​Droning on forever? Boeing patents UAV that could fly indefinitely, recharge in mid-air — RT News

Still from YouTube video/PatentYogi

As drone technology continues to advance, Boeing has raised the bar even higher. The aerospace giant has received a patent for a UAV that could fly forever – recharging in mid-air via a tether attached to the ground.

The patent – filed in March 2013 and approved by the US Patent and Trademark Office last week – could revolutionize unmanned aerial vehicles (UAVs) as we know them, foregoing the need to refuel or recharge on land.

According to the patent, the electrically-powered drone would have a retractable tether cable that would connect to a power source. When the drone was fully charged, it would automatically fly off to continue its task, and another UAV could then take its place at the charging station.

The drone could be connected to a number of sources, including land- and sea-based power supplies. It could even be connected to moving vehicles, allowing the drone to fly while charging.

The concept could be extremely beneficial for drone delivery services, or for those which need to stay airborne for an extended time due to long-term experiments, monitoring or travel, GeekWire reported. It could also completely do away with landing gear, which can be heavy and burdensome for drones.


Boeing has so far given no indication on whether it actually plans to build the drones.

An increasing number of companies are currently testing drones, indicating that widespread usage could be just around the corner.

As was reported last week, NASA and Verizon are investing in new technology that would use already existing cell phone towers to monitor civilian and commercial drones.

In April, Amazon was granted the authority totest delivery drones in the US. The e-commerce giant hopes to revolutionize delivery services with the technology. That same month, the US Federal Aviation Administration (FAA) approved the testing of UAVs by three insurance giants: AIG, State Farm and USAA.

The FAA has already come under fire for its alleged lack of privacy protections in its initial set of drone regulations. In April, the Electronic Privacy Information Center (EPIC) filed a suit against the agency, asking a federal appeals court to review its decision.

At present, the FAA prohibits commercial drone operators from flying drones beyond their line of sight, and restricts their use to daylight hours. Drones must weight a maximum of 55 pounds, stay below 500 feet in the air, and fly less than 100 miles per hour. A drone operator must also pass an aeronautics test.

Kidney failure impacts survival of sepsis patients

Researchers at Duke Medicine have determined that kidney function plays a critical role in the fate of patients being treated for sepsis, a potentially life-threatening complication of an infection.

In a study published May 20, 2015, in the journal Kidney International, Duke researchers and their colleagues identified physiological changes at the molecular level that might be affected by . The findings could help physicians improve hemodialysis practices, increasing patient survival rates after kidney failure.

Acute kidney injury is a serious and common health complication, occurring in up to 20 percent of all hospitalized and more than 45 percent of patients in a critical-care setting, according to the National Institutes of Health.

“There are a lot of things that we assume to be true about the impact of acute kidney injury on patients,” said lead author Ephraim Tsalik, M.D., Ph.D., assistant professor at Duke University School of Medicine. “This study is the first to comprehensively characterize what is happening at the patient level, potentially as a cause and a consequence of acute kidney injury that we see in the setting of .”

Sepsis, which is defined as systemic inflammation resulting from an infection, often results in an abrupt decrease in the kidney’s ability to effectively filter the blood.

The Community Acquired Pneumonia and Sepsis Outcome Diagnostic (CAPSOD) study, led by Stephen Kingsmore, M.B, D.Sc., of Children’s Mercy Hospitals and Clinic, was initially created as a repository for patients visiting the emergency department with suspected sepsis. The researchers used clinical and molecular information generated in the CAPSOD study to correlate patient-level data with changes in molecular markers in the blood.

They found that was a major determinant of how a patient responded to treatment for sepsis.

“We have over 2,000 patients enrolled in the CAPSOD repository,” Tsalik said. “We are trying to use new tools to ask why is it that some patients show up and get sicker, despite getting all the right treatment, and why some patients show up, get the right treatment, and quickly get better.”

Using an “‘omics-based” approach, the researchers looked at variations in metabolite level, protein production, and gene expression in the blood in 150 patients with critical illness. The study design also allowed the researchers to investigate what impact hemodialysis, a medical treatment for that filters toxins from the blood, was having on a variety of molecular markers.

