Is the Alzheimer’s protein contagious?


Controversial new research suggests that the Alzheimer’s disease protein amyloid-beta (above) may be transmissible via surgical instruments or other medical procedures

 

Controversial new research suggests that the Alzheimer’s disease protein amyloid-beta (above) may be transmissible via surgical instruments or other medical procedures

 

Beginning in 1958, roughly 30,000 people worldwide—mostly children—received injections of human growth hormone extracted from the pituitary glands of human cadavers to treat their short stature. The procedure was halted in 1985, when researchers found that a small percentage of recipients had received contaminated injections and were developing Creutzfeldt-Jakob disease (CJD), a fatal neurodegenerative condition caused by misfolded proteins called prions.

Now, a new study of the brains of eight deceased people who contracted CJD from such injections suggests that the injections may also have spread amyloid-β, the neuron-clogging protein that is a hallmark of Alzheimer’s disease. The study is the first evidence in humans that amyloid-β might be transmissible through medical procedures such as brain surgery—according to the researchers. Skeptics, however, note that the CJD prion itself often triggers unusual amyloid deposits; epidemiological studies, they say, find no connection between the injections and increased risk of developing Alzheimer’s disease.

Aside from CJD and the related mad cow disease, kuru is perhaps the most famous prion disease. Endemic to Papua New Guinea and now essentially eradicated, kuru is transmitted through the ritual consumption of human brain tissue at funerals. Increasingly, however, scientists are recognizing that a number of other neurodegenerative diseases, including Alzheimer’s, Huntington disease, and Parkinson’s disease, also involve aberrant proteins that act like “seeds” in the brain. They convert otherwise normal proteins into fibers that “break, form more seeds, break, and form more seeds,” says John Collinge, a neuropathologist at University College London and lead author of the new study.

Still unknown in Alzheimer’s is what role misfolded proteins such as amyloid-β and tau play in the disease, and whether they are transmissible through direct contact with or consumption of contaminated brain tissue. Although scientists have successfully induced amyloid-β transmission in rodents, these experiments relied on “massive” overexpression of the protein, says Samuel Gandy, a neuropathologist at the Icahn School of Medicine at Mount Sinai in New York City. “Exhaustive” attempts to reproduce such transmission in primates have failed, he says, leading many to doubt whether such propagation is possible.

In the current study, Collinge and colleagues examined the brain tissue of eight people, aged 36 to 51, who died of CJD roughly 30 to 40 years after they received the growth hormone injections. Four had a pattern of amyloid-β that pathologists consider moderate-to-severe in people with Alzheimer’s, though they lacked a second type of protein, tau, that is considered an important hallmark of the disease as well, the team reports online today in Nature. Two had milder, more patchy deposits; one was amyloid-free. “It’s a highly unusual finding,” Collinge says. “In that age group, you really don’t see this kind of pathology unless you have a genetic predisposition to Alzheimer’s,” which none of them did, he says.

Still, scientists have known since the 1990s that the prion protein that causes CJD can “cross-seed” amyloid-β, causing abnormal deposits to form, and vice versa, Gandy says. In such a small, observational study, it is impossible to determine whether CJD itself caused the amyloid-β seen in the deceased subjects’ brain tissue, or seeds of the protein were transmitted via injection, he argues. None of the subjects showed signs of tau, the other protein associated with Alzheimer’s disease, he and others point out.

To explore the possibility that CJD, and not amyloid-β seeds, was the culprit, Collinge and colleagues also examined the brains of 116 people with a range of prion diseases unrelated to the hormone injections. They found little to no β amyloid pathology in that group, suggesting that CJD alone was not responsible for the pathology, they say. That’s a “strong argument” in the group’s favor, says Claudio Soto, a neuroscientist at the University of Texas Health Science Center at Houston. Given that prions come in many different forms, however, it’s still possible that the β-amyloid deposits found in the brains of the injection recipients were indeed caused by CJD, whereas the controls remained plaque-free, he notes.

Next, Collinge’s team plans to test vials of archived growth hormone from the original treatments to see whether they can detect amyloid-β protein “seeds.” One obstacle, however, is that scientists don’t know precisely what constitutes such seeds on a molecular level, Collinge says.

