Soy-dairy protein blend increases muscle mass, study shows

A new study published online in the Journal of Applied Physiology shows additional benefits of consuming a blend of soy and dairy proteins after resistance exercise for building muscle mass. Researchers from the University of Texas Medical Branch found that using a protein blend of soy, casein and whey post-workout prolongs the delivery of select amino acids to the muscle for an hour longer than using whey alone. It also shows a prolonged increase in amino acid net balance across the leg muscle during early post-exercise recovery, suggesting prolonged muscle building.The study was conducted by researchers from UTMB in collaboration with DuPont Nutrition and Health. “This study sheds new light on how unique combinations of proteins, as opposed to single protein sources, are important for muscle recovery following exercise and help extend amino acid availability, further promoting muscle growth,” said Blake B. Rasmussen, chairman of UTMB’s Department of Nutrition and Metabolism and lead researcher of the study.This new research, using state-of-the-art methodology, builds on an earlier publication reporting that a soy-dairy blend extends muscle protein synthesis when compared to whey alone, as only the blended protein kept synthesis rates elevated three to five hours after exercise. Together, these studies indicate that the use of soy-dairy blends can be an effective strategy for active individuals seeking products to support muscle health.”Because of the increased demand for high-quality protein, this study provides critical insight for the food industry as a whole, and the sports nutrition market in particular,” said Greg Paul, global marketing director for DuPont Nutrition and Health. “With more and more consumers recognizing the importance of protein for their overall health and well-being, the results of this study have particular relevance to a large segment of the population, from the serious sports and fitness enthusiast to the mainstream consumer.”The double-blind, randomized clinical trial included 16 healthy subjects, ages 19 to 30, to assess if consumption of a blend of proteins with different digestion rates would prolong amino acid availability and lead to increases in muscle protein synthesis after exercise. The protein beverages provided to study subjects consisted of a soy-dairy blend (25 percent isolated DuPont Danisco SUPRO soy protein, 50 percent caseinate, 25 percent whey protein isolate) or a single protein source (whey protein isolate). Muscle biopsies were taken at baseline and up to five hours after resistance exercise. The protein sources were ingested one hour after exercise in both groups.The study demonstrates that consuming a soy-dairy blend leads to a steady rise in amino acids, the building blocks of muscle. …

Read more

Food quality will suffer with rising carbon dioxide, field study shows

For the first time, a field test has demonstrated that elevated levels of carbon dioxide inhibit plants’ assimilation of nitrate into proteins, indicating that the nutritional quality of food crops is at risk as climate change intensifies.Findings from this wheat field-test study, led by a UC Davis plant scientist, will be reported online April 6 in the journal Nature Climate Change.”Food quality is declining under the rising levels of atmospheric carbon dioxide that we are experiencing,” said lead author Arnold Bloom, a professor in the Department of Plant Sciences.”Several explanations for this decline have been put forward, but this is the first study to demonstrate that elevated carbon dioxide inhibits the conversion of nitrate into protein in a field-grown crop,” he said.The assimilation, or processing, of nitrogen plays a key role in the plant’s growth and productivity. In food crops, it is especially important because plants use nitrogen to produce the proteins that are vital for human nutrition. Wheat, in particular, provides nearly one-fourth of all protein in the global human diet.Many previous laboratory studies had demonstrated that elevated levels of atmospheric carbon dioxide inhibited nitrate assimilation in the leaves of grain and non-legume plants; however there had been no verification of this relationship in field-grown plants.Wheat field studyTo observe the response of wheat to different levels of atmospheric carbon dioxide, the researchers examined samples of wheat that had been grown in 1996 and 1997 in the Maricopa Agricultural Center near Phoenix, Ariz.At that time, carbon dioxide-enriched air was released in the fields, creating an elevated level of atmospheric carbon at the test plots, similar to what is now expected to be present in the next few decades. Control plantings of wheat were also grown in the ambient, untreated level of carbon dioxide.Leaf material harvested from the various wheat tests plots was immediately placed on ice, and then was oven dried and stored in vacuum-sealed containers to minimize changes over time in various nitrogen compounds.A fast-forward through more than a decade found Bloom and the current research team able to conduct chemical analyses that were not available at the time the experimental wheat plants were harvested.In the recent study, the researchers documented that three different measures of nitrate assimilation affirmed that the elevated level of atmospheric carbon dioxide had inhibited nitrate assimilation into protein in the field-grown wheat.”These field results are consistent with findings from previous laboratory studies, which showed that there are several physiological mechanisms responsible for carbon dioxide’s inhibition of nitrate assimilation in leaves,” Bloom said.3 percent protein decline expectedBloom noted that other studies also have shown that protein concentrations in the grain of wheat, rice and barley — as well as in potato tubers — decline, on average, by approximately 8 percent under elevated levels of atmospheric carbon dioxide.”When this decline is factored into the respective portion of dietary protein that humans derive from these various crops, it becomes clear that the overall amount of protein available for human consumption may drop by about 3 percent as atmospheric carbon dioxide reaches the levels anticipated to occur during the next few decades,” Bloom said.While heavy nitrogen fertilization could partially compensate for this decline in food quality, it would also have negative consequences including higher costs, more nitrate leaching into groundwater and increased emissions of the greenhouse gas nitrous oxide, he said.Story Source:The above story is based on materials provided by University of California – Davis. Note: Materials may be edited for content and length.