“Rather than setting out to prove existing hypotheses, this study was designed to identify new questions or associations we were not previously aware of,” Tsalik said. “There were a number of things that we expected to see and did, such as the accumulation of molecules normally cleared by the kidney among patients with .”

Those known molecules are usually filtered out when a patient is receiving hemodialysis; however, the researchers also identified other chemicals and metabolites that were not previously shown to be abnormal in patients on hemodialysis.

“It may be that these newly implicated metabolites are not clinically relevant, but by identifying them, we’ve opened up opportunities for researchers to see if they cause toxicity to the patient,” Tsalik said. “We want to understand how to improve the care of patients with acute and those requiring hemodialysis.”

Engineers Develop Wi-Fi Powered Devices.

Why Is This Important?

Tech News: Engineers Develop Wi-Fi Powered Devices

Because batteries are a drag.

Long Story Short

University of Washington engineers have developed a surveillance camera powered not by batteries or wires, but by regular, ambient Wi-Fi signals. The camera draws enough power from nearby Wi-Fi hotspots to snap a picture every 35 minutes or so.

Long Story

The 20th century marked a huge leap forward in wireless communications – cordless telephones, cell phones and wireless internet access wasn’t far behind. In terms of powering devices, though, we’ve fallen short of Nikola Tesla’s dream of a wirelessly powered world. There have been recent enhancements in wireless charging technology, sure, but anything that relies on electricity still needs to either be wired directly into the power grid, or run on an inefficient battery. The tide may be changing, though, because researchers at the University of Washington have developed small devices – a camera and a temperature sensor – that can run solely on the power provided by common WiFi signals.

The system, called power over Wi-Fi (PoWi-Fi) operates on a relatively simple principle: W-Fi signals are energy just like anything else, only we tend to receive and use them in a particular way. There’s no reason, though, that we couldn’t capture them for the sake of their energy, which happens to come close to the 300 millivolt operating threshold for most small devices.

The only problem is that since Wi-Fi signals are only transmitted when there’s a request for data, the signals aren’t consistent enough to power a device. The engineers fixed that by re-programming a few routers to broadcast “noise” constantly (even when they weren’t transmitting data), using multiple channels to avoid messing with data rates.

Their workaround was a resounding success. The small temperature sensor could operate as far as six meters from the routers without any other power provided. The camera could operate about five meters away from the hotspot (including through walls), and was able to store up enough juice to snap a low-resolution signal every 35 minutes.

There’s some concern that having three routers pushing out constant Wi-Fi signals could interfere with other devices, but so far this remains to be seen. The engineers actually saw an improvement in their internet connections, but they admit they aren’t sure of any effects felt by neighbors trying to use their own Wi-Fi. Regardless, the possibility of a truly cordless future has, at the very least, been proven in concept.

Own The Conversation

Iranian scientists create hybrid heart valve

Two Iranian scientists have successfully created the first hybrid tissue-engineered heart valve with the use of a metal alloy.

An artificial heart valve (file photo)

Hamed Alavi, PhD, and Arash Kheradvar, MD, PhD, from the University of California in Irvine, developed the new valve, which can become a replacement for current valves thanks to its durability, the Mehr news agency reported on Monday.

The findings of their research were published in an article in the latest edition of the Annals of Thoracic Surgery.

Iranian scientist Arash Kheradvar, MD, PhD (L) and Hamed Alavi, PhD

In the current technology used in valve replacement, the patient’s cells are used to create an artificial valve set on a scaffold that will eventually degrade, resulting in the failure of the valve.

The scientists believe by using the new technology, patient’s life quality will be improved as the valve eventually incorporates itself into the patient’s heart structure.

The valve is built on a “non-degradable scaffold that stays within the valve to provide the support it needs without interfering with its normal function,” said Kheradvar.

“The valve we created uses an ultra-flexible scaffold made of an alloy of nickel and titanium (nitinol) that is enclosed within the patient’s own cultured tissue,” he added.