Although provocative, the new study cannot answer the question of whether pathogenic amyloid-β “seeds” can be transmitted from person to person through contaminated surgical instruments or blood, Collinge and Soto agree. There is no epidemiological evidence to support that possibility, and any alarm over Alzheimer’s infectiousness is premature, they emphasize. Still, “that’s something that needs to be investigated,” Soto says.

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Creutzfeldt–Jakob Disease


A 54-year-old man presented to the emergency department with a 3-week history of cognitive deterioration and functional decline. He was disoriented, inattentive, and disinhibited. Neurologic examination revealed horizontal gaze-evoked nystagmus, hyperreflexia on the left side, startle myoclonus, and ataxia. Magnetic resonance imaging (MRI) revealed hyperintensity of the cortical gyri of the frontal and occipital lobes, called cortical ribboning (Panel A, arrow), and within the caudate heads on both sides (Panel B, arrows) on diffusion-weighted imaging. Electroencephalography revealed lateralized periodic discharges in the right hemisphere without evidence of seizures. Testing of cerebrospinal fluid was positive for 14-3-3 and tau proteins, which are known markers of prion disease, and the real-time quaking-induced conversion assay, which is highly sensitive for the detection of the abnormal form of the prion protein, was also positive. Given the patient’s rapid clinical deterioration, imaging findings, and cerebrospinal fluid markers, he received a diagnosis of Creutzfeldt–Jakob disease, a fatal spongiform encephalopathy that is caused by the accumulation of abnormal prions. Creutzfeldt–Jakob disease leads to cognitive decline and is characterized by additional neurologic features that manifest according to the location of lesions. Common MRI findings include hyperintensity of the cortex, pulvinar and dorsomedial thalamic nuclei, and basal ganglia on T2-weighted, diffusion-weighted, and fluid-attenuated inversion recovery sequences. The patient died in hospice 8 weeks after the initial onset of symptoms.

Genetic mutation blocks prion disease


Unknown mechanism helped some people in Papua New Guinea escape historic, deadly outbreak.

A genetic variant protected some practitioners of cannibalism from prion disease.

Scientists who study a rare brain disease that once devastated entire communities in Papua New Guinea have described a genetic variant that appears to stop misfolded proteins known as prions from propagating in the brain1.

Kuru was first observed in the mid-twentieth century among the Fore people of Papua New Guinea. At its peak in the late 1950s, the disease killed up to 2% of the group’s population each year. Scientists later traced the illness to ritual cannibalism2, in which tribe members ate the brains and nervous systems of their dead. The outbreak probably began when a Fore person consumed body parts from someone who had sporadic Creutzfeldt-Jakob disease (CJD), a prion disease that spontaneously strikes about one person in a million each year.

Scientists have noted previously that some people seem less susceptible to prion diseases if they have an amino-acid substitution in a particular region of the prion protein — codon 1293. And in 2009, a team led by John Collinge — a prion researcher at University College London who is also the lead author of the most recent analysis — found another protective mutation among the Fore, in codon 1274.

The group’s latest work, reported on 10 June in Nature1, shows that the amino-acid change that occurs at this codon, replacing a glycine with a valine, has a different and more powerful effect than the substitution at codon 129. The codon 129 variant confers some protection against prion disease only when it is present on one of the two copies of the gene that encodes the protein. But transgenic mice with the codon-127 mutation were completely resistant to kuru and CJD regardless of whether they bore one or two copies of it.

The researchers say that the mutation in codon 127 appears to confer protection by preventing prion proteins from becoming misshapen.

“It is a surprise,” says Eric Minikel, a prion researcher at the Broad Institute in Cambridge, Massachusetts. “This was a story I didn’t expect to have another chapter.”

Collinge and his colleagues are now continuing their work, to figure out the mutant protein’s structure and how it shields against illness.

Research could lead to blood test to detect Creutzfeldt-Jakob disease


CJD research
Prion proteins are visualized with immunostaining in this tissue sample from a tonsil biopsy in from a patient variant CJD. 

The detection of prions in the blood of patients with variant Creutzfeldt-Jakob disease (vCJD) could lead to a noninvasive diagnosis prior to symptoms and a way to identify prion contamination of the donated blood supply, according to researchers at McGovern Medical School at The University of Texas Health Science Center at Houston (UTHealth).

