Posts about medical research
animals bacteria Career Cats commentary cool curiouscat economy Energy Engineering engineering education engineers evolution experiment food fun Funding government green Health Care human health innovation K-12 kids Life Science medical research MIT nature ocean physics Products Research Robots Science science education science explained science facts science webcasts scientific inquiry Students Technology university research USA water webcasts

NASA Biocapsules Deliver Medical Interventions Based Upon What They Detect in the Body

Posted on February 10, 2012  Comments (0)

Very cool innovation from NASA. The biocapsule monitors the environment (the body it is in) and responds with medical help. Basically it is acting very much like your body, which does exactly that: monitors and then responds based on what is found.

The Miraculous NASA Breakthrough That Could Save Millions of Lives

The Biocapsules aren’t one-shot deals. Each capsule could be capable of delivering many metred doses over a period of years. There is no “shelf-life” to the Biocapsules. They are extremely resilient, and there is currently no known enzyme that can break down their nanostructures. And because the nanostructures are inert, they are extremely well-tolerated by the body. The capsules’ porous natures allow medication to pass through their walls, but the nanostructures are strong enough to keep the cells in one place. Once all of the cells are expended, the Biocapsule stays in the body, stable and unnoticed, until it is eventually removed by a doctor back on Earth.
…
Dr. Loftus [NASA] thinks we could realistically see wildspread usage on Earth within 10 to 15 years.
…
The cells don’t get released from the capsule. The cells inside the capsule secrete therapeutic molecules (proteins, peptides), and these agents exit the capsule by diffusion across the capsule wall.

NASA plans to use the biocapsules in space, but they also have very promising uses on earth. They can monitor a diabetes patient and if insulin is needed, deliver it. No need for the person to remember, or give themselves a shot of insulin. The biocapsule act just like out bodies do, responding to needs without us consciously having to think about it. They can also be used to provide high dose chemotherapy directly to the tumor site (thus decreasing the side effects and increasing the dosage delivered to the target location. Biocapsules could also respond to severe allergic reaction and deliver epinephrine (which many people know have to carry with them to try and survive an attack).

It would be great if this were to have widespread use 15 years from now. Sadly, these innovations tend to take far longer to get into productive use than we would hope. But not always, so here is hoping this innovation from NASA gets into ourselves soon.

Related: Using Bacteria to Carry Nanoparticles Into Cells – Nanoparticles With Scorpion Venom Slow Cancer Spread – Self-Assembling Cubes Could Deliver Medicine – Nanoengineers Use Tiny Diamonds for Drug Delivery

Microbiologist Develops Mouthwash That Targets Only Harmful Cavity Causing Bacteria

Posted on February 1, 2012  Comments (0)

A new mouthwash developed by a microbiologist at the UCLA School of Dentistry is highly successful in targeting the harmful Streptococcus mutans bacteria that is the principal cause tooth decay and cavities.

In a recent clinical study, 12 subjects who rinsed just one time with the experimental mouthwash experienced a nearly complete elimination of the S. mutans bacteria over the entire four-day testing period.

Dental caries, commonly known as tooth decay or cavities, is one of the most common and costly infectious diseases in the United States, affecting more than 50 percent of children and the vast majority of adults aged 18 and older. Americans spend more than $70 billion each year on dental services, with the majority of that amount going toward the treatment of dental caries.

This new mouthwash is the product of nearly a decade of research conducted by Wenyuan Shi, chair of the oral biology section at the UCLA School of Dentistry. Shi developed a new antimicrobial technology called STAMP (specifically targeted anti-microbial peptides) with support from Colgate-Palmolive and from C3-Jian Inc., a company he founded around patent rights he developed at UCLA; the patents were exclusively licensed by UCLA to C3-Jian.

The human body is home to millions of different bacteria, some of which cause diseases such as dental caries but many of which are vital for optimum health. Most common broad-spectrum antibiotics, like conventional mouthwash, indiscriminately kill both benign and harmful pathogenic organisms and only do so for a 12-hour time period.