According to the team, initial lab tests on the valve have been completed and the next phase of testing is set to begin.

Miniature Device Could Unlock the Promise of Some Kidney Cancer Drugs .

Ideas abound about how to develop smarter cancer drugs with the help ofnanotechnology, using tiny materials with unusual chemical and physical properties. For renal cell carcinoma (RCC), a common form of kidney cancer, a new nanoparticle could make it possible to deliver therapies directly to the tumor site while preventing their uptake in other organs. The device could also enable new ways to treat chemotherapy-induced kidney failure.

  • MSK researchers have created a new type of nanoparticle.
  • Its size and chemistry differ from many similar materials.
  • When injected into mice, the new particle sticks to the kidneys.
  • Ongoing studies will tell if it can carry drugs to RCC tumors.

Inspired by a surprise discovery, Memorial Sloan Kettering scientists have engineered a tiny particle that could make it possible to deliver drugs directly to the kidneys and minimize their uptake in other organs. The device, called a mesoscale nanoparticle, could help boost the usefulness of some kidney cancer drugs and might also be used in the treatment and diagnosis of other kidney conditions.

Nanoparticles are polymers — large molecules consisting of many small parts — that typically measure between one and 100 nanometers and can be loaded with drugs or imaging agents. (For comparison, an average human cell measures about 50,000 nanometers in diameter.) They hold promise for many medical applications, partly because they are biocompatible — not harmful to living tissue — and have unusual chemical and physical properties.

At MSK and elsewhere, scientists are seeking to develop new nanoparticles capable of ferrying drugs to tumors and making them stay there long enough to be effective. “Targeting tumors specifically has often proved to be challenging,” says chemist and engineer Daniel Heller, who led the study. “For cancers growing in specific sites, such as the kidneys, the next best thing may be a particle that’s capable of seeking out the right organ.”

A Serendipitous Result

The kidney-bound particle is the result of an incidental finding made while studying how the size and chemical properties of some nanomaterials could be modulated to guide their distribution in the body. The goal of the project — a collaboration between Dr. Heller’s group and MSK lung cancer physicians — was to create a nanoparticle capable of targeting cancer drugs to the lung.

Mesoscale nanoparticles imaged by scanning electron microscopy.Mesoscale nanoparticles visualized by scanning electron microscopy. The diameter of an average particle measures about 400 nanometers, which is about 50 times smaller than the width of a human hair.

The investigators produced a number of nanoparticles of different sizes and chemical properties. They then injected these particles into mice and tracked their location using CT scans and other imaging methods.

The results of the initial experiments were mixed. In particular, one of the particles didn’t behave as expected. The researchers could find only low levels of it in the animals’ lungs, and very little in the liver or spleen, where many similar substances tend to gather. “To our surprise, this particle accumulated almost exclusively in a specific structure of the kidney,” says postdoctoral fellowRyan Williams, the study’s first author, “and it stayed there until all of it had degraded.”

The researchers dubbed the particle “mesoscale” or middle-size because it’s bigger than most of its forerunners, with a diameter of about 400 nanometers. It takes up to two months for the mesoscale nanoparticle to fall apart completely, which means it could potentially be used to release a drug very slowly inside the kidneys.

Redeeming Failed Drugs

Located right below the rib cage, the kidneys are two fist-size organs whose main function is to filter waste and excess water out of the blood to make urine. While waste products enter the kidneys through a network of filtering blood vessels called the glomerulus, the researchers found that mesoscale nanoparticles are absorbed — through a poorly understood process — in a different part of the kidney called the proximal tubule.

“This is interesting for several reasons,” Dr. Heller says. “First, the proximal tubule happens to be where renal cell carcinoma [RCC, the most common form of kidney cancer] originates.”

The team is now working to develop a nanoparticle-based technology to deliver chemotherapy or targeted therapies directly to the site of RCC. They hope the method will help reduce side effects of the drugs by keeping them away from other organs.

RCC drugs that haven’t met expectations could potentially be improved with nanotechnology.