The results of the research, led by senior author Claudio Soto, MD, professor in the Department of Neurology and the director of the George and Cynthia Mitchell Center for Alzheimer’s disease and Related Brain Disorders at UTHealth, are published in Science Translational Medicine. First author of the paper is Luis Concha-Marambio, senior research assistant in the Department of Neurology at McGovern Medical School.

CJD research

Claudio Soto, PhD, in his lab at McGovern Medical School at UTHealth.

“Our findings, which need to be confirmed in further studies, suggest that our method of detection could be useful for the noninvasive diagnosis of this disease in pre-symptomatic individuals,” Soto said. “Early diagnosis would allow any potential therapy to be given before substantial brain damage has occurred. In the case of the blood supply, availability of a procedure to efficiently detect small quantities of the infectious agent would allow removal of blood units contaminated with prions, so that new cases can be minimized substantially.”

Human prion diseases are infectious and invariably fatal neurodegenerative diseases. They include sporadic Creutzfeldt-Jakob disease (sCJD), the most common form, and variant Creutzfeldt-Jakob disease, which is caused by the transmission of bovine spongiform encephalopathy—commonly known as mad cow disease—from infected cattle to humans.

Since 1990, 178 people in the United Kingdom have died from vCJD, according to the National CJD Research & Surveillance Unit at the University of Edinburgh. The disease has claimed an additional 49 people worldwide, including four United States residents, according to the European Centre for Disease Prevention and Control. In a handful of cases, the disease was spread through the donated blood supply.

The disease can lay silent in the body for decades as damage slowly builds in the brain from the misfolded infectious proteins called prions. On average, people infected with vCJD die two years after the development of the first symptoms, which can include psychiatric alterations such as depression, anxiety and hallucinations that progress to more severe dementia, muscle contractions and loss of coordination.

Soto’s team analyzed blood samples from 14 cases of vCJD and 153 controls, which included patients affected by sCJD and other neurodegenerative or neurological disorders as well as healthy subjects. To detect the prions, the team used a protein misfolding cyclic amplification assay, invented in Soto’s lab, which mimics the prion replication process in vitro that occurs in prion disease.

The results showed that prions could be detected with 100 percent sensitivity and specificity in blood samples from vCJD patients.

The new study builds on years of research by Soto’s team, whose detection of prions in urine was published in the New England Journal of Medicine in August 2014. In June of this year, Soto received $11 million (USD) from the National Institute of Allergy and Infectious Diseases, part of the National Institutes of Health (U.S.), to study the pathogenesis, transmission and detection of prion diseases including chronic wasting disease in deer.

Scientists develop nasal test for human prion disease


A nasal brush test can rapidly and accurately diagnose Creutzfeldt-Jakob disease (CJD), an incurable and ultimately fatal neurodegenerative disorder, according to a study by National Institutes of Health (NIH) scientists and their Italian colleagues.

Up to now, a definitive CJD diagnosis requires testing brain tissue obtained after death or by biopsy in living patients. The study describing the less invasive nasal test appears in the Aug. 7 issue of the New England Journal of Medicine.

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CJD is a . These diseases originate when, for reasons not fully understood, normally harmless prion protein molecules become abnormal and gather in clusters. Prion diseases affect animals and people. Human prion diseases include variant, familial and sporadic CJD. The most common form, sporadic CJD, affects an estimated 1 in one million people annually worldwide. Other prion diseases include scrapie in sheep; chronic wasting disease in deer, elk and moose; and bovine spongiform encephalopathy (BSE), or mad cow disease, in cattle. Scientists have associated the accumulation of these clusters with tissue damage that leaves sponge-like holes in the brain.

“This exciting advance, the culmination of decades of studies on prion diseases, markedly improves on available diagnostic tests for CJD that are less reliable, more difficult for patients to tolerate, and require more time to obtain results,” said Anthony S. Fauci, M.D., director of the National Institute of Allergy and Infectious Diseases (NIAID), a component of NIH. “With additional validation, this test has potential for use in clinical and agricultural settings.”

An easy-to-use diagnostic test would let doctors clearly differentiate prion diseases from other brain diseases, according to Byron Caughey, Ph.D., the lead NIAID scientist involved in the study. Although specific CJD treatments are not available, prospects for their development and effectiveness could be enhanced by early and accurate diagnoses. Further, a test that identifies people with various forms of prion diseases could help to prevent the spread of prion diseases among and between species. For instance, it is known that can be transmitted via medical procedures such as blood transfusions, transplants and the contamination of surgical instruments. People also have contracted variant CJD after exposure to BSE-infected cattle.