Read more

Diets high in animal protein may help prevent functional decline in elderly individuals

A diet high in protein, particularly animal protein, may help elderly individuals maintain a higher level of physical, psychological, and social function according to a study published in the Journal of the American Geriatrics Society.Due to increasing life expectancies in many countries, increasing numbers of elderly people are living with functional decline, such as declines in cognitive ability and activities of daily living. This can have profound effects on the health and well-being of older adults and their caregivers, as well as on health care resources.Research suggests that as people age, their ability to absorb or process protein may decline. To compensate for this loss, protein requirements may increase with age. Megumi Tsubota-Utsugi, PhD, MPH, RD, of the National Institute of Health and Nutrition in Japan, and her colleagues in Tohoku University and Teikyo University, Japan, wondered whether protein intake might affect the functional capabilities of older adults. They designed a study to investigate the relationship between protein intake and future decline in higher-level functional capacity in older community-dwelling adults in Japan. Their analysis included 1,007 individuals with an average age of 67.4 years who completed food questionnaires at the start of the study and seven years later. Participants were divided into four groups (quartiles) according to their intake levels of total, animal, and plant protein. Tests of higher-level functional capacity included social and intellectual aspects as well as measures related to activities of daily living.Men in the highest quartile of animal protein intake had a 39 percent decreased chance of experiencing higher-level functional decline than those in the lowest quartile. These associations were not seen in women. No consistent association was observed between plant protein intake and future higher-level functional decline in either sex.”Identifying nutritional factors that contribute to maintaining higher-level functional capacity is important for prevention of future deterioration of activities of daily living,” said Dr. …

Read more

Look back at US soybeans shows genetic improvement behind increased yields

Soybean improvement through plant breeding has been critical over the years for the success of the crop. In a new study that traces the genetic changes in varieties over the last 80 years of soybean breeding, researchers concluded that increases in yield gains and an increased rate of gains over the years are largely due to the continual release of greater-yielding cultivars by breeders.”This research in some ways looks back and informs us how soybean varieties have changed. It’s useful to document these traits and changes,” said Brian Diers, a University of Illinois plant breeder and researcher on the study. “We can show that we really have been successful at increasing yield.”But this study is also about the future of the soybean crop.”The study has actually created quite a lot of interest among soybean breeders because they want to understand what’s happened, and when we look at physiological traits, we can see what has been changed. This gives us clues about what traits we should focus on in breeding for future increases based what has been inadvertently changed over time as we have selected for yield,” he said.Diers and a multi-institutional team of researchers evaluated historic sets of 60 maturity group (MG) II, 59 MG III, and 49 MG IV soybean varieties, released from 1923 to 2008, in field trials conducted in 17 states and one Canadian province during 2010 to 2011.The experiments included plant introductions (PIs) and public cultivars obtained from the USDA Soybean Germplasm Collection housed at the National Soybean Research Center at the U of I, as well as from varieties provided by Monsanto, Pioneer, and Syngenta.In the process of documenting the genetic changes, the researchers observed an increase in yields over the past 80 years that is equivalent to one-third of a bushel per acre per year increase.Diers said that the researchers estimated that about two-thirds of the yield increases in farmer’s fields are due to new varieties that breeders have introduced with the other third due to other reasons such as improved agronomic practices.”When we compare old varieties to new varieties, the new varieties do yield much better than the old varieties. When we look at the data more closely, the yield increases have actually accelerated starting in the 1960s and 1970s. It’s different for each maturity group, but current yield increases are greater than they were earlier,” Diers said.This research also showed that when compared to old varieties, plants in the new varieties are shorter in height, mature later, lodge less, and have seeds with less protein and greater oil concentration.”The new varieties tend to mature later within these maturity groups, which is something that theoretically shouldn’t happen because we classify these varieties based on when they mature. So theoretically MG II varieties should mature at the same time now as one back in the 1970s, but this is not the case,” Diers said. “Probably over time, people have been selecting varieties that are a little bit later and later, and these changes have accumulated. In some ways, it’s not a bad thing, because farmers are planting earlier than they did back in the 1970s so they actually need varieties that will mature later than back then. …