“We are currently doing experiments to verify that the particles can be used to effectively deliver a drug to RCC tumors in mice,” Dr. Heller says. The main focus of this work, he adds, will be on kidney cancer drugs that have failed clinical trials or preclinical testing.

“The drugs that have been shown to work already are presumably hitting their target,” he explains. “So it might make more sense to focus on compounds whose development has been halted, either because they didn’t work as well as people had hoped or because they caused too many side effects. There’s a chance we could rescue the promise of some of these drugs by delivering them directly to the tumor site.”

More Possible Applications

The researchers are exploring other potential uses of the particle as well. For example, they believe it could be employed to help repair kidney failure, a common problem in people who receive chemotherapy for various types of cancer. “In these patients, the proximal tubule is often the first site of damage,” Dr. Heller says.

In collaboration with nephrologist Edgar Jaimes, who heads MSK’s Renal Service, he and Dr. Williams are investigating whether this technology could potentially be used to develop therapies to accelerate kidney recovery or prevent chemotherapy-induced kidney injury. They will soon start experiments to find out if the particles can deliver small molecules that target proteins involved in acute kidney injury. They will first explore the approach in animal models with the ultimate goal to determine its usefulness in patients with chemotherapy-induced kidney injury.

Say hello to your inner molecules .

Structural biologists are revealing the astounding complexity of the molecular machinery of life. But why is it so hard to get any real sense of our molecular nature?

Computer generated images of nucleosomes

I’d like to show you your inner molecule but, to be perfectly honest, I don’t think you’re interested. Which is rather frustrating for scientists like myself who have spent a career in structural biology working out what the molecules of human life look like. You know – proteins, nucleic acids, carbohydrates, lipids. The stuff we’re all made of.

It may seem odd to complain about a lack of interest in our molecular nature because people seem to be endlessly fascinated – if not obsessed – by DNA, one of the most famous biological molecules of all time. We have little trouble understanding its importance, as the stuff of our genes, in shaping our identity and experience. It links us through evolution to every other living thing on earth and is an essential part of the story of who we are. Our individual stories can take unpleasant turns when our genes malfunction as a result of mutations that cause hereditary diseases or cancers. And lately the manipulation of DNA has been driving the fascinating, if controversial, business of genetically modifying the animals and plants on our farms; even changes to human DNA are now up for discussion as the recent debates around mitochondrial transfer and genome editing have shown.

But with DNA the focus is on the idea of genetics as an explanatory framework, rather than on the molecule itself. You can tell that’s the case because as soon as someone mentions gene products, the myriad protein molecules encoded by genes, suddenly there’s a switch-off. These minuscule molecular machines perform a bewildering range of tasks inside and outside the living cell – including synthesising pretty much all the other interesting molecules in our bodies – but even so the conversation stalls. We just don’t talk about proteins. For most people there’s no sense of connection, despite the fact that to have a sense of anything involves the protein ion channels and neurotransmitter receptors in our brains relaying the electrical and chemical signals that constitute thought. Why are we not more interested in the molecules we’re made of?

David Goodsell's painting of the cell nucleus

I guess I shouldn’t complain. It’s hard to love a protein molecule. It’s hard even to get to know one. They’re so small that you’re not ever likely to clap eyes on one unless you have access to a laboratory. It seems unfair that these vital micro-machines should be so incognito.

If I asked you right now to think of a protein, any protein, what picture would come into your mind? I don’t wish to be judgemental but I’m guessing you may well have drawn a blank. Everyone knows what DNA looks like with its oh-so-elegant double helix. But what about myoglobin, the first protein to have its structure worked out in three-dimensions – just a few years after DNA grabbed the limelight? Not such a celebrity.

Part of the problem is bad PR. John Kendrew’s work to solve the structure of myoglobin, a handy oxygen store found in muscle cells, was in fact a more impressive scientific feat that figuring out DNA (no mean achievement in itself). But the end product lacked pizzaz. It was no looker, to be sure. You can see for yourself in London’s Science Museum where the original atomic model painstakingly constructed by Kendrew in 1960 is on show as part of the Churchill’s Scientists exhibition. It’s well worth a visit if you would like to meet one of your inner molecules. The myoglobin model in the display is from sperm whale but the version in your body basically looks identical. (That’s one of the clever and unappreciated things about structural biology: it reveals similarities at the molecular level that testify to the evolutionary unity of all living things, at a level even deeper than correspondences between DNA sequences.)