The overuse of broad-spectrum antibiotics can seriously disrupt the body’s normal ecological balance, rendering humans more susceptible to bacterial, yeast and parasitic infections.

Shi’s Sm STAMP C16G2 investigational drug, tested in the clinical study, acts as a sort of “smart bomb,” eliminating only the harmful bacteria and remaining effective for an extended period.

“With this new antimicrobial technology, we have the prospect of actually wiping out tooth decay in our lifetime,” said Shi, who noted that this work may lay the foundation for developing additional target-specific “smart bomb” antimicrobials to combat other diseases.

Related: full press release – False Teeth For Cats – Cavity-Fighting Lollipop – Biologists Identified a New Way in Which Bacteria Hijack Healthy Cells

How Lysozyme Protein in Our Tear-Drops Kill Bacteria

Posted on January 24, 2012  Comments (0)

A disease-fighting protein in our teardrops has been tethered to a tiny transistor, enabling UC Irvine scientists to discover exactly how it destroys dangerous bacteria. The research could prove critical to long-term work aimed at diagnosing cancers and other illnesses in their very early stages.

Ever since Nobel laureate Alexander Fleming found that human tears contain antiseptic proteins called lysozymes about a century ago, scientists have tried to solve the mystery of how they could relentlessly wipe out far larger bacteria. It turns out that lysozymes have jaws that latch on and chomp through rows of cell walls like someone hungrily devouring an ear of corn.

“Those jaws chew apart the walls of the bacteria that are trying to get into your eyes and infect them,” said molecular biologist and chemistry professor Gregory Weiss, who co-led the project with associate professor of physics & astronomy Philip Collins.

The researchers decoded the protein’s behavior by building one of the world’s smallest transistors – 25 times smaller than similar circuitry in laptop computers or smartphones. Individual lysozymes were glued to the live wire, and their eating activities were monitored.

“Our circuits are molecule-sized microphones,” Collins said. “It’s just like a stethoscope listening to your heart, except we’re listening to a single molecule of protein.”

It took years for the UCI scientists to assemble the transistor and attach single-molecule teardrop proteins. The scientists hope the same novel technology can be used to detect cancerous molecules. It could take a decade to figure out but would be well worth it, said Weiss, who lost his father to lung cancer.

“If we can detect single molecules associated with cancer, then that means we’d be able to detect it very, very early,” Weiss said. “That would be very exciting, because we know that if we treat cancer early, it will be much more successful, patients will be cured much faster, and costs will be much less.”

The project was sponsored by the National Cancer Institute and the National Science Foundation. Co-authors of the Science paper are Yongki Choi, Issa Moody, Patrick Sims, Steven Hunt, Brad Corso and Israel Perez.

Related: full press release – Why ‘Licking Your Wounds’ Works – How Bleach Kills Bacteria – Algorithmic Self-Assembly

Healthy Diet, Healthy Living, Healthy Weight

Posted on January 4, 2012  Comments (2)

Living and eating healthily is tricky but not entirely confusing. The whole area of eating healthy food and what is a healthy weight is one where the scientific inquiry process and the complexity of scientific research on what is healthy for us is clear. Scientists study various issues and learn things but creating simple rules has proven difficult. Different studies seem to show benefits of contradictory advice, advice once seen as wise is now seen as wrong…

This is an area I am far from knowledgable about. Still I try to pay some attention as I like being healthy. Being sick is the quickest way to appreciate how great it is to be healthy. From various things I have skimmed it seems there is more evidence from several studies about how difficult it is to lose weight. Our bodies seem to work against our efforts.

And this, it seems to me, makes the problem of increasing childhood and teen obesity even more important to deal with as soon as issues arise.

It seems to me the most important thing to take from this, is the importance of maintaining a healthy weight: since you can’t just easily make up for a bad year of weight gain. I am not sure why I haven’t seen this note in most of what I have read – I suspect it is our reluctance to make value judgements about what is healthy. The problem I see with that is, the best advice we have is confusing enough without people with more knowledge being reluctant to state their best advice given the current knowledge. That doesn’t mean the suggestions are right, but at least they are educated guesses.