Read more

New biological mechanisms, treatment paradigm for kidney disease

Prevention and reversal of chronic kidney disease is an urgent public health need. The disease affects 1 in 10 Americans, is debilitating and deadly, and existing drugs, at best, offer only mild delay in progression to end-stage kidney failure. New research led by Icahn School of Medicine at Mount Sinai investigators has uncovered abnormal molecular signaling pathways from disease initiation to irreversible kidney damage, kidney failure, and death. Results from their preclinical and human research are published online March 3 in the Journal of Clinical Investigation.“Our group is the first to show that endothelial mitochondrial oxidative stress [damage to blood vessel lining that affects the energy-producing part of the cell caused by oxidative stress] regulates the passage of proteins from blood to urine and filtration of waste products in the kidney,” said Erwin Bottinger, MD, Director of the Charles Bronfman Institute for Personalized Medicine, and the study’s senior author. Specifically, the researchers found albuminuria (protein in the urine) and depletion of the cells that form the kidney’s glomerular filtration barrier. “These findings were unexpected and open the door for developing new therapeutic targets,” Dr. Bottinger added.In the preclinical part of the research, investigators used a mouse model to induce scarring in the filtration part of the kidney, or glomeruli. This allowed progressive amounts of protein to pass into the urine and interfered with the clearance of waste products by the kidney. Essentially, the researchers were examining how different signaling mechanism and cellular interactions work, and how when they are disturbed, they promote chronic kidney disease.Initially, key cells of the glomerular filtration barrier, also called podocytes, cause alterations in endothelin-1, a vasoconstrictor, activating the endothelin receptor A. The activated endothelin receptor A triggered disturbances manifested as endothelial mitochondrial oxidative stress.The research team was able to confirm that this worked the same way in humans. …

Read more

Clutter cutter: Computer modeling used to understand how messy cells contribute to cancer

Life can be messy at all scales, requiring different organizational strategies — from cleaning the house, to removing damaged or expired cells from the body to avoid cancer progression.In a messy house, people use computers to manage paper and photo clutter; companies use computer systems to track their inventory. Now a team of researchers at Vanderbilt University in Nashville, Tenn., is taking a similar approach to cell-molecular inventory control for cancer. They have created computer models, using their programming framework (PySB), which enable them to explore the complex biochemical processes that drive cancer growth.”Our hypothesis is that understanding how the cell uses their protein inventory will lead to understanding why cells dysregulate and become carcinogenic. We expect model outputs will lead to novel, targeted cancer therapies — possibly by 2019,” explained researcher Carlos F. Lopez, who will present the work at the 58th annual Biophysical Society Meeting in San Francisco, Feb.15-19.Lopez is interested in understanding how cells in multicellular organisms engage programmed cell death — so-called “cell suicide” — for cellular removal. It is a natural part of many cells’ life cycle.When cancer cells avoid programmed cell death, uncontrolled growth fuels tumor progression. The Vanderbilt team expects their computer models to identify what goes wrong in these cases, at a speed and scale never before possible. Lopez noted: “We are bridging the nanoscale molecular-level biochemical interactions with the macroscale cancer tumor outcomes, which is a huge range in scales. Most people don’t realize this, but molecular chemical reactions at the nanometer and nanosecond level affect things that happen at the timescale level of years — nine orders of magnitude in space and time! For comparison, a nanosecond is to a second like a second is to one century.”Rather than listing the cellular biochemical reactions by hand, PySB enables the researchers to “write” the biochemical cellular processes as computer programs. …