Kendrew’s myoglobin model buried in a forest of rods
On show at the museum: Kendrew’s myoglobin model buried in a forest of rods Photograph: Stephen Curry/Personal Collection
It may not be pretty but there is a certain majesty to Kendrew’s model. It’s big – about a metre and a half on a side – and fantastically detailed. Every atom is on display. However, it’s not exactly easy to take in because the wireframe model has to be supported on a dense forest of wooden rods and these rather dominate proceedings. You have to peer closely to discern the wire connections between atoms and to get an idea of how the molecule takes shape. From every angle the view is obscured and fragmented. It’s difficult to appreciate that there is a superb piece of natural engineering lurking within.

But it’s not just the rods that are the problem. The thousands of protein structures that tumble out of labs every year can now be displayed in an instant in your web browser. You can go to the Protein Data Bank (PDB) where they are stored and have a look. The PDB has been working hard in recent years to make these structures accessible to the non-specialist but I wonder how many drop by?

I suspect it’s hard to drum up visitor traffic because most people don’t feel enough of a connection with their molecular selves to have a reason to go exploring. It’s not just the looks – a significant part of the problem is the complexity. To really appreciate a large biological molecule you have to know something about what it does and that often involves a fair bit of chemistry. In every case, the back story is full of arcane detail. The fancy computer graphics these days might soften some of the complex edges, and make the molecule appear friendlier, more appealing, but that’s not enough if you can’t get a handle on how the protein fits into the scheme of things.

Computer-generated representations of protein and RNA in a molecular embrace (an aminoacyl tRNA synthetase) Facebook Twitter Pinterest
Computer-generated representations of protein (grey) and RNA (orange and yellow) in a molecular embrace (an aminoacyl tRNA synthetase) Photograph: Stephen Curry/Personal Collection
The situation is made even worse by the fact that molecules are often worked on and presented to the world one at a time. Because of that isolation it can be difficult to get the sense of the thing, never mind absorb the idea that the protein you are looking at is a part of you.

That’s why I am such a fan of the work of David Goodsell, an associate Professor of Molecular Biology at the Scripps Research Institute in California. In addition to his day job as a scientist, he has faced down the complexity and isolation intrinsic to the scientific analysis of bimolecular structure by creating beautiful paintings of cellular interiors. These images put the molecules of life into a rich and meaningful context. There is some artistic licence in his work to be sure, but it is informed by the latest science – the scales, shapes and numbers of the molecular participants of these living landscapes are based on the best available information. If you would like to see inside yourself in magnificent molecular detail I highly recommend his illustrated book, The Machinery of Life, which I’ve written about before.
The molecular world comes even more alive in the animations of Drew Berry, a biomedical animator at the Walter and Eliza Hall Institute for Medical Research in Melbourne. Berry has brought a truly cinematic vision to the portrayal of biological molecules. He has taken us the closest we have yet come to seeing what really happens at the molecular level within the cells of our bodies – the processes that keep us ticking, such as the replication of DNA needed before every cell divides, or the translation of the gene sequences into the proteins that structure our cells and keep the biochemistry of life in motion. Here he is giving a TEDx talk at Sydney in 2011, showing off some of his best work. Please take a look – the animation starts at 2:48.
Drew Berry explains his art and his science at TEDx Sydney, 2011
Berry’s animations are fantastic. Like Goodsell he is committed to bringing as much rigour and scientific detail as possible to his depictions of the machinations of life. (In an accompanying post, he explains the philosophy and process of his work). There’s an impressive exactitude here, combined with a passion to show us what we are like at a granular level far beyond the ken of our senses.