The NIAID study involved 31 nasal samples from patients with CJD and 43 nasal samples from patients who had other neurologic diseases or no neurologic disease at all. These samples were collected primarily by Gianluigi Zanusso, M.D., Ph.D., and colleagues at the University of Verona in Italy, who developed the technique of brushing the inside of the nose to collect olfactory neurons connected to the brain. Testing in Dr. Caughey’s lab in Montana then correctly identified 30 of the 31 CJD patients (97 percent sensitivity) and correctly showed negative results for all 43 of the non-CJD patients (100 percent specificity). By comparison, tests using cerebral spinal fluid—currently used to detect sporadic CJD—were 77 percent sensitive and 100 percent specific, and the results took twice as long to obtain.

Lasers might be the cure for brain diseases such as Alzheimer’s and Parkinson’s.


Researchers at Chalmers University of Technology in Sweden, together with researchers at the Polish Wroclaw University of Technology, have made a discovery that may lead to the curing of diseases such as Alzheimer’s, Parkinson’s and Creutzfeldt-Jakob disease (the so called mad cow disease) through photo therapy.

The researchers discovered, as they show in the journal Nature Photonics, that it is possible to distinguish aggregations of the proteins, believed to cause the diseases, from the the well-functioning proteins in the body by using multi-photon .

“Nobody has talked about using only light to treat these diseases until now. This is a totally new approach and we believe that this might become a breakthrough in the research of diseases such as Alzheimer’s, Parkinson’s and Creutzfeldt-Jakob disease. We have found a totally new way of discovering these structures using just laser light“, says Piotr Hanczyc at Chalmers University of Technology.

If the aggregates are removed, the disease is in principle cured. The problem until now has been to detect and remove the aggregates.
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The researchers now harbor high hopes that photo acoustic therapy, which is already used for tomography, may be used to remove the malfunctioning proteins. Today amyloid are treated with chemicals, both for detection as well as removal. These chemicals are highly toxic and harmful for those treated.

With multi photon laser the chemical treatment would be unnecessary. Nor would surgery be necessary for removing of aggregates. Due to this discovery it might, thus, be possible to remove the harmful protein without touching the surrounding tissue.

These diseases arise when amyloid beta protein are aggregated in large doses so they start to inhibit proper cellular processes.

Different proteins create different kinds of amyloids, but they generally have the same structure. This makes them different from the well-functioning proteins in the body, which can now be shown by multi photon technique.

Over 75 Million Americans are now eating organic. Here are 10 reasons why.


Organic foods and products are the fastest growing items in America’s grocery carts. Thirty million households, comprising 75 million people, are now buying organic foods, clothing, body care, supplements, pet food, and other products on a regular basis. Fifty-six percent of U.S. consumers say they prefer organic foods.

Here are 10 reasons why you should buy organic foods and products:

1. Organic foods are produced without the use of Genetically Modified Organisms (GMOs). Consumers worry about untested and unlabeled genetically modified food ingredients in common supermarket items. Genetically engineered ingredients are now found in 75% of all non-organic U.S. processed foods, even in many products labeled or advertised as “natural.” In addition, the overwhelming majority of non-organic meat, dairy, and eggs are derived from animals reared on a steady diet of GM animal feed. Although polls indicate that 90% of Americans want labels on gene-altered foods, government and industry adamantly refuse to respect consumers’ right to know, understanding quite well that health and environmental-minded shoppers will avoid foods with a GMO label.

2. Organic foods are safe and pure. Organic farming prohibits the use of toxic pesticides, antibiotics, growth hormones, nano-particles, and climate-destabilizing chemical fertilizers. Consumers worry about pesticide and drug residues routinely found in non-organic produce, processed foods, and animal products. Consumer Reports has found that 77% of non-organic produce items in the average supermarket contain pesticide residues. The beef industry has acknowledged that 94% of all U.S. beef cattle have hormone implants, which are banned in Europe as a cancer hazard. Approximately 10% of all U.S. dairy cows are injected with Monsanto and Elanco’s controversial genetically engineered Bovine Growth Hormone, banned in most industrialized nations. Recent studies indicate that an alarming percentage of non-organic U.S. meat contains dangerous antibiotic-resistant bacteria.

