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  • richardmitnick 9:09 pm on September 21, 2017 Permalink | Reply
    Tags: , Diamond Light Source, Medicine, Rift Valley fever phlebovirus (RVFV), Significant step made towards understanding Rift Valley Fever virus, ,   

    From University of St Andrews: “Significant step made towards understanding Rift Valley Fever virus” 

    U St Andrews bloc

    University of St Andrews

    21 September 2017
    Fiona MacLeod
    01334 462108/07714 140 559
    fm43@st-andrews.ac.uk

    1
    The NSs protein of RVFV forms characteristic filaments (green) in the nuclei of infected cells (red): a three-dimensional structure of a fibrillar assembly of NSs, determined by Barski et al using X-ray crystallography (green) is shown on top of an image of three infected cells. Image credit: Ben Brennan and Uli Schwarz-Linek.

    Researchers at the Universities of St Andrews and Glasgow have made a significant step forward in tackling a viral disease which causes frequent epidemics in Africa and could spread to Europe due to global warming.

    Dr Michal Barski and Dr Uli Schwarz-Linek of the School of Biology at the University of St Andrews, with colleagues at the University of Glasgow, have published a paper in online journal eLife revealing new information about a key molecule used by the virus to cause disease, which could help to eventually find a cure or a vaccine.

    Rift Valley fever phlebovirus (RVFV) is a virus affecting humans and livestock which is transmitted by mosquitos and contact with infected animals. RVFV is increasingly likely to cause widespread epidemics, and could potentially follow the pattern of Dengue virus or West Nile virus and spread to temperate regions, such as Europe or the USA, as global warming allows the mosquitos which carry the virus to extend their geographic range.

    Infection can cause severe disease, including haemorrhagic fever, and may lead to death. Historically, the virus was only found in central Africa but has spread to the Arabian Peninsula. There are no vaccines or treatments available for use in humans so if there is a serious outbreak of the virus it could become an epidemic and cause great economic loss and severe human disease.

    The research team combined two techniques, NMR spectroscopy and X-ray crystallography, carried out at Diamond Light Source, to study the atomic three-dimensional structure of NSs – a key molecule of the RVFV virus which assembles into large fibres inside infected cells.

    Diamond Light Source, located at the Harwell Science and Innovation Campus in Oxfordshire U.K.

    The virus relies on NSs to cause disease but the mechanism behind this process, and the formation of the fibres, have not been fully understood. The structure of this molecule revealed that only the central part, or core domain, of the protein is needed for the fibres to form. Further experiments identified how NSs molecules come together to build the fibres inside the infected cells.

    Dr Schwarz-Linek said: “The structural insights we generated will help to unravel the complexity of Rift Valley fever. It will pave the way for research on Rift Valley fever phlebovirus and many other related viruses that have the ability to infect animals and humans.”

    Dr Barski added: “With this research we have opened up a new avenue for understanding Rift Valley fever virus and hopefully also for developing therapy targeted at this virus. The recent, sudden epidemics of Ebola virus and Zika virus have highlighted the need to understand dangerous tropical viral diseases which could quickly spread to far away places. Rift Valley fever is on that very short list of viruses which might cause large epidemics next.”

    These findings mark an important step towards understanding how the NSs protein helps RVFV to cause disease in humans and livestock. In the future, this work may aid the development of much needed drugs and vaccines against RVFV.

    Earlier this year the World Health Organization ranked RVFV among the ten most dangerous pathogens most likely to cause wide epidemics in the near future, requiring urgent attention.

    See the full article here .

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    U St Andrews campus

    St Andrews is made up from a variety of institutions, including three constituent colleges (United College, St Mary’s College, and St Leonard’s College) and 18 academic schools organised into four faculties. The university occupies historic and modern buildings located throughout the town. The academic year is divided into two terms, Martinmas and Candlemas. In term time, over one-third of the town’s population is either a staff member or student of the university. The student body is notably diverse: over 120 nationalities are represented with over 45% of its intake from countries outside the UK; about one-eighth of the students are from the rest of the EU and the remaining third are from overseas — 15% from North America alone. The university’s sport teams compete in BUCS competitions, and the student body is known for preserving ancient traditions such as Raisin Weekend, May Dip, and the wearing of distinctive academic dress.

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  • richardmitnick 5:30 pm on September 20, 2017 Permalink | Reply
    Tags: , Chagas disease, Kissing bug, Medicine,   

    From UC Riverside: “Scientists Identify New Hosts for Chagas Disease Vectors” 

    UC Riverside bloc

    UC Riverside

    9.20.17
    Sarah Nightingale
    Tel: (951) 827-4580
    E-mail: sarah.nightingale@ucr.edu
    Twitter: @snightingale

    1
    A UCR study is the first to show that tayras, long, slender animals that look similar to weasels, are hosts for parasite-spreading kissing bugs. CC BY 1.0

    Solitary weasel-like animals called tayra might look pretty harmless, but some may actually be incubators for a parasite that causes Chagas disease, a chronic, debilitating condition that is spread by insects called kissing bugs and affects more than 8 million people worldwide. In a study published Monday in the journal PeerJ, researchers from the University of California, Riverside have identified several new hosts for parasite-spreading kissing bug species, including tayras, new world monkeys, sloths, porcupines, and coatis—which are the South American cousins of racoons.

    The research is important because, despite its prevalence, relatively little is known about the transmission of Chagas disease, a deadly, incurable condition that is most common in Latin America.

    “There are 152 species of kissing bug, but we don’t know much about most of them, including the animals they feed on that can act as reservoirs for the parasite. Overall, the existing data is piecemeal, scattered, and biased toward a handful of heavily studied and well-documented species, while little data exists for insects that are found in very secluded habitats,” said Christiane Weirauch, a professor of entomology in UCR’s College of Natural and Agricultural Sciences.

    The UCR study not only increases our knowledge of Chagas disease transmission in rural environments, but also provides the most comprehensive review of animal hosts of the kissing bugs that spread Chagas disease. The research, led by Anna Georgieva, an undergraduate majoring in biology, and Eric Gordon, a graduate student researcher in Weirauch’s lab, will support efforts to control the disease, particularly in poor, rural populations in South America.

    2
    Kissing bugs, like the specimen shown in this image, may be infected with Trypanosoma cruzi, the parasite that causes Chagas disease. No image credit.

    Chagas disease is caused by the parasite Trypanosoma cruzi, which is transmitted to animals and humans by members of the assassin bug subfamily called kissing bugs that feed on blood and are named for their tendency to bite people around the mouth. According to the Centers for Disease Control and Prevention, kissing bugs become infected with T. cruzi by biting an infected animal or person and, once infected, they pass T. cruzi parasites in their feces. When they bite a person and ingest blood, they defecate on them. A person can become infected if bug feces enters their body through mucous membranes or skin lesions caused by the bite wound or scratching. Research also suggests that animals can become infected by eating other animals that harbor the parasite.