The power of these animations in revealing our molecular selves is undeniable. And yet… there is an inescapable artifice that raises yet another barrier between us and our molecular components. The proteins and DNA within us cannot be seen even with the best light microscopes since they are far smaller than the wavelength of light. Scientists therefore have to resort to a bizarre toolkit of indirect methods such as X-ray crystallography, nuclear magnetic resonance or cryo-electron microscopy to provide the data that allow three-dimensional molecular models to be reconstructed in the computer. Nothing is ever seen directly though we can be confident that these techniques yield atomic coordinates accurate enough to specify how the molecules are constructed. For his movies Berry has the choice of how best to render the resulting structures – with individual atoms as spheres, or perhaps just displaying the molecular surfaces – and to colour them to enhance distinctions between different molecular parts and players (in reality, most proteins are rather colourless). These decisions are entirely reasonable and help us to see what is going on but the fact remains that none of the representations used shows what the molecules really look like because no-one has ever seen one.

None of which is to diminish Berry’s work. You can tell from his TEDx talk that he is serious about this stuff. As a structural biologist I appreciate more than most the lengths he has gone to to get things right. But even though I am immersed daily in this world, there’s one final problem with making a connection to our inner molecules that I’ve discovered in watching Berry’s careful, artful animations. However many times I tell myself that all the jiggling machinery depicted his films is at work every second of every day inside every cell of my body, somehow it still doesn’t seem quite real to me. The same is true of Goodsell’s elaborate scientific paintings. The complexity on show is mind-boggling, but immediately raises a disturbing question: how on earth does the whole shebang keep going for the decades of a human life without grinding to a halt?

Is it is too much for the mind to accept its dependence on so many thousands of molecular encounters – encounters that seem blind and mechanical? The jostling actions of mere molecules sits uncomfortably with my sense of myself as a rational agent and perhaps that is ultimately what disrupts any deep-rooted sense of the molecular self. It doesn’t matter that I know that all these molecular interactions are vital for life, that I know they have been shaped and guided by the unseen hand of evolutionary selection over billions of years, or that I’m quite comfortable with my evolutionary connections to the history of life on Earth. None of this helps me to make forge a relationship with my inner molecules that I can feel.

There is some serious cognitive dissonance going on here that is personally and professionally disturbing. Despite all my years in structural biology, it appears that knowing is not enough.

Watch the video. URL: https://youtu.be/WFCvkkDSfIU

Your Blood Type May Put You at Risk for Heart Disease

People whose blood type is A, B or AB have an increased risk of heart disease and shorter life spans than people who have type O blood, according to a new study.

But that doesn’t mean people with blood types other than O should be overly concerned, because heart disease risk and life span are influenced by multiple factors, includingexercise and overall health, experts said.

In the study, researchers followed about 50,000 middle-age and elderly people in northeastern Iran for an average of seven years. They found that people with non-O blood types were 9 percent more likely to die during the study for any health-related reason, and 15 percent more likely to die from cardiovascular disease, compared with people with blood type O.

“It was very interesting to me to find out that people with certain blood groups — non-O blood groups — have a higher risk of dying of certain diseases,” said the study’s lead investigator, Dr. Arash Etemadi, an epidemiologist at the U.S. National Institutes of Health.

The researchers also examined whether people’s blood type may be linked with their risk of gastric cancer, which has a relatively high incidence rate among the people living in northeastern Iran. They found that people with non-O blood types had a 55 percent increased risk of gastric cancer compared with people with type O blood, according to the study, published online today (Jan. 14) in the journal BMC Medicine.

The association between blood type and people’s disease risk and life span held even when the researchers accounted for other factors, including age, sex, smoking, socioeconomic status and ethnicity.

Previous studies have shown that people with non-O blood types may be at higher risk of certain cancers and cardiovascular disease, but it was less clear whether blood type is linked with life span, Etemadi told Live Science.

About 11,000 people in the study provided information about their blood’s biochemistry, including their cholesterol levels, glucose levels and blood pressure. But only certain metrics stood out — for example, the people with type A blood tended to have higher levels of total cholesterol and LDL cholesterol, also known as the “bad” cholesterol.