Read more

New RNA interference technique finds seven genes for head and neck cancer

In the hunt for genetic mutations that cause cancer, there is a lot of white noise. So although genetic sequencing has identified hundreds of genetic alterations linked to tumors, it’s still an enormous challenge to figure out which ones are actually responsible for the growth and metastasis of cancer. Scientists in Rockefeller’s Laboratory of Mammalian Cell Biology and Development have created a new technique that can weed out that noise — eliminating the random bystander genes and identifying the ones that are critical for cancer. Applying their technique to head and neck cancers, they’ve discovered seven new tumor-suppressor genes whose role in cancer was previously unknown.The new technique, which the lab recently applied to a screen for skin tumor genes, is particularly useful because it takes a fraction of the resources and much less time than the traditional method for determining gene function — breeding genetically modified animals to study the impact of missing genes.”Using knockout mice, which are model organisms bred to have a particular gene missing, is not feasible when there are 800 potential head and neck cancer genes to sort through,” says Daniel Schramek, a postdoctoral fellow in the lab, which is headed by Rebecca C. Lancefield Professor Elaine Fuchs. “It can take about two years per gene. Our method can assess about 300 genes in a single mouse, in as little as five weeks.”The researchers made use of RNA interference, a natural process whereby RNA molecules inhibit gene expression. They took short pieces of RNA which are able to turn off the function of specific genes, attached them to highly concentrated viruses, and then, using ultrasound to guide the needle without damaging surrounding tissue, they injected the viruses into the sacs of mouse embryos.”The virus is absorbed and integrated into the chromosomes of the single layer of surface cells that cover the tiny embryo,” explains Fuchs. “As the embryo develops, this layer of cells becomes the skin, mammary glands and oral tissue, enabling us to efficiently, selectively and quickly eliminate the expression of any desired gene in these tissues. The non-invasive method avoids triggering a wound or inflammatory response that is typically associated with conventional methods to knockdown a gene in cultured cells and then engraft the cells onto a mouse.”When the mice grew, the researchers determined which genes, when turned off, were promoting tumor growth, and what they found was surprising.”Among the seven novel tumor suppressor genes we found, our strongest hit was Myh9, which codes for the protein myosin IIa, a motor protein with well-known function in cell structure and cell migration,” says Schramek. …

Read more

Superbright, fast X-rays image single layer of proteins

In biology, a protein’s shape is key to understanding how it causes disease or toxicity. Researchers who use X-rays to take snapshots of proteins need a billion copies of the same protein stacked and packed into a neat crystal. Now, scientists using exceptionally bright and fast X-rays can take a picture that rivals conventional methods with a sheet of proteins just one protein molecule thick.Using a type of laser known as XFEL, the technique opens the door to learning the structural details of almost 25 percent of known proteins, many of which have been overlooked due to their inability to stack properly. The team of researchers led by the Department of Energy’s Pacific Northwest and Lawrence Livermore National Laboratories report their results with this unique form of X-ray diffraction in the March issue of the International Union of Crystallography Journal.”In this paper, we’re proving it’s possible to use an XFEL to study individual monolayers of protein,” said PNNL microscopist James Evans. “Just being able to see any diffraction is brand new.”Evans co-led the team of two dozen scientists with LLNL physicist Matthias Frank. The bright, fast X-rays were produced at the Linac Coherent Light Source at SLAC National Accelerator Laboratory in Menlo Park, Calif., the newest of DOE’s major X-ray light source facilities at the national laboratories. LCLS, currently the world’s most powerful X-ray laser, is an X-ray free-electron laser. It produces beams millions of times brighter than earlier X-ray light sources.Coming in at around 8 angstrom resolution (which can make out items a thousand times smaller than the width of a hair), the proteins appear slightly blurry but match the expected view based on previous research. Evans said this level of clarity would allow researchers, in some cases, to see how proteins change their shape as they interact with other proteins or molecules in their environment.To get a clearer view of protein monolayers using XFEL, the team will need to improve the resolution to 1 to 3 angstroms, as well as take images of the proteins at different angles, efforts that are currently underway.Not Your Family’s CrystalResearchers have been using X-ray crystallography for more than 60 years to determine the shape and form of proteins that form the widgets and gears of a living organism’s cells. The conventional method requires, however, that proteins stack into a large crystal, similar to how oranges stack in a crate. …

Read more

Proteins snap those wrinkly fingers back into shape: Physicists model skin from wet to dry

You know how your fingers wrinkle up in the bath? The outer layer of your skin absorbs water and swells up, forming ridges — but quickly returns to its old state when dry. Two physicists, Professor Roland Roth of Tbingen University and Dr. Myfanwy Evans at Erlangen University have shown just why skin has this remarkable ability. Their conclusions were published recently in the journal Physical Review Letters.The swelling and absorption of water occur in the outermost skin layer, which is made of dead cells that are stacked in layers like bricks. These cells are filled with a network of filaments made of the protein keratin. These keratin strands interlock to form a three-dimensional lattice — which can increase its volume by five times when the strands stretch out.Evans and Roth have shown how the structure could help skin cells swell and shrink. They developed a model describing how the system’s energy varies as the network’s spacing changes. The researchers first calculated the filaments’ willingness to absorb water and found that this energy decreases, meaning that the structure is inclined to expand and absorb water.But they thought some other force must act to reverse the system’s expansion, since the process reverses easily in real cells. Inspired by previous filament elasticity measurements, they realized that the tension in a stretched filament could provide the counteracting force. …