    Although Chagas disease is common in rural areas, identifying new hosts among tree-dwelling, and sometimes nocturnal animals is a challenge. To sidestep this problem, the researchers identified new hosts by studying their blood—which they isolated straight from the guts of kissing bugs. The sample included 64 kissing bug samples collected from Central and South America between 2005 and 2015 that were preserved in ethanol.

    “Our modern approach using DNA allowed us to determine this wide variety of animal hosts without a bias towards ones that are already known, unlike some older detection methods” Georgieva said.

    DNA analyses of the ingested blood revealed host associations for 24 of the samples. Among the newly identified hosts was the tayra, which has never before been named as a host for kissing bugs.

    Gordon said the findings will help public health officials develop new methods to control Chagas disease.

    “Education and pesticide application around homes has helped reduce the impact of kissing bugs associated with homes and domestic animals, but now more and more cases of Chagas disease are driven by species most often associated with more rural hosts,” Gordon said.

    “One important consideration in controlling Chagas disease in wild animals is the possibility of bioaccumulation of the parasite in certain carnivores near the top of the food chain. If kissing bugs also feed on these carnivores, as has occurred for the tayra in our study, they are likely to be one of the important links in the transmission chain of the disease in the wild. If a vaccine becomes available one day in the future, they are good candidates to target for immunization to halt the natural spread of the parasite and potentially help to eradicate the pathogen.”

    See the full article here .

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    UC Riverside Campus

    The University of California, Riverside is one of 10 universities within the prestigious University of California system, and the only UC located in Inland Southern California.

    Widely recognized as one of the most ethnically diverse research universities in the nation, UCR’s current enrollment is more than 21,000 students, with a goal of 25,000 students by 2020. The campus is in the midst of a tremendous growth spurt with new and remodeled facilities coming on-line on a regular basis.

    We are located approximately 50 miles east of downtown Los Angeles. UCR is also within easy driving distance of dozens of major cultural and recreational sites, as well as desert, mountain and coastal destinations.

     
  • richardmitnick 1:29 pm on September 14, 2017 Permalink | Reply
    Tags: , cryo-EM at Yale, Medicine, , Yale Medicine   

    From Yale: “New imaging facility is a ‘revolution'” 

    Yale University bloc

    Yale University

    Cryo-electron microscope at West Campus brings unprecedented capabilities to Yale, spurring science and faculty recruitment.

    1
    School of Medicine faculty who welcomed the new device at its June dedication include (l-r) Jorge Galán, Thomas Pollard, Charles Sindelar, Scott Strobel, Yong Xiong, and Frederick Sigworth. (Photo by Harold Shapiro)

    1
    cryo-EM at Yale

    Microscopy at Yale has just received a major upgrade. Structural biologists at the School of Medicine and scientists from across the university have begun obtaining three-dimensional images at near-atomic resolutions from what Jorge E. Galán, Ph.D., D.V.M., chair and Lucille P. Markey Professor of Microbial Pathogenesis and professor of cell biology, calls “the mother of all microscopes.” The Titan Krios cryoelectron microscope arrived at West Campus in January and was dedicated in June. Cryo-electron microscopy (cryo-EM) is high-resolution electron microscopy of cryogenically cooled specimens. The specimens are unstained, and rapidly frozen so they are embedded in vitreous ice.

    As multimillion-dollar investments in infrastructure go, bringing cryo-EM to Yale was a rapid process, according to Scott A. Strobel, Ph.D., Henry Ford II Professor of Molecular Biophysics and Biochemistry and professor of chemistry, deputy provost for teaching and learning, and vice president for West Campus planning and program development. “The West Campus had a space that was ideally suited for this instrument in terms of height, and in terms of being on bedrock,” Strobel says. While preparing that space for such a delicate installation was still a huge task, its physical configuration allowed the work to move more quickly than would have been possible elsewhere. Says Strobel, “From the time we decided to do it to the time it was in place was less than a year.”

    The new device allows investigators to see structures in ways they previously could not. Its resolution rivals that of X-ray crystallography, but where crystallography requires looking at specimens in isolation, severed from biological systems of which they are a part, cryo-EM permits examination of samples in ways that better illustrate their function. Previously, researchers could only estimate the structure and function of many systems they study. Now, for the first time, they actually are seeing them.

    School of Medicine faculty who welcomed the new device at its June dedication include (l-r) Jorge Galán, Thomas Pollard, Charles Sindelar, Scott Strobel, Yong Xiong, and Frederick Sigworth. (Photo by Harold Shapiro)
    New imaging facility is a “revolution”

    Cryo-electron microscope at West Campus brings unprecedented capabilities to Yale, spurring science and faculty recruitment

    Microscopy at Yale has just received a major upgrade. Structural biologists at the School of Medicine and scientists from across the university have begun obtaining three-dimensional images at near-atomic resolutions from what Jorge E. Galán, Ph.D., D.V.M., chair and Lucille P. Markey Professor of Microbial Pathogenesis and professor of cell biology, calls “the mother of all microscopes.” The Titan Krios cryoelectron microscope arrived at West Campus in January and was dedicated in June. Cryo-electron microscopy (cryo-EM) is high-resolution electron microscopy of cryogenically cooled specimens. The specimens are unstained, and rapidly frozen so they are embedded in vitreous ice.

    As multimillion-dollar investments in infrastructure go, bringing cryo-EM to Yale was a rapid process, according to Scott A. Strobel, Ph.D., Henry Ford II Professor of Molecular Biophysics and Biochemistry and professor of chemistry, deputy provost for teaching and learning, and vice president for West Campus planning and program development. “The West Campus had a space that was ideally suited for this instrument in terms of height, and in terms of being on bedrock,” Strobel says. While preparing that space for such a delicate installation was still a huge task, its physical configuration allowed the work to move more quickly than would have been possible elsewhere. Says Strobel, “From the time we decided to do it to the time it was in place was less than a year.”

    The new device allows investigators to see structures in ways they previously could not. Its resolution rivals that of X-ray crystallography, but where crystallography requires looking at specimens in isolation, severed from biological systems of which they are a part, cryo-EM permits examination of samples in ways that better illustrate their function. Previously, researchers could only estimate the structure and function of many systems they study. Now, for the first time, they actually are seeing them.