I try to eat relatively healthily. Which for me means taking steps to increase the amount of vegetables I eat (especially greens and some fiber) and decrease the amount of sweets and heavily processed food I eat (I still eat way too much heavily processed food). And I try to exercise as it seems to have many benefits including helping make up for some weaknesses in your diet (like eating too many calories and too many “empty calories). In my opinion (which on this topic may well not be worth much) eating a bit more stuff that really isn’t so good for you and exercising more is an easier tradeoff than trying to eat perfectly and do the minimum amount of exercise needed to stay healthy.

I also eat yogurt – I like it and the beneficial benefits of some bacteria seems likely. I heard recently something that surprised me which is that the beneficial bacteria remain for close to 2 weeks. I figured they would be gone in a couple days. I only heard that from one source (I can’t remember now but some seemingly knowledgable source – scientist researching the area), so it might not be accurate but it was interesting.

Here is an example of one of these health studies. They find that a low protein diet resulted in a loss of “lean weight” (muscle…) and more fat than a comparable diet with more protein. The same weight with a higher percentage of fat is not a good thing for human health. Thus the message is that a lower protein diet has this risk that must be considered (and therefor higher protein diets may well be wise). Of course things get much more complicated than that when we actually try to live by a diet.

Effect of Dietary Protein Content on Weight Gain, Energy Expenditure, and Body Composition During Overeating

Continue reading →

Can Just A Few Minute of Exercise a Day Prevent Diabetes?

Posted on December 17, 2011  Comments (5)

That just 1 minute of exercise a day could help prevent diabetes seems to good to be true. But research at the University of Bath indicates it might be true. I am a bit of a soft touch for seeing the benefits of exercise. And I also love health care that focuses on achieving healthy lives instead of what most of the spending focuses on: treating illness.

Performing short cycle sprints three times a week could be enough to prevent and possibly treat Type 2 diabetes researchers at the University of Bath believe.

Volunteers were asked to perform two 20-second cycle sprints, three times per week (but really this works out to under 10 minutes of total time including warm up). After six weeks researchers saw a 28% improvement in their insulin function. Type 2 diabetes occurs when blood sugar levels build up to dangerously high levels due to reduced insulin function, often caused by a sedentary lifestyle. The condition can cause life-threatening complications to the heart, kidneys, eyes and limbs, and has huge costs (monetarily and to people’s lives).

Regular exercise can help keep blood sugar levels low but busy lifestyles and lack of motivation mean 66% of the population is not getting the recommended five 30-minute sessions of moderate exercise a week.

Dr Niels Vollaard who is leading the study, said: “Our muscles have sugar stores, called glycogen, for use during exercise. To restock these after exercise the muscle needs to take up sugar from the blood. In inactive people there is less need for the muscles to do this, which can lead to poor sensitivity to insulin, high blood sugar levels, and eventually type 2 diabetes… We already knew that very intense sprint training can improve insulin sensitivity but we wanted to see if the exercise sessions could be made easier and shorter.”

In the study the resistance on the exercise bikes could be rapidly increased so volunteers were able to briefly exercise at much higher intensities than they would otherwise be able to achieve. With an undemanding warm-up and cool-down the total time of each session was only 10 minutes.

This type of study is very helpful in identifying solutions that will allow more people to lead healthy lives and save our economies large amount of money. Medical studies can’t be accepted on face value. They are often not confirmed by future studies and therefore it is unwise to rely on the results of 1 study. The results provide interesting information but need to be confirmed (and in the area of studies on human health this has been shown to be problematic – are health is quite a tricky area to study).