Read more

Split decision: Stem cell signal linked with cancer growth

Researchers at the University of California, San Diego School of Medicine have identified a protein critical to hematopoietic stem cell function and blood formation. The finding has potential as a new target for treating leukemia because cancer stem cells rely upon the same protein to regulate and sustain their growth.Hematopoietic stem cells give rise to all other blood cells. Writing in the February 2, 2014 advance online issue of Nature Genetics, principal investigator Tannishtha Reya, PhD, professor in the Department of Pharmacology, and colleagues found that a protein called Lis1 fundamentally regulates asymmetric division of hematopoietic stem cells, assuring that the stem cells correctly differentiate to provide an adequate, sustained supply of new blood cells.Asymmetric division occurs when a stem cell divides into two daughter cells of unequal inheritance: One daughter differentiates into a permanently specialized cell type while the other remains undifferentiated and capable of further divisions.”This process is very important for the proper generation of all the cells needed for the development and function of many normal tissues,” said Reya. When cells divide, Lis1 controls orientation of the mitotic spindle, an apparatus of subcellular fibers that segregates chromosomes during cell division.”During division, the spindle is attached to a particular point on the cell membrane, which also determines the axis along which the cell will divide,” Reya said. “Because proteins are not evenly distributed throughout the cell, the axis of division, in turn, determines the types and amounts of proteins that get distributed to each daughter cell. By analogy, imagine the difference between cutting Earth along the equator versus halving it longitudinally. In each case, the countries that wind up in the two halves are different.”When researchers deleted Lis1 from mouse hematopoietic stem cells, differentiation was radically altered. Asymmetric division increased and accelerated differentiation, resulting in an oversupply of specialized cells and an ever-diminishing reserve of undifferentiated stem cells, which eventually resulted in a bloodless mouse.”What we found was that a large part of the defect in blood formation was due to a failure of stem cells to expand,” said Reya. “Instead of undergoing symmetric divisions to generate two stem cell daughters, they predominantly underwent asymmetric division to generate more specialized cells. As a result, the mice were unable to generate enough stem cells to sustain blood cell production.”The scientists next looked at how cancer stem cells in mice behaved when the Lis1 signaling pathway was blocked, discovering that they too lost the ability to renew and propagate. …

Read more

Fruit flies reveal normal function of gene mutated in spinocerebellar ataxia type 7

Disruptive clumps of mutated protein are often blamed for clogging cells and interfering with brain function in patients with the neurodegenerative diseases known as spinocerebellar ataxias. But a new study in fruit flies suggests that for at least one of these diseases, the defective proteins may not need to form clumps to do harm.The study, published February 1, 2014, in the journal Genes and Development, focuses on ataxin-7, the gene that is mutated in patients with spinocerebellar ataxia type 7 (SCA-7). Researchers led by investigators Jerry Workman, Ph.D. and Susan Abmayr, Ph.D. at the Stowers Institute for Medical Research found that fruit flies that lack Ataxin-7 experience neurodegeneration in the brain and the eye — paralleling the effects of the human disease. “The assumption has been that the disease is caused by the aggregated proteins,” Workman says. “But in the mutated fly, there’s no aggregated protein. There’s no soluble protein. It’s not there at all. The lack of Ataxin-7 causes neurodegeneration in the fruit fly.”Workman and Abmayr did not set out to study Ataxin-7. …

Read more

CONTENT REMOVED

by Dan StoriesA few years ago I was in a dead end job and I was looking for a change.I set out to search, network, and if I had to, bribe (I was desperate..) my way into a new situation. I struck gold when I had coffee with a guy named Jim Grafas.After one or two more of these caffeine rendezvous, things were looking up. It seemed I had a new job and a new friend. Little did I know I was about to witness him go through one of the most incredible transformations I’ve ever seen.After a turning point moment Jim decided to change his life for the better and as a result he’s lost 88 pounds (40 kgs) and most importantly, kept …