    Images with 3-angstrom (3Å) resolution are now readily available to investigators such as Frederick J. Sigworth, Ph.D., professor of cellular and molecular physiology and of molecular biophysics and biochemistry. “The difference between 5Å or 8Å [the best resolutions attainable with Yale’s prior generation of equipment] and 3Å is huge,” says Sigworth, who hopes his work on ion channel function within cells can form the basis for therapies for muscular diseases. “It’s the difference between being able to pretty well place where the atoms are in a protein versus just saying, ‘Well, roughly we’ve got this kind of shape and this kind of structure.’ If you can place all the atoms, then you can begin to think, ‘OK, how is a drug going to bind to this, or how does a hormone interact with this binding pocket to activate this receptor?’ ”

    Yong Xiong, Ph.D., associate professor of molecular biophysics and biochemistry, says what investigators in Yale laboratories can see is “a revolution for us” and “will change how we do things.” Xiong’s primary work is deciphering the intricate dance between antiviral proteins in the immune system and viruses such as HIV. “We want to see how the virus infects the host, how the host tries to suppress the infection, and how the virus then develops another mechanism to escape the host’s suppression.”

    He now will take advantage of the new microscope’s ability to perform cryo-electron tomography (cryo-ET), a method still in its relative infancy whose capabilities include creating high-resolution 3-D images from an unprecedented array of angles. Xiong predicts that seeing clear images of specimens in their native environment, within cells, will be a major advance. He says the standard method prior to cryo-ET has been, “We take [the specimen] out, apply an input, look at the output, and guess what it is doing. If we can use cryo-electron tomography to directly see it, that power is unprecedented.” Xiong says cryo-ET may be the sort of advance that comes along only once in a few decades.

    In the lab of Charles V. Sindelar, Ph.D., assistant professor of molecular biophysics and biochemistry, one object of particular interest is the flagellum—a propeller-like molecular machine that transports pathogens through human tissue, causing diseases that include syphilis and Lyme disease. If flagella can be disabled, Sindelar explains, pathogens cannot move, so they cannot penetrate the body. “Flagella images in the past were uninterpretable,” Sindelar says. “We couldn’t translate them into a 3-D shape because they lie down in a certain way inside the microscope.” Those days, he says, are over, thanks to cryo-ET. “What we have been doing is basically tilting the stage [of the new instrument] back and forth and getting beautiful images like nothing we’ve ever seen. We could never have taken that to atomic resolution with anything except the device we have here.”

    Galán proclaims that cryo-ET “is truly, truly the future.” His own work focuses on molecular machines that directly inject bacterial proteins into mammalian cells. He hopes to find ways by which cells can thwart that interaction—an approach that could be superior to attacking the bacteria, which increasingly resist antibiotics. Galán says tomography may be the key to success.

    It also is key to bringing even more of the world’s top scientists to Yale. In September, Jun Liu, Ph.D., a renowned expert in tomography, will come to the School of Medicine faculty from the University of Texas Medical School at Houston, joining Galán’s Department of Microbial Pathogenesis. Says Galán of Liu, who has collaborated with Yale scientists in the past, “We’re bringing in someone who will be able to take us into the big leagues in cryo-electron tomography.”

    Recruitment efforts by other departments are also well underway, spurred by the arrival of the cryo-EM. Strobel says, “We are going to be able to bring new faculty to Yale as a result of this instrument.”

    As it draws top talent to Yale, the new device may also help democratize structural biology research. So intricate is the process of preparing purified samples for crystallography that, Sigworth recalls, “before the mid-1990s anyone who solved a membrane protein structure by X-ray crystallography got a Nobel Prize. It was that hard.” Preparing samples for comparable analysis by cryo-EM is far simpler. “With an automated instrument like this, solving an atomic structure is becoming so easy it can be part of a grad student’s thesis,” Sigworth says. “In fact, it could be a side project.”

    “What technology is allowing us to do now is completely breathtaking,” adds Galán. “We can see microbes in action. We can see them in excruciating detail as allowed by instruments like the Titan Krios. And I think that is in essence a fantastic strength of Yale as a university, and for the medical school as well.”

    See the full article here .

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    Yale University Campus

    Yale University comprises three major academic components: Yale College (the undergraduate program), the Graduate School of Arts and Sciences, and the professional schools. In addition, Yale encompasses a wide array of centers and programs, libraries, museums, and administrative support offices. Approximately 11,250 students attend Yale.

     
  • richardmitnick 7:39 am on September 14, 2017 Permalink | Reply
    Tags: , Crustacean diseases, Histopathology, Medicine, , Shrimp studies, , Zoology   

    From U Arizona: “Global Shrimp Industry Depends on UA” 

    U Arizona bloc

    University of Arizona

    Sept. 11, 2017
    Susan McGinley
    UA College of Agriculture and Life Sciences

    1
    Shrimp at the wet lab (live animal) facility at the West Campus Agricultural Center (Photo: Bob Demers/UANews)

    The Aquaculture Pathology Laboratory tests shrimp samples, identifies diseases and certifies disease-free stock to help the nearly $40 billion farmed shrimp industry provide a safe food supply.

    A world-renowned laboratory in Tucson has a quiet presence at the University of Arizona, but within the global farmed shrimp and aquaculture industry it exerts a tremendous influence.

    The Aquaculture Pathology Laboratory, housed within the College of Agriculture and Life Sciences’ School of Animal and Comparative Biomedical Sciences, works with commercial shrimp farming enterprises, research institutions and nongovernmental organizations, or NGOs, from across the world to diagnose infectious diseases of penaeid shrimp and other crustaceans in samples delivered to the UA, certify pathogen-free stock, test feed ingredients, conduct research and train shrimp disease specialists.

    _________________________________________________________________________

    Extra Info

    Facts About the Shrimp Industry

    About 75 percent of world shrimp production is Penaeus vannamei (Pacific white shrimp or king prawn).
    Total world shrimp production in 2014 was approximately 4 million metric tons.
    The shrimp industry has a projected annual growth rate of 4.2 percent.
    The top shrimp producers worldwide are China, India, Thailand, Vietnam, Indonesia and Ecuador.
    EMS (early mortality syndrome) disease was detected for the first time in the U.S. in Texas in July, with the research work carried out in the Aquaculture Pathology Laboratory at the UA: http://www.oie.int/wahis_2/public/wahid.php/Reviewreport/Review?page_refer=MapFullEventReport&reportid=24597.

    _________________________________________________________________________

    Clients pay for these services, which in turn help them maintain the biosecurity of their products and ultimately the health and profitability of their industry. For example, baby and adult stocker shrimp can’t be sold to large shrimp operations around the world — in the U.S., Mexico, South America, the Middle East and Asia — unless they are certified. The laboratory conducts certification testing and validation.

    The laboratory can do this because it is a reference laboratory, the only one in North America, certified for crustacean diseases by the Office International des Epizooties in Paris. It is also an approved laboratory of the U.S. Department of Agriculture Animal and Plant Health Inspection Service.

    “This lab has done a wonderful job of addressing the needs of the shrimp industry in terms of disease diagnosis and disease prevention worldwide,” said Arun K. Dhar, associate professor of shrimp and other crustacean aquaculture and director of the lab since January. He succeeded longtime professor and founding director Donald V. Lightner, who developed and guided the lab for more than 30 years as it became a facility recognized around the world.