Related: Aerobic Exercise Plus Resistance Training Helps Control Type 2 Diabetes – Regular Exercise Reduces Fatigue – Food Rules: An Eater’s Manual

Continue reading →

2011 Nobel Prize in Physiology or Medicine

Posted on October 3, 2011  Comments (0)

The Nobel Assembly at Karolinska Institutet has today decided that The Nobel Prize in Physiology or Medicine 2011 shall be divided, with one half jointly to Bruce A. Beutler and Jules A. Hoffmann for their discoveries concerning the activation of innate immunity and the other half to Ralph M. Steinman for his discovery of the dendritic cell and its role in adaptive immunity.

This year’s Nobel Laureates have revolutionized our understanding of the immune system by discovering key principles for its activation.

Scientists have long been searching for the gatekeepers of the immune response by which man and other animals defend themselves against attack by bacteria and other microorganisms. Bruce Beutler and Jules Hoffmann discovered receptor proteins that can recognize such microorganisms and activate innate immunity, the first step in the body’s immune response. Ralph Steinman discovered the dendritic cells of the immune system and their unique capacity to activate and regulate adaptive immunity, the later stage of the immune response during which microorganisms are cleared from the body.

The discoveries of the three Nobel Laureates have revealed how the innate and adaptive phases of the immune response are activated and thereby provided novel insights into disease mechanisms. Their work has opened up new avenues for the development of prevention and therapy against infections, cancer, and inflammatory diseases.

We live in a dangerous world. Pathogenic microorganisms (bacteria, virus, fungi, and parasites) threaten us continuously but we are equipped with powerful defense mechanisms (please see image below). The first line of defense, innate immunity, can destroy invading microorganisms and trigger inflammation that contributes to blocking their assault. If microorganisms break through this defense line, adaptive immunity is called into action. With its T and B cells, it produces antibodies and killer cells that destroy infected cells. After successfully combating the infectious assault, our adaptive immune system maintains an immunologic memory that allows a more rapid and powerful mobilization of defense forces next time the same microorganism attacks. These two defense lines of the immune system provide good protection against infections but they also pose a risk. If the activation threshold is too low, or if endogenous molecules can activate the system, inflammatory disease may follow.

The components of the immune system have been identified step by step during the 20th century. Thanks to a series of discoveries awarded the Nobel Prize, we know, for instance, how antibodies are constructed and how T cells recognize foreign substances. However, until the work of Beutler, Hoffmann and Steinman, the mechanisms triggering the activation of innate immunity and mediating the communication between innate and adaptive immunity remained enigmatic.

Related: 2009 Nobel Prize in Physiology or Medicine – Nobel Prize in Physiology or Medicine 2008 – 2009 Nobel Prize in Chemistry: the Structure and Function of the Ribosome

photo of Ralph Steinman

Ralph Steinman was awarded the Nobel Prize for his discovery of the dendritic cell and its role in adaptive immunity. He was born in Canada and was a professor at Rockefeller University at the end of his career.

Continue reading →

Molecule Found in Sharks Kills Many Viruses that are Deadly to People

Posted on September 20, 2011  Comments (1)

photo of 3 dogfish sharks
Shark Molecule Kills Human Viruses, Too

“Sharks are remarkably resistant to viruses,” study researcher Michael Zasloff, of the Georgetown University Medical Center, told LiveScience. Zasloff discovered the molecule, squalamine, in 1993 in the dogfish shark, a small- to medium-size shark found in the Atlantic, Pacific, and Indian Oceans.

“It looked like no other compound that had been described in any animal or plant before. It was something completely unique,” Zasloff said. The compound is a potent antibacterial and has shown efficacy in treating human cancers and an eye condition known as macular degeneration, which causes blindness.
…
By studying the compound’s structure and how it works in the human body, Zasloff thought it might have some antiviral properties. He saw that the molecule works by sticking to the cell membranes of the liver and blood vessels. While there, it kicks off other proteins, some of which are essential for viruses to enter and survive in the cell.

The researchers decided to test the compound on several different live viruses that infect liver cells, including hepatitis B, dengue virus and yellow fever. They saw high efficacy across the board.
…
Zasloff hopes to start human trials in the next few years.
…
Marc Maresca, a researcher at Paul Cézanne University in Aix-en-Provence, France, who wasn’t involved in the study, agreed that the concentrations used were quite high, possibly in toxic ranges for some cells, but in an email to LiveScience Meresca also called the study “very exciting.”