3. Organic foods and farming are climate-friendly. Citizens are increasingly concerned about climate-destabilizing greenhouse gas pollution (CO2, methane, and nitrous oxide), 35-50% of which in North America comes from our energy-intensive, chemical-intensive food and farming system. Organic farms and ranches, on the other hand, use far less fossil fuel and can safely sequester large amounts of CO2 in the soil (up to 7,000 pounds of CO2 per acre per year, every year.) Twenty-four billion pounds of chemical fertilizers applied on non-organic farms in the U.S. every year not only pollute our drinking water and create enormous dead zones in the oceans; but also release enormous amounts of nitrous oxide, a super potent, climate-destabilizing greenhouse gas.

4. Organic food certification prohibits nuclear irradiation. Consumers are justifiably alarmed about irradiating food with nuclear waste or electron beams, which destroy vitamins and nutrients and produce cancer-causing chemicals such as benzene and formaldehyde. The nuclear industry, large food processors, and slaughterhouses continue to lobby Congress to remove required labels from irradiated foods and replace these with misleading labels that use the term “cold pasteurization.” The USDA and large meat companies have promoted the use of irradiated meat in school lunches and senior citizen facilities. Many non-organic spices contain irradiated ingredients.

5. Consumers worry about rampant e-coli, salmonella, campylobacter, Methicillin-resistant Staphylococcus aureus (MRSA), and fecal contamination in animal products coming out of the nation’s inhumane and filthy slaughterhouses. The Centers for Disease Control have admitted that up to 76 million Americans suffer from food poisoning every year. Very few cases of food poisoning have ever been linked to organic farms or food processors.

6. Consumers are concerned about billions of pounds of toxic municipal sewage sludge dumped as “fertilizer” on 140,000 of America’s chemical farms. Scientific evidence has confirmed that municipal sewage sludge contains hundreds of dangerous pathogens, toxic heavy metals, flame-retardants, endocrine disruptors, carcinogens, pharmaceutical drugs and other hazardous chemicals coming from residential drains, storm water runoff, hospitals, and industrial plants. Organic farming categorically prohibits the use of sewage sludge.

7. Consumers worry about the routine practice of grinding up slaughterhouse waste and feeding this offal and blood back to other animals, a practice that has given rise to a form of human mad-cow disease called CJD, often misdiagnosed as Alzheimer’s disease. Animals on organic farms cannot be fed slaughterhouse waste, manure, or blood – daily rations on America’s factory farms.

8. Consumers care about the humane treatment of animals. Organic farming prohibits intensive confinement and mutilation (debeaking, cutting off tails, etc.) of farm animals. In addition to the cruel and unhealthy confinement of animals on factory farms, scientists warn that these CAFOs (Confined Animal Feeding Operations) produce enormous volumes of manure and urine, which not only pollute surface and ground water, but also emit large quantities of methane, a powerful climate-destabilizing greenhouse gas.

9. Consumers are concerned about purchasing foods with high nutritional value. Organic foods are nutritionally dense compared to foods produced with toxic chemicals, chemical fertilizers, and GMO seeds. Studies show that organic foods contain more vitamins, cancer-fighting anti-oxidants, and important trace minerals.

10. Consumers care about preserving America’s family farms, world hunger, and the plight of the world’s two billion small farmers. Just about the only small farmers who stand a chance of making decent living these days are organic farmers, who get a better price for their products. In addition study after study has shown that small organic farms in the developing world produce twice as much food per acre as chemical and GMO farms, while using far less fossil fuel and sequestering large amounts of excess CO2 in the soil. Yields on organic farms in the industrialized world are comparable to the yields on chemical and GMO farms, with the important qualification that organic farms far out-produce chemical farms under extreme weather conditions of drought or torrential rains. Of course, given accelerated climate change, extreme weather is fast becoming the norm.

For all these reasons, millions of American consumers are turning to organic foods and other organic items, including clothing and body care products – part of an overall movement toward healthy living, preserving the environment, and reversing global warming.

Source: Organic Consumers Association & RealFarmacy.com

Estimate doubled for vCJD carriers


CJD diseased brain tissue

Twice as many Britons as previously thought could be carrying the human form of “mad cow” disease, variant CJD.