    “We identify the pathogen, we get the specifics,” Dhar said. “When a disease emerges, we jump on it to determine the etiology (cause), the methods to detect it and the tools to prevent the spread of the disease. Then we tell that story to various audiences.”

    Wet Lab and Diagnostics Lab

    The UA laboratory includes a wet lab (live animal) facility at the West Campus Agricultural Center and a diagnostics lab of histology (tissue diagnostics) and molecular detection on the main campus.

    A staff of three in the center maintains tanks of specific pathogen-free (SPF) or specific pathogen-resistant quarantined stocks at the wet lab for companies and agencies, and they evaluate live shrimp samples from across the world to detect (or rule out) diseases so virulent that they can’t be tested anywhere near coastal waters. The risk of contamination to commercial shrimp beds would be too great.

    “Because of this, our lab is in the desert. We deal with the worst of the worst in emerging pathogens,” said senior research specialist Brenda Noble, who dips her boots in water when entering and exiting the quarantined areas. “Acute hepatopancreatic necrosis disease, also called EMS — early mortality syndrome — is big now, killing a lot of animals on farms in Asia and Latin America. EMS is bacterial and kills up to 100 percent in a day at the lab, although not on farms, where it is spread out.”

    White spot disease, or WSD, is another highly contagious and lethal viral disease. Shrimp diseases do not infect humans.

    The staff conducts challenge studies on animals (mainly crustaceans) brought in from all over the world to find family lines that are resistant to disease, and also product challenges on SPF animals to find out if ingredients in those products — probiotics, for example — enhance their survival. Two shrimp species form the bulk of the commercial farmed shrimp supply: Penaeus vannamei, Pacific white shrimp or king prawn, and Penaeus monodon, giant tiger prawn or Asian tiger shrimp.

    At the dry lab on campus, a team of seven tests tissue samples sent from the wet lab and from national and international companies and agencies. Most are from Hawaii, Florida and Latin America. Clients specify the tests they want: viral, bacterial, fungus, prokaryote or protozoa.

    In the histology lab, a team of two works on diagnosis via histopathology. Each sample is dissected into pieces, put into a cassette, processed overnight and embedded in wax blocks that cool and harden. The blocks are cut into thin sections, put on racks, cooked in a tissue oven to affix them and then stained. Each section is put into a slide folder to be read and diagnosed.

    These tests are conducted for regular surveillance of a company’s stock, or as a general health check on shrimp to make sure the shrimp population is safe.

    “Our department consists of different labs, but we are a team of lab technicians, scientists and specialists who help diagnose diseases and send results to clients in an ongoing relationship,” research specialist Jasmine Millabas said.

    In the PCR lab, extracts of shrimp feed are run in PCR (polymerase chain reaction) machines to note any presence of disease. Each report includes a picture of the PCR result as a proof of testing.

    “We have run samples from 461 clinical cases so far this year in this lab,” postdoctoral research associate Siddhartha Kanrar said.

    Shrimp Pathology Short Course

    Along with diagnostics, treatment and biosecurity, faculty and staff in the Aquaculture Pathology Laboratory teach an intensive one-week shrimp pathology short course plus several workshops annually, in Tucson and in various countries. The class is for professionals who conduct testing for companies and institutions dealing mainly with farm-raised shrimp.

    Dhar recently taught classes at the Bangladesh Fisheries Research Institute in Bangladesh and at Yangon University in Myanmar. He said shrimp is dubbed “white gold” in Bangladesh because it is the country’s third-largest export in revenue.

    In addition to methods for detecting and diagnosing diseases in farmed shrimp, the hands-on course takes participants through the steps of preparing tissue samples precisely to ensure accurate results when the samples are sent to the Aquaculture Pathology Laboratory. The participants learn about what to look for in cells in diseased animals and how to follow the proper procedures to get the detection correct. The West Campus experimental lab has inoculum for all Office International des Epizooties pathogens, kept in freezer at minus 80 degrees Celsius (minus 112 Fahrenheit) from diseased shrimp to use for testing the real thing in class.

    Nearly every shrimp pathologist in the world has taken the course. In July, the class included 19 participants from nine countries on four continents, mainly from commercial aquaculture businesses.

    While students prepared slides, senior research specialist Luis Fernando Aranguren Caro pointed out areas of slides projected on a screen that showed diseases or abnormalities, noting that “the degree of infection depends on the extent of the disease revealed.” Jessica Fox, director of veterinary services and biosecurity for Tru-Shrimp, a freshwater shrimp production facility in Minnesota, brought three employees to the UA who will prepare the histology samples that are sent to Arizona.

    “We wanted to learn more about the shrimp diseases to help us understand what to watch for, what screening measures we need to do and to help us develop other biosecurity protocols,” Fox said. “Our whole group understands more together. There’s quite a bit of hands-on here. We know what to look for and have done this before in-house, but it’s good to have experts checking your work.”

    See the full article here .

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    U Arizona campus

    The University of Arizona (UA) is a place without limits-where teaching, research, service and innovation merge to improve lives in Arizona and beyond. We aren’t afraid to ask big questions, and find even better answers.

    In 1885, establishing Arizona’s first university in the middle of the Sonoran Desert was a bold move. But our founders were fearless, and we have never lost that spirit. To this day, we’re revolutionizing the fields of space sciences, optics, biosciences, medicine, arts and humanities, business, technology transfer and many others. Since it was founded, the UA has grown to cover more than 380 acres in central Tucson, a rich breeding ground for discovery.

    Where else in the world can you find an astronomical observatory mirror lab under a football stadium? An entire ecosystem under a glass dome? Visit our campus, just once, and you’ll quickly understand why the UA is a university unlike any other.

     
  • richardmitnick 8:54 am on September 11, 2017 Permalink | Reply
    Tags: , , Medicine, ,   

    From Rutgers: Women in STEM – “Rutgers Neuroscientist Finds a Way to Track and Measure Female Autism, Asperger’s” 

    Rutgers University
    Rutgers University

    September 7, 2017
    Ken Branson

    1
    Objective electronic data, such as data generated by fMRI brain scans, are better tools for measuring and detecting autism in girls than subjective observation, Rutgers neuroscientist Elizabeth Torres says.

    A Rutgers University study found that tracking and measuring the involuntary head movements revealed in functional magnetic resonance imaging (fMRI) scans offers a new, more accurate way to detect autism in girls.

    Rutgers University-New Brunswick neuroscientist Elizabeth Torres said the traditional criteria used to diagnose autism are largely based on the observed behavior of children, and since boys in western society are expected to be active, deviations from that norm are easy to spot. Girls are socialized to be quieter, so autism is harder to observe. Perhaps partly due to these cultural biases, boys are diagnosed with autism five times as often as girls. “The criteria are male-driven, so we’re measuring females with a male ruler,” she said.