Related: Alligator Blood Provides Strong Resistance to Bacteria and Viruses – Female Sharks Can Reproduce Alone – Monarch Butterflies Use Medicinal Plants

Synthetic Biologists Design a Gene that Forces Cancer Cells to Commit Suicide

Posted on September 4, 2011  Comments (2)

Killing a cancer cell from the inside out

To create their tumor-killing program, the researchers designed a logic circuit — a system that makes a decision based on multiple inputs. In this case, the circuit is made of genes that detect molecules specific to a type of cervical cancer cell. If the right molecules are present, the genes initiate production of a protein that stimulates apoptosis, or programmed cell death. If not, nothing happens.

Because the genes used to create the circuits can be easily swapped in and out, this approach could also yield new treatments or diagnostics for many other diseases, according to Ron Weiss, an MIT associate professor of biological engineering and one of the leaders of the research team. “This is a general technology for disease-state detection,” he says.
…
the researchers created a synthetic gene for a protein, called hBax, that promotes cell death. They designed the gene with two separate safeguards against the killing of healthy, non-HeLa cells: It can be turned off by high levels of microRNAs that are ordinarily low in HeLa, and can also be deactivated by low levels of microRNAs that are normally plentiful in HeLa. A single discrepancy from the target microRNA profile is enough to shut off production of the cell-death protein.

If all microRNA levels match up with the HeLa profile, the protein is produced and the cell dies. In any other cell, the protein never gets made, and the synthetic genes eventually break down.

More very cool research. It is exciting to see how much can be done when we invest in science and engineering research. Of course the path from initial research to implemented solutions is long and complex and often fails to deliver on the initial hopes. But some remarkable breakthroughs achieve spectacular results that we benefit from every day.

Related: Cancer Vaccines – Researchers Find Switch That Allows Cancer Cells to Spread – Global Cancer Deaths to Double by 2030 – Cloned Immune Cells Clear Patient’s Cancer

MIT Scientists Find New Drug That Could Cure Nearly Any Viral Infection

Posted on August 17, 2011  Comments (1)

New drug could cure nearly any viral infection

The drug works by targeting a type of RNA produced only in cells that have been infected by viruses. “In theory, it should work against all viruses,” says Todd Rider, a senior staff scientist in Lincoln Laboratory‘s Chemical, Biological, and Nanoscale Technologies Group who invented the new technology.
…
There are a handful of drugs that combat specific viruses, such as the protease inhibitors used to control HIV infection, but these are relatively few in number and susceptible to viral resistance.

Rider drew inspiration for his therapeutic agents, dubbed DRACOs (Double-stranded RNA Activated Caspase Oligomerizers), from living cells’ own defense systems. When viruses infect a cell, they take over its cellular machinery for their own purpose — that is, creating more copies of the virus. During this process, the viruses create long strings of double-stranded RNA (dsRNA), which is not found in human or other animal cells.

As part of their natural defenses against viral infection, human cells have proteins that latch onto dsRNA, setting off a cascade of reactions that prevents the virus from replicating itself. However, many viruses can outsmart that system by blocking one of the steps further down the cascade.

Rider had the idea to combine a dsRNA-binding protein with another protein that induces cells to undergo apoptosis (programmed cell suicide) — launched, for example, when a cell determines it is en route to becoming cancerous. Therefore, when one end of the DRACO binds to dsRNA, it signals the other end of the DRACO to initiate cell suicide.

Combining those two elements is a “great idea” and a very novel approach, says Karla Kirkegaard, professor of microbiology and immunology at Stanford University. “Viruses are pretty good at developing resistance to things we try against them, but in this case, it’s hard to think of a simple path pathway to drug resistance,” she says.

Each DRACO also includes a “delivery tag,” taken from naturally occurring proteins, that allows it to cross cell membranes and enter any human or animal cell. However, if no dsRNA is present, DRACO leaves the cell unharmed.