Read more

Model plant misled scientists about multicellular growth

Oct. 22, 2013 — Scientists have misunderstood one of the most fundamental processes in the life of plants because they have been looking at the wrong flower, according to University of Leeds researchers.Arabidopsis thaliana — also known as thale cress or mouse-ear cress — grows abundantly in cracks in pavements all over Europe and Asia, but the small white flower leads a second life as the lab rat of the plant world.It has become the dominant “model plant” in genetics research because of its simple genetics and ease of use in a research environment. Thousands of trays of the humble weed are cultivated in laboratories across the world, but it turns out they may actually contain a rather oddball plant.A study by researchers at the University of Leeds found that Arabidopsis thaliana was exceptional in not having a “censorship” protein called SMG1.SMG1 was known to play a vital role in the growth of animals as multicellular organisms, but scientists thought that plants built their complex life fundamentally differently. That conclusion, it turns out, was built on a dummy sold by Arabidopsis thaliana.Professor Brendan Davies from the University of Leeds’ School of Biology, who led the study, said: “Everybody thought that this protein was only in animals. They thought that because, basically, most of the world studies one plant: Arabidopsis thaliana.”Gene expression — the process by which the information from a genome is converted into the differentiated cells that make up complex life — relies on processes that turn genes on, when their genetic messages are required, and off when they are not.”Switching genes on and off is really what life is about. If you can’t do that, you can’t have life,” said Professor Davies. “There are various ways this is done, but one way in more complex life such as animals and plants is through a sort of ‘censorship’ process. The system looks at the messages that come out of the nucleus and effectively makes a judgement on them. It says ‘I am going to destroy that message now’ and intervenes to destroy it before it takes effect.”Scientists know that this “censorship” process — called Nonsense Mediated mRNA Decay (NMD) — is used by both plants and animals, but thought the two types of organism did it in different ways.Because Arabidopsis thaliana does not have SMG1, which plays a key role in triggering the censorship system in animals, scientists had concluded that SMG1 was not present in any plant.However, the Leeds researchers discovered that the plant that has established itself as the standard reference plant for all of biology is in fact an anomaly.”We have found that SMG1 is in every plant for which we have the genome apart from Arabidopsis and we have established that it is being used in NMD. Rather than being just in animals, we are suggesting that the last common ancestor of animals and plants had SMG1,” Professor Davies said.The study also found SMG1 in Arabidopsis lyrata, a close relative of Arabidopsis thaliana, which suggests that the missing protein has been lost relatively recently in evolutionary time, perhaps in the last 5-10 million years.The next key question for researchers is to explain how organisms without SMG1, such has funghi and Arabiposis thaliana, work without the protein.As for Arabidopsis thaliana, it may not have met its Waterloo just yet. …

Read more

Two genetic wrongs make a biochemical right

Oct. 20, 2013 — In a biological quirk that promises to provide researchers with a new approach for studying and potentially treating Fragile X syndrome, scientists at the University of Massachusetts Medical School (UMMS) have shown that knocking out a gene important for messenger RNA (mRNA) translation in neurons restores memory deficits and reduces behavioral symptoms in a mouse model of a prevalent human neurological disease. These results, published today in Nature Medicine, suggest that the prime cause of the Fragile X syndrome may be a translational imbalance that results in elevated protein production in the brain. Restoration of this balance may be necessary for normal neurological function.”Biology works in strange ways,” said Joel Richter, PhD, professor of molecular medicine at UMMS and senior author on the study. “We corrected one genetic mutation with another, which in effect showed that two wrongs make a right. Mutations in each gene result in impaired brain function, but in our studies, we found that mutations in both genes result in normal brain function. This sounds counter-intuitive, but in this case that seems to be what has happened.”Fragile X syndrome, the most common form of inherited mental retardation and the most frequent single-gene cause of autism, is a genetic condition resulting from a CGG repeat expansion in the DNA sequence of the Fragile X (Fmr1) gene required for normal neurological development. People with Fragile X suffer from intellectual disability as well as behavioral and learning challenges. Depending on the length of the CGG repeat, intellectual disabilities can range from mild to severe.While scientists have identified the genetic mutation that causes Fragile X, on a molecular level they still don’t know much about how the disease works or what precisely goes wrong in the brain as a result. What is known is that the Fmr1 gene codes for the Fragile X protein (FMRP). …

Read more

Blood stem cells age at the unexpected flip of a molecular switch

Oct. 20, 2013 — Scientists report in Nature they have found a novel and unexpected molecular switch that could become a key to slowing some of the ravages of getting older as it prompts blood stem cells to age.The study is expected to help in the search for therapeutic strategies to slow or reverse the aging process, and possibly rejuvenate these critically important stem cells (called hematopoietic stem cells, or HSCs), said scientists from Cincinnati Children’s Hospital Medical Center and the University of Ulm in Germany who conducted study.Published online Oct. 20, the study builds on earlier research from the same scientific team, who in 2012 reported they could make aging HSCs from laboratory mice functionally younger.Properly functioning HSCs — which form in the bone marrow — are vital to the ongoing production of different types of blood cells that allow the immune system to fight infections. The cells are also important for the regeneration of other important cells in the body.”Although there is a large amount of data showing that blood stem cell function declines during aging, the molecular processes that cause this remain largely unknown. This prevents rational approaches to attenuate stem cell aging,” said Hartmut Geiger, PhD, senior investigator and a scientist at Cincinnati Children’s and the University of Ulm. “This study puts us significantly closer to that goal through novel findings that show a distinct switch in a molecular pathway is very critical to the aging process.”The pathway is called the Wnt signaling pathway, a very important part of basic cell biology that regulates communications and interactions between cells in animals and people. Disruptions in the pathway have been linked to problems in tissue generation, development and a variety of diseases.Analyzing mouse models and HSCs in laboratory cultures, the scientists observed in aging cells that a normal pattern of Wnt signaling (referred to in science as canonical) switched over to an atypical mode of activity (called non-canonical). They also noticed that the shift from canonical to non-canonical signaling was triggered by a dramatic increase in the expression of a protein in aged HSCs called Wnt5a.When the researchers decided to test this observation by intentionally increasing the expression of Wnt5 in young HSCs, the cells began to exhibit aging characteristics.Interestingly, the dramatic increase of Wnt5a in aged HSCs activated another protein called Cdc42, which turned out to be critical to stem cell aging. Cdc42 is the same protein the scientists targeted in their 2012 study. In that study, the authors showed that pharmacologically inhibiting Cdc42 reversed the aging process and rejuvenated HSCs to be functionally younger.The researchers decided that for the current study, they would conduct experiments to see how blocking Wnt5a would affect HSC aging. …