    In a paper published in Frontiers in Integrative Neuroscience, Torres and her co-authors report on what they found by matching data about involuntary head movements from fMRI scans to diagnoses of autism spectrum disorder. “When you go in an fMRI machine, they tell you to hold still,” she said. “But you can’t hold totally still; nobody can. The machine will pick up involuntary movements that the patient is unaware of and that an observer wouldn’t see with the naked eye.”

    Torres, associate professor of psychology in the School of Arts and Sciences, used data from the Autism Brain Imaging Data Exchange (ABIDE) databases, which contain raw information from brain scans collected from laboratories around the world – a guard against the cultural bias inherent in observation. The researchers examined the scans of 2,199 people, all of whom had been diagnosed with autism or Asperger’s syndrome, a relatively mild disorder on the autism spectrum. Three hundred nine of the scans were of females.

    Torres says the tools traditionally used to diagnose autism offer no definition of “normal” behavior, nor do they offer standardized scales that can be mapped to the kind of neurophysiological data that comes from fMRI scans. However, involuntary motions, like those measured by fMRI scans, may help clinicians more accurately determine whether and where a person belongs on the autism spectrum.

    This is the latest in a series of articles in which Torres has made use of electronic data, either obtained from fMRI scans or from wearable sensors, to study such conditions as autism and stroke.

    Torres’ co-authors are Sejal Mistry, a an undergraduate student when the research was done and now a Fulbright Scholar in India; and Caroline Whyatt and Carla Caballero, both post-doctoral researchers in Torres’ laboratory at Rutgers University-New Brunswick.

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    rutgers-campus

    Rutgers, The State University of New Jersey, is a leading national research university and the state’s preeminent, comprehensive public institution of higher education. Rutgers is dedicated to teaching that meets the highest standards of excellence; to conducting research that breaks new ground; and to providing services, solutions, and clinical care that help individuals and the local, national, and global communities where they live.

    Founded in 1766, Rutgers teaches across the full educational spectrum: preschool to precollege; undergraduate to graduate; postdoctoral fellowships to residencies; and continuing education for professional and personal advancement.

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    As a ’67 graduate of University college, second in my class, I am proud to be a member of

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  • richardmitnick 7:26 am on September 8, 2017 Permalink | Reply
    Tags: , , Human Cell Atlas hopes to unravel mysteries hidden in our genes, Medicine, Microsatellites   

    From Horizon: “Human Cell Atlas hopes to unravel mysteries hidden in our genes” 

    1

    Horizon

    06 September 2017
    Richard Gray

    1
    A process called droplet microfluidics isolates thousands of cells in microscopic water droplets allowing up-close analysis of genetic material. Image credit – Dr Linas Mazutis

    A major international project is attempting to create the first comprehensive three-dimensional map of all human cells which could end up revealing secrets about our health and how our bodies function.

    It is nearly 350 years since scientists first discovered that our bodies are made up of tiny building blocks known as cells. Today we still know very little about their nature, but if we did, we could better understand how our bodies work, how diseases afflict us and how we age.

    A global project called Human Cell Atlas is now attempting to create the first comprehensive three-dimensional map of the human body in order to unravel some of these mysteries.

    ‘It will hopefully have the same impact as when the human genome was sequenced,’ said Dr Linas Mazutis, a biochemist at Vilnius University in Lithuania. ‘A human cell atlas could set the stage to develop new technologies and provide new answers about the human body.’

    The project could also lead to better diagnosis and treatment of diseases, but taking a census of all human cells is no simple task – there are an estimated 40 trillion in each adult body.

    Dr Mazutis coordinates an EU-funded project called Cells-in-drops, which is aimed at developing some of the techniques needed to create this enormous map of human cells.

    Their technology allows thousands of individual cells to be rapidly isolated into microscopic water droplets around 100 micrometres across – about the same width as a human hair.

    Known as droplet microfluidics, this approach can be loaded with biochemical reagents that break open the cells, spilling their contents into the water they are encased in.

    This essentially turns each droplet into a microscopic test tube where the genetic material, or its other contents, can be analysed.

    ‘We are particularly looking at gene expression programs of single cells,’ said Dr Mazutis.

    This is important as not all genes, or DNA, in every cell in the human body are switched on – in some tissues certain genes are deactivated while others are amplified.

    DNA can also be read in different ways depending on the cell it is in, meaning different proteins can be produced from the same genetic code.

    To help unravel this complexity, Dr Mazutis co-developed a technique with colleagues at Harvard University that analyses another type of genetic material called ribonucleic acid (RNA).

    Barcoding

    RNA plays an important role in cells by helping to translate the DNA code into proteins the cell needs to grow or replicate. Analysing this can then reveal details about a cell’s activity and functions.

    The technique used by Dr Mazutis converts the RNA from a cell in one of the microdroplets back into DNA, but adds a unique barcode into the sequence of genes. The genetic material from all of the droplets are then pooled together and analysed in bulk.

    As the genetic material from each droplet has been labelled with a barcode, it means the RNA sequences from each cell can be individually identified.

    Compared to previous techniques, which required separating cells into 96 individual wells on a plastic plate, it is orders of magnitude faster and cheaper, something that will be essential for building the Human Cell Atlas.

    Doing this for 40 trillion cells, however, will generate staggering volumes of data, requiring expertise from around the world in many different disciplines, but scientists are already seeing what may come out of it.

    Professor Ehud Shapiro, a computer scientist and biologist at the Weizmann Institute of Science in Rehovot, Israel, said: ‘The Human Cell Atlas 1.0 is trying to map all cell types in the human body.

    ‘Once that is achieved, the thought is to look at questions of cell lineage to produce a sort of 4D atlas of human cell development over time.’

    Cellular history

    The first multi-cellular organism to have its cellular history mapped was a tiny 1 millimetre-long nematode worm called Caenorhabditis elegans. Composed of just 1 000 cells when fully grown, the worm was filmed as it matured from a cell into an adult, allowing scientists to follow its development.

    This feat has not been repeated with any larger organism due to the difficulties in tracking cells in this way. But Prof. Shapiro and his team are developing techniques that allow them to reconstruct the lineage of cells in the human body, using tiny errors that occur in parts of the genome known as microsatellites.

    These are composed of long repeats of the same code, which suffer errors as the DNA is copied when cells divide and replicate.

    Prof. Shapiro and his colleagues calculated that they could reconstruct the family tree of a cell if they could track one million of these errors in its DNA. But so far it has only been possible to examine just a few hundred microsatellite errors in each cell.

    However, Prof. Shapiro has being developing new techniques to look at thousands and even tens of thousands at a time.

    In a project funded by the EU’s European Research Council, called LineageDiscovery, he is now working on an advanced technology called padlock, or molecular inversion, which uses open loop-shaped genetic probes to target potential sites of errors.

