supplies a Large Amount of Fructose

The reason added sugar (and its evil twin… High Fructose Corn Syrup) is bad for you, is that it supplies a very large amount of fructose.
Sugar (and HFCS) are half glucose, half fructose. Glucose is essential and can be metabolized by pretty much every cell in the body. If we don’t get it from the diet, our bodies make it from proteins and fat.
Fructose, however, is not essential to our functioning in any way.
The only organ that can metabolize fructose is the liver, because only the liver has a transporter for it (1).
When large amounts of fructose enter the liver and it is already full of glycogen, most of the fructose gets turned into fat (2).
This process is probably one of the leading causes of the epidemics of many chronic, Western diseases.
I’d like to point out that this does NOT apply to fruit, which are a real food with vitamins, minerals, fiber, lots of water and are very difficult to overeat on.
Bottom Line: The only organ that can metabolize fructose is the liver. When we eat a lot of fructose, many things in the body start to go wrong.

2. Sugar Doesn’t Contain Any Vitamins or Minerals (Empty Calories)

Sugar IS empty calories. No doubt about that.
Most high-sugar foods like pastries, sodas and candy bars contain very little essential nutrients.
People who eat them instead of other more nutritious foods will probably become deficient in many important nutrients.
Bottom Line: Most products with added sugars in them contain very little nutrients and can therefore be classified as “empty” calories.

3. Sugar Causes Deposition of Fat in The Liver

When we eat fructose, it goes to the liver.
If liver glycogen is low, such as after a run, the fructose will be used to replenish it (3).
However, most people aren’t consuming fructose after a long workout and their livers are already full of glycogen.
When this happens, the liver turns the fructose into fat (2).
Some of the fat gets shipped out, but part of it remains in the liver. The fat can build up over time and ultimately lead to Non-Alcoholic Fatty Liver Disease (4, 5, 6).
Bottom Line: Eating a lot of added sugar (fructose) can cause deposition of fat in the liver and lead to Non-Alcoholic Fatty Liver Disease.

4. Sugar Harms Your Cholesterol and Triglycerides

Most of the fat generated in the liver gets shipped out as Very Low Density Lipoprotein (VLDL) particles.
These particles are rich in triglycerides and cholesterol.
In a controlled study, people were assigned to drink 25% of calories as either a glucose-sweetened drink or a fructose-sweetened drink for 10 weeks (7).
The fructose group had:
Increases in blood triglycerides.
Increases in small, dense LDL and oxidized LDL (very, very bad).
Higher fasting glucose and insulin.
Decreased insulin sensitivity.
Increased fat in the abdominal cavity (visceral fat).
Basically, 25% of calories as fructose significantly harmed blood lipids and caused features characteristic of the metabolic syndrome, which is a stepping stone towards obesity, heart disease, diabetes and a (short) lifetime of poor health. 
Bottom Line: Consuming a large part of calories as fructose can lead to serious adverse effects on blood markers in as little as 10 weeks.

5. Sugar Causes Insulin Resistance

The main function of insulin is to drive glucose from the bloodstream into cells.
But when we eat a Western diet, the cells tend to become resistant to the effects of insulin.
When this happens, the pancreas start secreting even more insulin to remove the glucose from the bloodstream, because elevated blood glucose is toxic.
This is how insulin resistance leads to elevated insulin levels in the blood.
But insulin also has another important function… it tells the fat cells to pick up fat from the bloodstream and to hold on to the fat that they already carry.
This is how insulin causes obesity.
When the body becomes even more resistant to insulin, the beta cells in the pancreas eventually become damaged and lose the ability to produce sufficient insulin. This is how you get type II diabetes, which now afflicts about 300 million people worldwide.
Excess fructose is a known cause of insulin resistance and elevated insulin in the blood (8, 9, 10).
Bottom Line: Excess fructose consumption can lead to insulin resistance, a stepping stone towards obesity and diabetes.

6. Sugar Raises Your Risk of Western Diseases

Excess sugar consumption has been associated with many Western diseases.
If anything, sugar is the single largest contributing factor to the poor health of affluent nations.
Every time sugar (and refined flour and vegetable oils) enter a population’s diet, these people become sick.
Sugar has been associated with:
Obesity. Sugar causes weight gain via various mechanisms, including elevated insulin and leptin resistance (11, 12).
Diabetes. Sugar is probably a leading cause of diabetes (13, 14, 15).
Heart disease. Sugar raises the bad cholesterol, triglycerides and causes various other issues that can ultimately lead to heart disease (16, 17).
Bottom Line: Excess sugar consumption has been associated with many serious diseases, including obesity, type II diabetes and cardiovascular disease.

7. Sugar Doesn’t Cause Proper Satiety

n area in the brain called the Hypothalamus is supposed to regulate our food intake.
In a study published in 2013, two groups drank either a glucose-sweetened drink or a fructose-sweetened drink (18).
The glucose drinkers had decreased blood flow in the hypothalamus and felt satiated, while the fructose drinkers had increased blood flow in this area of the brain.
The fructose drinkers felt less satisfied and were still hungry.
Another study revealed that fructose didn’t reduce levels of the hunger hormone ghrelin like glucose. The more ghrelin, the hungrier you are (19).
Bottom Line: Studies comparing fructose and glucose show that fructose does not induce satiety like glucose, which will contribute to a higher calorie intake.