It’s possible that higher cholesterol levels could partly explain the increased mortality risk. People with non-O blood types also have an increased tendency to form blood clots, and this higher coagulation might lead to more heart problems, Etemadi said.

Moreover, the gene that is responsible for blood type is on the same chromosome as some of the genes responsible for controlling blood cholesterol, Etemadi said.

But it’s unlikely that the cholesterol link is solely responsible for the difference in people’s life span, he said. “We think that it’s a mixture of both causes that contribute to this increased mortality,” Etemadi said.

Although people with non-O blood types may have these increased risks, they should “absolutely not” be concerned that their blood type is the determining factor in their health, said Dr. Massimo Franchini, director of hematology and transfusion medicine at the Carlo Poma Hospital in Italy, who was not involved with the study.

“Belonging to a non-O blood type represents only a risk factor (among many others), and actually, there are many and many millions of people worldwide with non-O blood type that do not have, and will never develop, any of these diseases,” said Franchini, who wrote a commentary on the study that was also published in the journal. “Thus, in my opinion, a healthy lifestyle still remains the main factor able to influence the health status of an individual.”

Statins for Young T1D Patients, Too?

Type 1 diabetes patients younger than 40 may be candidates for statin use, as guidelines recommend after age 40, researchers suggested.

Under the American Heart Association/American College of Cardiology definition, the 10-year cardiovascular risk was about 5% for type 1 diabetes patients ages 30 to 39 and about 13% in those ages 40 to 44, Rachel G. Miller, MD, of the University of Pittsburgh, and colleagues found.

Adding coronary revascularization to that definition — which also included cardiovascular death or nonfatal stroke or myocardial infarction — brought the 10-year risk to nearly 7% for type 1 diabetes patients in their 30s, the group reported here at the American Diabetes Association meeting.

Although still a little shy of the 7.5% 10-year risk threshold recommended for statin treatment in the guidelines, the 20% of the cohort already on a statin before age 40 was excluded along with a number of events that happened before the start of follow-up.

“We conclude that young adults aged 30 to 39 years with 20 or less years’ type 1 diabetes duration are at sufficiently high atherosclerotic cardiovascular disease risk to merit statin therapy,” the group concluded in their poster presentation.

Both the AHA/ACC and the American Diabetes Association guidelinesrecommend statins after 40 for essentially all diabetes patients and support possible use for younger people with cardiovascular disease risk factors.

“We’ve been comfortable with the concept that anybody over the age of 40 with type 2 should be on a statin and by extrapolation anybody who has type 1 over the age of 40 should be recommended for statins,” commentedNaveed Sattar, MD, a metabolic medicine specialist at the University of Glasgow, Scotland.

“What we now need is good guidance: Who are these people under 40 with type 1 who should get a statin, and how do we recognize them?” he toldMedPage Today.

There isn’t enough data to develop a risk score for type 1 diabetes yet, he noted. Lifetime risk might be a better criterion in that population than the 10-year risks, which are heavily predicated upon age and which underpin current guidelines, Sattar noted.

“I think in the next 2 or 3 years either from national databases within Scandinavia or Scotland we’re going to have a type 1 diabetes risk score that might allow us to look at this question,” he suggested.

Comparisons with the general population in the surrounding county showed huge elevations in risk with type 1 diabetes even at these early ages, but absolute event numbers were small in Miller’s study.

Among the 517 people under age 45 without pre-existing atherosclerotic cardiovascular disease followed from 1996 to 2011 in the Pittsburgh Epidemiology of Diabetes Complications study (a prospective group of childhood-onset cases seen at a single center soon after diagnosis):

  • One event occurred in 20- to 29-year-olds
  • 18 accrued in those in their 30s
  • 22 occurred in participants in their early 40s

The fatal coronary artery event and nonfatal stroke or MI rates were 134 per 100,000 in the cohort ages 20 to 29, 502 per 100,000 people in their 30s, and 1,336 per 100,000 in the 40 to 44 age range.

Sattar cautioned against overinterpreting the “very crude analysis.”