    ‘So far we can use 12 000 padlock probes at once and we are now working on using 50 000 probes,’ explained Prof. Shapiro. ‘It makes a million probes seem not so far away.’

    If successful, unlocking the human cell lineage tree in this way could answer some of the fundamental questions bothering biologists today. For example, it could help uncover why some cancers spread to new areas in the body.

    See the full article here .

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  • richardmitnick 12:42 pm on September 6, 2017 Permalink | Reply
    Tags: , Medical camera sees through the body, Medicine, ,   

    From U Edinburgh: “Medical camera sees through the body” 

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    University of Edinburgh

    Sep 4, 2017
    No writer credit

    Scientists have developed a camera that can see through the human body.

    The camera is designed to help doctors track medical tools known as endoscopes that are used to investigate a range of internal conditions. The new device is able to detect sources of light inside the body, such as the illuminated tip of the endoscope’s long flexible tube.

    Light detection

    Until now, it has not been possible to track where an endoscope is located in the body in order to guide it to the right place without using X-rays or other expensive methods. Light from the endoscope can pass through the body, but it usually scatters or bounces off tissues and organs rather than travelling straight through. This makes it nearly impossible to get a clear picture of where the endoscope is.

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    Images from a new camera that can detect tiny traces of light through the body’s tissues. Here, the camera is detecting light emitted from a medical device known as an optical endomicroscope whilst in use in sheep lungs. Image on left shows light emitted from the tip of the endomicroscope, revealing its precise location in the lungs. Right image shows the picture that would be obtained using a conventional camera, with light scattered through the structures of the lung.

    Advanced technology
    The new camera takes advantage of advanced technology that can detect individual particles of light, called photons. Experts have integrated thousands of single photon detectors onto a silicon chip, similar to that found in a digital camera.

    Sensitive

    The technology is so sensitive that it can detect the tiny traces of light that pass through the body’s tissue from the light of the endoscope. It can also record the time taken for light to pass through the body, allowing the device to also detect the scattered light.

    Bedside tool

    By taking into account both the scattered light and the light that travels straight to the camera, the device is able to work out exactly where the endoscope is located in the body. Researchers have developed the new camera so that it can be used at the patient’s bedside.

    Prototype

    Early tests have demonstrated that the prototype device can track the location of a point light source through 20 centimetres of tissue under normal light conditions.

    Proteus project

    The project – led by the University of Edinburgh and Heriot-Watt University – is part of the Proteus Interdisciplinary Research Collaboration, which is developing a range of revolutionary new technologies for diagnosing and treating lung diseases. Proteus is a collaboration between the Universities of Edinburgh and Bath and Heriot-Watt University. It is funded by the Engineering and Physical Sciences Research Council. The research is published in the journal Biomedical Optics Express.

    See the full article here.

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    The University’s mission is the creation, dissemination and curation of knowledge.

    As a world-leading centre of academic excellence we aim to:

    Enhance our position as one of the world’s leading research and teaching universities and to measure our performance against the highest international standards
    Provide the highest quality learning and teaching environment for the greater wellbeing of our students
    Produce graduates fully equipped to achieve the highest personal and professional standards
    Make a significant, sustainable and socially responsible contribution to Scotland, the UK and the world, promoting health and economic and cultural wellbeing.

    As a great civic university, Edinburgh especially values its intellectual and economic relationship with the Scottish community that forms its base and provides the foundation from which it will continue to look to the widest international horizons, enriching both itself and Scotland.

     
  • richardmitnick 8:27 am on September 6, 2017 Permalink | Reply
    Tags: , CorAssist Cardiovascular of Haifa, CORolla, Haifa hospital tests first implant for heart failure, ISREAL21c, Medicine   

    From ISRAEL21c: “Haifa hospital tests first implant for heart failure” 

    Israel21c

    August 31, 2017
    No writer credit

    Canadian patient flew to Israel for the procedure after his wife read about the experimental implant online and his cardiologist encouraged him.

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    Cardiologist Gil Bolotin checking patient Robert MacLachlan, the first in the world to receive the CORolla implant, at Rambam Health Care Campus, Haifa. Photo by Pioter Fliter/RHCC

    A 72-year old Canadian man has become the world’s first recipient of an Israeli-developed implant to treat diastolic heart failure – a fairly common condition for which there is no effective long-term treatment.

    The minimally invasive surgery was performed on July 26th at Rambam Health Care Campus, a medical center in Haifa, by a multidisciplinary team led by cardiologists Gil Bolotin, director of cardiac surgery, and Arthur Kerner, senior physician in the Interventional Cardiology Unit.

    The implant, called CORolla, was developed by Israeli startup CorAssist Cardiovascular of Haifa. The elastic device is implanted inside the left ventricle of the heart and can improve cardiac diastolic function by applying direct expansion force on the ventricle wall to help the heart fill with blood.

    The CorAssist technology was invented by Dr. Yair Feld, a Rambam cardiologist, with doctors Yotam Reisner and Shay Dubi.

    The patient, Robert MacLachlan, explained that he had run out of treatment options in Canada for his diastolic heart failure. His wife had read about the CORolla implant on the Internet and contacted Dr. Karen Bitton Worms, head of research in the department of cardiac surgery at Rambam. MacLachlan’s cardiologist encouraged him to apply to have the experimental procedure in Israel.

    Bolotin said that while many potential applicants were interested in the procedure, no one wanted to be first until MacLachlan came along.

    “I am proud that Rambam offers treatments to patients not available anywhere else in the world,” commented Dr. Rafi Beyar, director and CEO of Rambam.

    The hospital did not comment on the condition of the patient, but in a video released a month after the procedure MacLachlan said he already feels better and has noticed that his skin color looks healthy for the first time in a long time.

    The Israel Ministry of Health has authorized up to 10 clinical trials at Rambam to test the efficacy of cardiac catheterization for placement of the CORolla implant.

    The potential market for the device is large. It is estimated that more than 23 million people worldwide suffer from heart failure, a condition in which the heart fails to pump sufficient oxygenated blood to meet the body’s needs.

    Approximately half of heart failure patients suffer from diastolic heart failure, in which the left ventricle fails to relax and adequately refill with blood, resulting in a high filling pressure, congestion and shortness of breath. This is the condition for which the CORolla device was invented.

    See the full article here.

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    ISRAEL21c is a non-partisan, nonprofit organization and the publisher of an English-language online news magazine recognized as the single most diverse and reliable source of news and information about 21st century Israel.

    Our website offers a vast resource of more than 10,000 originally researched and produced articles, videos, images and blogs by some of Israel’s leading journalists, uncovering the country’s rich and diverse culture, innovative spirit, wide-ranging contributions to humanity, and democratic civil society.

    Every week we reach millions of people through our website, social media channels, and e-newsletter.