8. Sugar is Addictive

When we eat sugar, dopamine is released in the brain, giving us a feeling of pleasure.
This is actually how drugs of abuse like cocaine function (20).
Our brain is hardwired to seek out activities that release dopamine. Activities that release an enormous amount of it are especially desirable.
In certain individuals with a certain predisposition to addiction, this causes reward-seeking behavior typical of addiction to abusive drugs.
Studies in rats demonstrate that they can in fact become physically addicted to sugar (21).
This is harder to prove in humans, but many people consume sugar and other junk foods in a pattern that is typical for addictive, abusive compounds.
Bottom Line: Sugar, due to its powerful effects on the reward system in the brain, can lead to classic signs of addiction.

9. Sugar Causes Resistance to a Hormone Called Leptin

Leptin is a hormone that is secreted by our fat cells. The more fat we have, the more leptin is secreted.
This is supposed to function as a signal to tell the brain that we’re full and need to stop eating. It is also supposed to raise our energy expenditure.
Obese individuals actually have high levels of leptin, but the problem is that the leptin isn’t working.This is called leptin resistance and is a major reason why people eat more calories than they burn and become obese.

Scientists map 3-D structure of telomerase enzyme – key actor in cancer, aging

Like finally seeing all the gears of a watch and how they work together, researchers from UCLA and UC Berkeley have, for the first time ever, solved the puzzle of how the various components of an entire telomerase enzyme complex fit together and function in a three-dimensional structure.



The creation of the first complete visual map of the telomerase enzyme – which is known to play a significant role in aging and most cancers – represents a breakthrough that could open up a host of new approaches to fighting disease, the researchers said.

"Everyone in the field wants to know what telomerase looks like, and there it was. I was so excited, I could hardly breathe," said Juli Feigon, a UCLA professor of chemistry and biochemistry and a senior author of the study. "We were the first to see it."
The scientists report the positions of each component of the enzyme relative to one another and the complete organisation of the enzyme's active site. In addition, they demonstrate how the different components contribute to the enzyme's activity, uniquely correlating structure with biochemical function. Their research is published in Nature.
"We combined every single possible method we could get our hands on to solve this structure and used cutting-edge technological advances," said co-first author Jiansen Jiang, a researcher who works with Feigon. "This breakthrough would not have been possible five years ago."

"We really had to figure out how everything fit together, like a puzzle," said co-first author Edward Miracco, a National Institutes of Health postdoctoral fellow in Feigon's laboratory. "When we started fitting in the high-resolution structures to the blob that emerged from electron microscopy, we realized that everything was fitting in and made sense with decades of past biochemistry research. The project just blossomed, and the blob became a masterpiece."

The telomerase enzyme is a mixture of components that unite inside our cells to maintain the protective regions at the ends of our chromosomes, which are called telomeres. Telomeres act like the plastic tips at the end of shoelaces, safeguarding important genetic information. But each time a cell divides, these telomeres shorten, like the slow-burning fuse of a time bomb. Eventually, the telomeres erode to a point that is no longer tolerable for cells, triggering the cell death that is a normal part of the aging process.

While most cells have relatively low levels of telomerase, 80 percent to 90 percent of cancer cells have abnormally high telomerase activity. This prevents telomeres from shortening and extends the life of these tumorigenic cells — a significant contributor to cancer progression.

The new discovery creates tremendous potential for pharmaceutical development that takes into account the way a drug and target molecule might interact, given the shape and chemistry of each component. Until now, designing a cancer-fighting drug that targeted telomerase was much like shooting an arrow to hit a bulls-eye while wearing a blindfold. With this complete visual map, the researchers are starting to remove that blindfold.
"Inhibiting telomerase won't hurt most healthy cells but is predicted to slow down the progression of a broad range of cancers," said Miracco. "Our structure can be used to guide targeted drug development to inhibit telomerase, and the model system we used may also be useful to screen candidate drugs for cancer therapy."

The researchers solved the structure of telomerase in Tetrahymena thermophila, the single-celled eukaryotic organism in which scientists first identified telomerase and telomeres, leading to the 2009 Nobel Prize in medicine or physiology. Research on Tetrahymena telomerase in the lab of co-senior author Kathleen Collins, a professor of molecular and cell biology at UC Berkeley, laid the genetic and biochemical groundwork for the structure to be solved.

An illustration of how telomerase elongates telomere ends progressively. Credit: Uzbas, F

"The success of this project was absolutely dependent on the collaboration among our research groups," said Feigon.

"At every step of this project, there were difficulties," she added. "We had so many technical hurdles to overcome, both in the electron microscopy and the biochemistry. Pretty much every problem we could have, we had – and yet at each stage these hurdles were overcome in an innovative way."

One of the biggest surprises, the researchers said, was the role of the protein p50, which acts as a hinge in Tetrahymena telomerase to allow dynamic movement within the complex; p50 was found to be an essential player in the enzyme's activity and in the recruitment of other proteins to join the complex.

"The beauty of this structure is that it opens up a whole new world of questions for us to answer," Feigon said. "The exact mechanism of how this complex interacts with the telomere is an active area of future research."