At its annual assembly in Geneva last week, the World Health Organization approved a radical and far-reaching plan to slow the rapid, extensive spread of antibiotic resistance around the world. The plan hopes to curb the rise caused by an unchecked use of antibiotics and lack of new antibiotics on the market.

New Tel Aviv University research published in PNAS introduces a promising new tool: a two-pronged system to combat this dangerous situation. It nukes antibiotic resistance in selected bacteria, and renders other bacteria more sensitive to antibiotics. The research, led by Prof. Udi Qimron of the Department of Clinical Microbiology and Immunology at TAU’s Sackler Faculty of Medicine, is based on bacterial viruses called phages, which transfer “edited” DNA into resistant bacteria to kill off resistant strains and make others more sensitive to antibiotics.

According to the researchers, the system, if ultimately applied to pathogens on hospital surfaces or medical personnel’s hands, could turn the tide on untreatable, often lethal bacterial infections. “Since there are only a few pathogens in hospitals that cause most of the antibiotic-resistance infections, we wish to specifically design appropriate sensitization treatments for each one of them,” Prof. Qimron says. “We will have to choose suitable combinations of DNA-delivering phages that would deliver the DNA into pathogens, and the suitable combination of ‘killing’ phages that could select the re-sensitized pathogens.”

Reprogramming the system

“Antibiotic-resistant pathogens constitute an increasing threat because antibiotics are designed to select resistant pathogens over sensitive ones,” Prof. Qimron says. “The injected DNA does two things: It eliminates the genes that cause resistance to antibiotics, and it confers protection against lethal phages.

“We managed to devise a way to restore antibiotic sensitivity to drug-resistant bacteria, and also prevent the transfer of genes that create that resistance among bacteria,” he continues.

Earlier research by Prof. Qimron revealed that bacteria could be sensitized to certain antibiotics — and that specific chemical agents could “choose” those bacteria more susceptible to antibiotics. His strategy harnesses the CRISPR-Cas system — a bacterial DNA-reprogramming system Prof. Qimron pioneered — as a tool to expand on established principles.

According to the researchers, “selective pressure” exerted by antibiotics renders most bacteria resistant to them — hence the epidemic of lethal resistant infections in hospitals. No counter-selection pressure for sensitization of antibiotics is currently available. Prof. Qimron’s strategy actually combats this pressure — selecting for the population of pathogens exhibiting antibiotic sensitivity.

“We believe that this strategy, in addition to disinfection, could significantly render infections once again treatable by antibiotics,” said Prof. Qimron.

Prof. Qimron and his team are now poised to apply the CRISPR/phage system onpseudomonas aeruginosa — one of the world’s most prevalent antibiotic-resistant pathogens involved in hospital-acquired infections — and to test whether bacterial sensitization works in a more complex microbial environment: the mouse cage.



Human supercentenarians share at least one thing in common–over 95 percent are women. Scientists have long observed differences between the sexes when it comes to aging, but there is no clear explanation for why females live longer. In a discussion of what we know about stem cell behavior and sex, Stanford University researchers Ben Dulken and Anne Brunet argue that it’s time to look at differences in regenerative decline between men and women. This line of research could open up new explanations for how the sex hormones estrogen and testosterone, or other factors, modify lifespan.

It’s known that estrogen has direct effects on stem cell populations in female mice, from increasing the number of blood stem cells (which is very helpful during pregnancy) to enhancing the regenerative capacity of brain stem cells at the height of estrus. Whether these changes have a direct impact on lifespan is what’s yet to be explored. Recent studies have already found that estrogen supplements increase the lifespan of male mice, and that human eunuchs live about 14 years longer than non-castrated males.

More work is also needed to understand how genetics impacts stem cell aging between the sexes. Scientists have seen that knocking out different genes in mice can add longevity benefits to one sex but not the other, and that males in twin studies have shorter telomeres–a sign of shorter cellular lifespan–compared to females.

“It is likely that sex plays a role in defining both lifespan and healthspan, and the effects of sex may not be identical for these two variables,” the authors write. “As the search continues for ways to ameliorate the aging process and maintain the regenerative capacity of stem cells, let us not forget one of the most effective aging modifiers: sex.”