     
  • richardmitnick 2:28 pm on September 1, 2017 Permalink | Reply
    Tags: , , Going with the Ion Flow, Ion channels, Medicine, Northwestern University   

    From Northwestern: “Going with the Ion Flow” 

    Northwestern U bloc
    Northwestern University

    Undated
    BRIDGET KUEHN

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    Northwestern Medicine scientists are diving deep into the structure and function of ion channels to inform new therapies.

    A growing cohort of talented Northwestern Medicine scientists is working to unlock the secrets of ion channels and discover how these tiny molecular machines contribute to an array of diseases, from brain tumors and epilepsy to kidney disease and devastating immune deficiencies.

    This group of investigators, including seasoned faculty like Alfred George Jr., MD, Magerstadt Professor and chair of Pharmacology, and newcomers like Paul DeCaen, PhD, assistant professor in the same department, are not only fundamentally altering understanding of disorders, they’re also revealing how existing treatments work and pointing to potential new treatment strategies.

    “All of this expertise provides fertile ground for making new discoveries,” says DeCaen, a former Howard Hughes and Harvard University fellow who joined Northwestern in October 2016. “And a world-class hospital here gives us access to the medical perspective on ion channel-linked diseases.”

    Ion channels are a class of proteins that control the flow of ions such as calcium, sodium or potassium across the membranes of cells, DeCaen explains. Maintaining a proper flow of ions is critical to a multitude of bodily functions, from the transmission of messages between brain cells to the beating of the heart.

    “It seems like a simple job, but it ends up frequently being problematic,” he says.

    Mutations in the genes that encode ion channels have been linked to many medical conditions. To understand how these mutations lead to disease, ion channel investigators try to piece together the three-dimensional molecular structures of ion channels.

    For example, DeCaen and colleagues from the lab of Erhu Cao, PhD, at the University of Utah took this approach to better understand a gene called polycystic kidney disease 2 (PKD2). Mutations in the gene had been found in patients who develop large cysts in their kidneys that cause organ failure. Scientists knew the gene encoded an ion channel that controls the flow of ions, but did not know which ions. Work from DeCaen’s lab pointed to potassium and sodium.

    “We now know what ions move through the channel, but no one had any idea of what it looked like in three-dimensional space,” DeCaen says. “Since function follows form, we figured that this is an important knowledge gap to fill.”

    So, the team chilled the protein to a very low temperature and then used a powerful electron microscope to get the first glimpse of the protein’s configuration. The results were published in the journal Cell last year.

    “Now that we know what the ion channel looks like, we can see how mutations that cause alterations in its structure may cause it to malfunction in the disease state,” he says. “We can start to do some pie-in-the-sky thinking about developing small molecules that can affect the ion channel’s function.”

    For example, in polycystic kidney disease it is not clear whether mutations cause the PKD2 channel to be continually open, allowing an unending flow of ions, or if the mutation closes the channel. There might even be a mix of on/off effects depending on the specific mutation. So, DeCaen and colleagues are using electrophysiological techniques to find out. Their results could inform the design of drugs to combat the disease.

    DeCaen has also been consulting Northwestern clinicians about complications beyond cysts in patients with polycystic kidney disease. These clinical insights might provide clues on the function of these ion channels throughout the body and potentially suggest treatment strategies.

    “In ion channel research, you need a broad range of expertise in medicine,” DeCaen explained. “You need a neurologist, a cardiac arrhythmias expert and kidney disease experts. We have that large pool of scientists and clinicians here at Northwestern.”

    Working with George, and Jennifer Kearney, PhD, associate professor of Pharmacology, DeCaen is also probing the role of ion channels in epilepsy. His lab is recreating the structure of a bacterial version of an epilepsy-linked sodium channel as a first step toward recreating the mammalian version. So far, the work has yielded unexpected clinical benefits.

    “This gave us our first glimpse into how anti-epileptic drugs work,” DeCaen says. It has also suggested potential antibacterial treatments that would target the channel.

    The applications of this line of research go even further: This summer, George and colleagues showed how mutations in a sodium channel called Nav1.9 can lead to a disorder where people are unable to feel pain. The findings, published in The Journal of Clinical Investigation, might have implications for the development of novel therapies for pain.

    “Ion channels represent an under-appreciated class of druggable protein targets,” says George. “A goal for the Department of Pharmacology has been to place ion channels at the center stage of research efforts to find new drug targets.”

    MOVING PARTS

    Meanwhile, Murali Prakriya, PhD, associate professor of Pharmacology, focuses on the Ca2+ release-activated Ca2+ (CRAC) channel. Originally described in immune cells, CRAC channels are found in the plasma membranes of most, if not all, human cells. When the channel opens, it allows calcium ions to flow into the cell, signaling functions such as gene expression and cell proliferation. A growing number of diseases are associated with abnormalities in CRAC channel function including immunodeficiencies, muscular dystrophy and neurological diseases such as Alzheimer’s disease.

    “CRAC calcium channels are widespread and important for many biological processes, from the birth of cells to the death of cells,” Prakriya says. “Therefore, dissecting how CRAC channel activity is controlled and regulated in different contexts is of great interest.”

    His lab is working to understand how CRAC channels operate and contribute to immune host defense mechanisms, the detection of allergens in the lung airways, and brain function.

    “If you lose CRAC channel function through mutations, human patients develop devastating immune deficiencies and muscle weakness,” he explains. “Children born with these symptoms often die in the first six months of life. The simplest infections are quite dangerous to these children.”

    In a paper published in Nature Communications early this year, Prakriya worked with Megumi Yamashita, PhD, DDS, research assistant professor of Pharmacology, and Priscilla Yeung, a student in Feinberg’s Medical Scientist Training Program, to reveal how the CRAC channel opens and closes. This research identified the molecular structure in the channel that functions as the gate, as well as the movements in the channel pore that open the gate.

    First, the scientists used electrophysiology and microscopy techniques to systematically probe the contributions of different regions of the CRAC channel protein to pore opening, identifying an oily amino acid as the channel gate in the process. Then, computer simulations developed by University of Toronto collaborators helped reveal how this amino acid impedes ion conduction.

    “In ion channels, the pore is usually filled with water, so one way to close the pore is to present an oily, hydrophobic chemical group in the pore to prevent water and ions from going through — similar to the way that oil and water don’t mix. To open the pore, the hydrophobic group swings out of the way allowing the pore to fill with water and ions,” Prakriya explains. “The presence of the oily amino acid in the pore creates a closed channel state.”

    These conclusions have important clinical implications. Some human mutations in the gene encoding the CRAC channel leave the gate open and cause uncontrolled bleeding, neurological problems and muscle weakness because the cells in these individuals have excessive levels of calcium all the time.

    “We showed that one of these mutations affected the oiliness of the gate region, thereby chronically filling the pore with water and ions,” Prakriya says. “As a consequence, ions were going through when they shouldn’t.”