Read more

CONTENT REMOVED

Banana bread is a classic and a great way to use over-ripe bananas.However, most banana bread recipes call for white flour, a fair amount of sugar and lack much nutrition other than ALL the carbs!But, banana bread is delicious, so what’s a girl or guy to do when they have brown banana’s and a hankering for delicious banana bread?THIS!Instead of a traditional recipe, why not make this delicious, protein packed, whole wheat version of the bread that’s really a dessert staple.Here’s What You’ll Need(For Bread)1 1/2 scoops chocolate protein powder 1/2 cup whole wheat flour 1 teaspoon baking soda 1/2 teaspoon cinnamon 2 ripe bananas, mashed 2 egg whites 2 tbsp vanilla greek yogurt 1/3 cup oats Optional: 1/3 cup chocolate chips (if you want it really chocolatey – I …

Read more

Finding blood clots before they wreak havoc

Oct. 16, 2013 — Life-threatening blood clots can form in anyone who sits on a plane for a long time, is confined to bed while recovering from surgery, or takes certain medications.There is no fast and easy way to diagnose these clots, which often remain undetected until they break free and cause a stroke or heart attack. However, new technology from MIT may soon change that: A team of engineers has developed a way to detect blood clots using a simple urine test.The noninvasive diagnostic, described in a recent issue of the journal ACS Nano, relies on nanoparticles that detect the presence of thrombin, a key blood-clotting factor.Such a system could be used to monitor patients who are at high risk for blood clots, says Sangeeta Bhatia, senior author of the paper and the John and Dorothy Wilson Professor of Biochemistry.”Some patients are at more risk for clotting, but existing blood tests are not consistently able to detect the formation of new clots,” says Bhatia, who is also a senior associate member of the Broad Institute and a member of MIT’s Koch Institute for Integrative Cancer Research and Institute for Medical Engineering and Science (IMES).Lead authors of the paper are Kevin Lin, a graduate student in chemical engineering, and Gabriel Kwong, a postdoc in IMES. Other authors are Andrew Warren, a graduate student in Health Sciences and Technology (HST), and former HST postdoc David Wood.Sensing thrombinBlood clotting is produced by a complex cascade of protein interactions, culminating in the formation of fibrin, a fibrous protein that seals wounds. The last step of this process — the conversion of fibrinogen to fibrin — is controlled by an enzyme called thrombin.Current tests for blood clotting are very indirect, Bhatia says. One, known as the D-dimer test, looks for the presence of fibrin byproducts, which indicates that a clot is being broken down, but will not detect its initial formation.Bhatia and her colleagues developed their new test based on a technology they first reported last year for early detection of colorectal cancer. “We realized the same exact technology would work for blood clots,” she says. “So we took the test we had developed before, which is an injectable nanoparticle, and made it a thrombin sensor.”The system consists of iron oxide nanoparticles, which the Food and Drug Administration has approved for human use, coated with peptides (short proteins) that are specialized to interact with thrombin. After being injected into mice, the nanoparticles travel throughout the body. When the particles encounter thrombin, the thrombin cleaves the peptides at a specific location, releasing fragments that are then excreted in the animals’ urine.Once the urine is collected, the protein fragments can be identified by treating the sample with antibodies specific to peptide tags included in the fragments. …