Very cool stuff and potentially hugely beneficial. Just a reminder: this works against viruses – not bacteria (just as antibiotics do not work against viruses).

image showing the results of cultures treated with DRACO v. those not treated

Related: Science Explained: RNA Interference – 8 Percent of the Human Genome is Old Virus Genes – Virus Engineered To Kill Deadly Brain Tumors
Continue reading →

Cat Allergy Vaccine Created

Posted on April 2, 2011  Comments (5)

McMaster University researchers have developed a vaccine which successfully treats people with an allergy to cats. Traditionally, frequent allergy shots have been considered the most effective way to bring relief — other than getting rid of the family pet — for the 8 to 10% of the population allergic to cats.

Both options, may now be avoided thanks to the work of immunologist Mark Larché, professor at the Michael G. DeGroote School of Medicine and Canada Research Chair in Allergy & Immune Tolerance.

Building on research he’s conducted for the past 10 years in Canada and Britain, Larché and his research team have developed a vaccine which is effective and safe with almost no side effects. The research is published in a the January 2011 issue of the Journal of Allergy & Clinical Immunology, a leading journal in the allergy field.

The researchers took one protein (molecule) that cats secrete on their fur which causes the majority of allergic problems. Using blood samples from 100 patient volunteers allergic to cats, they deconstructed the molecule and identified short regions within the protein which activate T-cells (helper cells that fight infection) in the immune system.

Using the amino acid code for the whole protein, researchers made synthetic versions of these regions. For the cat allergy vaccine, they found seven peptides (strings of amino acids). “And those synthetic peptides are what we mix together to make the vaccine,” said Larché. “We picked the peptides that would work in as much of the population as possible.”

Known as “peptide immunotherapy,” a low dose of the vaccine is given into the skin. Initially, four to eight doses a year may be required, but the side effects of the traditional allergy shots do not arise, Larché said. The optimal dose will be determined in phase three clinical trials which are getting underway with a much larger group of cat allergy sufferers.

The development of a vaccine to treat people allergic to cats is the first in a line of vaccines developed with Adiga Life Sciences, a company established at McMaster in 2008. It is a joint venture between McMaster University Circassia Ltd., a UK-based biotech company.

Adiga and McMaster are now collaborating on research into the use of peptide immunotherapy for house dust mite, ragweed, grass, birch tree and moulds

Related: MIT Engineers Design New Type of Nanoparticle for Vacines – 10 Questions to Ask Your Vet About Cat Medications – Vaccine For Strep Infections

Video showing malaria breaking into cell

Posted on January 20, 2011  Comments (0)

Malaria caught on camera breaking and entering cell

The Plasmodium parasite responsible for malaria is transmitted by the bite of infected mosquitoes, and is thought to kill almost 1 million people worldwide each year.

Jake Baum at the Walter and Eliza Hall Institute of Medical Research in Melbourne, Australia, and colleagues used transmission electron microscopy and 3D immuno-fluorescence microscopy to record a series of still images during the 30-second-long invasion, and combined them into a movie.

Related: Parasites in the Gut Help Develop a Healthy Immune System – Parasite Rex

  • Recent Comments:

    • Donnie: Hong Kong is a city in China…… The stupidity of my country continues to amaze me.
    • Igoritza: Damn, Abel … where did you get that one from .. ? I would like to see extended theory of Dr...
    • curiouscat: I agree that ADHD medication is warranted in some cases. My guess is that is much much lower...
    • Tom Bargeron: I know that there is tendency for over active kids especially boys to be diagnosed as having...
    • sojib: wow Magnetic Movie is so amazing . I don’t think about that how can it’s making for...
    • Vance Miller: I can’t get enough vegetables, even when I try. I have made it a priority to go to our...
    • marylou: I’m agree. I’ve been friendless for 2 years and my BF said I’m more stone...
    • marylou: what a terrible myth it is those wannabe experts spread that if you want to lose weight, you have...

  • Recent Trackbacks:

  • Links