    Prakriya’s lab is currently working to understand the molecular signals that open the hydrophobic gate and to identify small molecules that can interact with the gate to alter the channel’s activity. These could correct defects in cell signaling and ameliorate symptoms associated with aberrant CRAC channel activity seen in immune, muscular and neurodegenerative diseases.

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    Anatomy of an Ion Channel
    Ion channels are a class of proteins that control the flow of ions such as calcium, sodium or potassium across the membranes of cells.

    TRANSLATING DISCOVERIES

    While investigators like DeCaen and Prakriya focus on molecular-level details, Rintaro Hashizume, MD, PhD, assistant professor of Neurological Surgery and of Biochemistry and Molecular Genetics, is using mouse models of brain tumors to begin to translate basic ion channel discoveries into experimental therapeutics.

    Before he joined Northwestern in 2014, Hashizume collaborated with a team of ion channel investigators at the University of California, San Francisco, who figured out that medulloblastoma, a cancerous pediatric brain tumor, was enriched with Ether-a-go-go 2 (EAG2) potassium ion channels.

    The EAG2 channel helps regulate the cell cycle and volume of cells, so the investigators searched for a drug that could inhibit it. They found that thioridazine, used to treat schizophrenia, did the trick. Hashizume gave the drug to mice with human medulloblastoma and showed that it stopped tumor growth and, more importantly, prevented metastasis, which occurs when the tumor spreads to other parts of the body, decreasing patient survival rates. The findings were published in Nature Neuroscience.

    “That’s an important therapeutic advantage of the potassium ion channel blocker — if the tumor doesn’t metastasize you can focus on the management of the original tumor,” he says.

    Hashizume has since launched a pediatric tumor research collaboration with George. Using cells derived from a Northwestern pediatric patient with a brain tumor, Hashizume created a mouse model that will allow the team to probe how the mutation affects ion channel function and test treatments that might correct the problem.

    “That’s an important therapeutic advantage of the potassium ion channel blocker — if the tumor doesn’t metastasize you can focus on the management of the original tumor,” he says.

    Hashizume has since launched a pediatric tumor research collaboration with George. Using cells derived from a Northwestern pediatric patient with a brain tumor, Hashizume created a mouse model that will allow the team to probe how the mutation affects ion channel function and test treatments that might correct the problem.

    See the full article here .

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    Northwestern South Campus
    South Campus

    On May 31, 1850, nine men gathered to begin planning a university that would serve the Northwest Territory.

    Given that they had little money, no land and limited higher education experience, their vision was ambitious. But through a combination of creative financing, shrewd politicking, religious inspiration and an abundance of hard work, the founders of Northwestern University were able to make that dream a reality.

    In 1853, the founders purchased a 379-acre tract of land on the shore of Lake Michigan 12 miles north of Chicago. They established a campus and developed the land near it, naming the surrounding town Evanston in honor of one of the University’s founders, John Evans. After completing its first building in 1855, Northwestern began classes that fall with two faculty members and 10 students.
    Twenty-one presidents have presided over Northwestern in the years since. The University has grown to include 12 schools and colleges, with additional campuses in Chicago and Doha, Qatar.

    Northwestern is recognized nationally and internationally for its educational programs.

     
  • richardmitnick 12:13 pm on August 31, 2017 Permalink | Reply
    Tags: , Medicine, Progeria, , Protein turnover could be clue to living longer,   

    From Salk: “Protein turnover could be clue to living longer” 

    Salk Institute bloc

    Salk Institute for Biological Studies

    August 30, 2017

    Overactive protein synthesis found in premature aging disease may also play role in normal aging.

    Scientists at the Salk Institute found that protein synthesis is overactive in people with progeria. The work, described in Nature Communications on August 30, 2017, adds to a growing body of evidence that reducing protein synthesis can extend lifespan—and thus may offer a useful therapeutic target to counter both premature and normal aging.

    “The production of proteins is an extremely energy-intensive process for cells,” says Martin Hetzer, vice president and chief science officer of the Salk Institute and senior author of the paper. “When a cell devotes valuable resources to producing protein, other important functions may be neglected. Our work suggests that one driver of both abnormal and normal aging could be accelerated protein turnover.”

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    Nucleoli in the cell nucleus, stained bright magenta and cyan against the purple backdrop of the nucleus, are enlarged in the progeria cell (right) compared to the normal cell (left). Credit: Salk Institute

    Hutchinson-Gilford progeria is a very rare genetic disease causing people to age 8 to 10 times faster than the rest of us and leading to an early death. The rare mutation occurs in one of the structural proteins in the cell nucleus, lamin A, but it has been unclear how a single defective protein in the nucleus causes the myriad rapid-aging features seen in the disease.

    Initially, Salk Staff Scientist Abigail Buchwalter, first author of the paper, was interested in whether the mutation was making the lamin A protein less stable and shorter lived. After measuring protein turnover in cultured cells from skin biopsies of both progeria sufferers and healthy people, she found that it wasn’t just lamin A that was affected in the disease.

    “We analyzed all the proteins of the nucleus and instead of seeing rapid turnover in just mutant lamin A and maybe a few proteins associated with it, we saw a really broad shift in overall protein stability in the progeria cells,” says Buchwalter. “This indicated a change in protein metabolism that we hadn’t expected.”

    Along with the rapid turnover of proteins, the team found that the nucleolus, which makes protein-assembling structures called ribosomes, was enlarged in the prematurely aging cells compared to healthy cells.

    Even more intriguing, the team found that nucleolus size increased with age in the healthy cells, suggesting that the size of the nucleolus could not only be a useful biomarker of aging, but potentially a target of therapies to counter both premature and normal aging.

    The work supports other research that appears in the same issue showing that decreasing protein synthesis extends lifespan in roundworms and mice. The Hetzer lab plans to continue studying how nucleolus size may serve as a reliable biomarker for aging.

    “We always assume that aging is a linear process, but we don’t know that for sure,” says Hetzer, who also holds the Jesse and Caryl Philips Foundation Chair. “A biomarker such as this that tracks aging would be very useful, and could open up new ways of studying and understanding aging in humans.”

    The work was funded by the National Institutes of Health, the Nomis Foundation, and the Glenn Center for Aging Research.

    See the full article here .

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    Salk Institute Campus

    Every cure has a starting point. Like Dr. Jonas Salk when he conquered polio, Salk scientists are dedicated to innovative biological research. Exploring the molecular basis of diseases makes curing them more likely. In an outstanding and unique environment we gather the foremost scientific minds in the world and give them the freedom to work collaboratively and think creatively. For over 50 years this wide-ranging scientific inquiry has yielded life-changing discoveries impacting human health. We are home to Nobel Laureates and members of the National Academy of Sciences who train and mentor the next generation of international scientists. We lead biological research. We prize discovery. Salk is where cures begin.

     
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