Read more

To live and learn: Making memories has to be a speedy business

Oct. 15, 2013 — The brain is plastic — adapting to the hundreds of experiences in our daily lives by reorganizing pathways and making new connections between nerve cells. This plasticity requires that memories of new information and experiences are formed fast. So fast that the body has a special mechanism, unique to nerve cells, that enables memories to be made rapidly. In a new study from The Montreal Neurological Institute and Hospital, The Neuro, McGill University with colleagues at the Université de Montréal, researchers have discovered that nerve cells have a special ‘pre-assembly’ technique to expedite the manufacture of proteins at nerve cell connections (synapses), enabling the brain to rapidly form memories and be plastic.Share This:Making a memory requires the production of proteins at synapses. These proteins then change the strength of the connection or pathway. In nerve cells the production process for memory proteins is already pre-assembled at the synapse but stalled just before completion, awaiting the proper signals to finish, thereby speeding up the entire process. When it comes time to making the memory, the process is switched on and the protein is made in a flash. The mechanism is analogous to a pre-fab home, or pre-made pancake batter that is assembled in advance and then quickly completed in the correct location at the correct time.”It’s not only important to make proteins in the right place but, it’s also important not to make the protein when it’s the wrong time,” says Dr. Wayne Sossin, neuroscientist at The Neuro and senior investigator on the paper. …

Read more

A bacterium reveals the crucible of its metallurgical activity

Oct. 14, 2013 — Magnetotactic bacteria have the ability to synthesize nanocrystals of magnetite (Fe3O4) enabling them to align themselves with the terrestrial magnetic field in order to find the position in the water column that is most favorable to their survival. The alignment of the nanomagnets is similar to that of a compass needle. The magnetite crystal synthesis process is a complex one, and it is little understood at the present time. Magnetite is a compound of oxygen and iron in a mixture of two different oxidation states [Fe(II)Fe(III)2O4]. In this study, the researchers have described the mechanism by which the bacterium produces these two states, one of which, Fe(III), is essentially insoluble.Share This:The determination of the structure of the protein MamP has shown for the first time that a section of this protein possesses an original folding structure known as a magnetochrome. This structure is only found in magnetotactic bacteria. The structure has a crucible-like shape capable of containing iron. Additional experiments have shown that MamP has the ability to oxidize iron from the Fe(II) state to the Fe(III) state, and to stabilize the latter in its crucible. Mutagenesis studies and the phenotyping of magnetotactic bacteria variants have confirmed the physiological importance of this crucible.Finally, a number of in vitro experiments have shown that MamP is capable of producing a magnetite precursor when incubated in the presence of Fe(II) alone, proving that the Fe (III) results from the activity of this protein.This fundamental study reveals part of the process whereby iron is biomineralized and nanomagnets are synthesized in magnetotactic bacteria. …

Read more

Genetically modified tobacco plants are viable for producing biofuels

Oct. 14, 2013 — In her PhD thesis Ruth Sanz-Barrio, an agricultural engineer of the NUP/UPNA-Public University of Navarre and researcher at the Institute of Biotechnology (mixed centre of the CSIC-Spanish National Research Council, Public University of Navarre and the Government of Navarre), has demonstrated, for the first time, the viability of using specific tobacco proteins (known as thioredoxins) as biotechnological tools in plants. Specifically, she has managed to increase the amount of starch produced in the tobacco leaves by 700% and fermentable sugars by 500%. “We believe that these genetically modified plants,” she explained, “could be a good alternative to food crops for producing biofuels, and could provide an outlet for the tobacco-producing areas in our country that see their future in jeopardy owing to the discontinuing of European grants for this crop.”Thioredoxins (Trxs) are small proteins present in most living organisms. In the course of her research Ruth Sanz demonstrated the capacity of the thioredoxins f and m in tobacco as biotechnological tools not only to increase the starch content in the plant but also to increase the production of proteins like human albumin. “For some time Trxs have been known to have a regulating function in living organisms, but in the thesis we have shown that they can also act by helping other proteins to fold and structure themselves so that they become functional.”Human albumin is the most widely used intravenous protein in the world for therapeutic purposes. It is used to stabilize blood volume and prevent the risk of infarction, and its application in operating theatres is almost a daily occurrence. It is also used in burns, surgical operations, haemorrhages, or when the patient is undernourished or dehydrated, and in the case of chronic infections and renal or hepatic diseases.Although commercial albumin is extracted from blood, the lack of a sufficient volume in reserve has prompted many researchers to seek new formulas for obtaining this protein on a large scale economically and safely. “We have come up with an easier, cheaper procedure for producing it in the tobacco plant and extracting it. By fusing the genes encoding the Trxs f or m, we increased the amount of recombinant protein (the albumin, in this case). …

Read more

Utilizzando il sito, accetti l'utilizzo dei cookie da parte nostra. maggiori informazioni

The cookie settings on this website are set to "allow cookies" to give you the best browsing experience possible. If you continue to use this website without changing your cookie settings or you click "Accept" below then you are consenting to this.

Close