Researchers believe one in 2,000 people in the UK is a carrier of the disease linked to eating contaminated beef.

Their estimate in the BMJ comes from studying more than 32,000 samples of human tissue removed during appendix operations carried out between 2000 and 2012 at 41 hospitals.

It remains unclear if any of these carriers will ever develop symptoms.

Early predictions of a vCJD epidemic didn’t come to fruition.

To date, here have been 177 UK deaths from vCJD. Most of these occurred in the late 90s and early 2000s. There has been only one death in the last two years.

The rare, fatal disease progressively attacks the brain.

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Will these people develop disease and can they transmit it? There are many questions we still do not know the answers to”

Lead researcher Prof Sebastian Brandner

But it appears that relatively few who catch the infectious agent that causes the disease develop symptoms. People can be “silent” carriers for decades and not even know it.

The BMJ research identified 16 such carriers out of the thousands of appendix tissue samples studied.

Experts say many vital questions remain unanswered.

Since the link between vCJD and bovine spongiform encephalopathy (BSE), known as mad cow disease, was discovered in 1996, there have been strict controls to prevent meat from infected cattle from entering the food chain.

However, the average time it takes for the symptoms of vCJD to occur after initial infection is still unclear.

Preventing spread

This means people exposed to infected meat before the food controls were introduced continue to develop variant CJD, and may spread it to others.

Experience tells us that the disease could be transmitted from human to human via blood – in the UK, there have been three reported cases of vCJD associated with a blood transfusion.

Blood donor services take measures to ensure blood is not infected but there is no test to screen for vCJD, although scientists are working on this.

And there is currently no cure for the disease.

Prof Sebastian Brandner of University College London, who led the BMJ research, said: “We do not know what will happen.

“Will these people develop disease and can they transmit it? There are many questions we still do not know the answers to.”

Prof Richard Knight, director of the National CJD Research and Surveillance Unit in Edinburgh, said the answers might not be known for decades.

In the meantime, surveillance was key, he said.

“You can see from the data available that its likely that we will get a secondary or tertiary wave of disease but its likely that these further waves will be small.

“Future clinical cases will be pretty small in number,” he added.

Dr Graham Jackson, of the MRC Prion Unit at UCL Institute of Neurology, said: “Given the high levels of infection indicated by this research, it is now crucial we establish how many people in the UK harbour that infection in their bloodstream in order to adequately assess the risks of transmission through contaminated blood donations.

“Studies to develop new blood tests for CJD must remain a priority to assist with screening and protecting the UK blood supply.”

New test predicts risk for Autism.


A team of Australian researchers, led by University of Melbourne has developed a genetic test that is able to predict the risk of developing Autism Spectrum Disorder, ASD.

Lead researcher Professor Stan Skafidas, Director of the Centre for Neural Engineering at the University of Melbourne said the test could be used to assess the risk for developing the disorder.
 
“This test could assist in the early detection of the condition in babies and children and help in the early management of those who become diagnosed,” he said.
 
“It would be particularly relevant for families who have a history of Autism or related conditions such as Asperger’s Syndrome,” he said.

Autism affects around one in 150 births and is characterized by abnormal social interaction, impaired communication and repetitive behaviours.

The test correctly predicted ASD with more than 70 per cent accuracy in people of central European descent. Ongoing validation tests are continuing including the development of accurate testing for other ethnic groups.

Clinical neuropsychologist, Dr Renee Testa from the University of Melbourne and Monash University, said the test would allow clinicians to provide early interventions that may reduce behavioural and cognitive difficulties that children and adults with ASD experience.
 
“Early identification of risk means we can provide interventions to improve overall functioning for those affected, including families,” she said.

A genetic cause has been long sought with many genes implicated in the condition, but no single gene has been adequate for determining risk.
 
Using US data from 3,346 individuals with ASD and 4,165 of their relatives from Autism Genetic Resource Exchange (AGRE) and Simons Foundation Autism Research Initiative (SFARI), the researchers identified 237 genetic markers (SNPs) in 146 genes and related cellular pathways that either contribute to or protect an individual from developing ASD.

Senior author Professor Christos Pantelis of the Melbourne Neuropsychiatry Centre at the University of Melbourne and Melbourne Health said the discovery of the combination of contributing and protective gene markers and their interaction had helped to develop a very promising predictive ASD test.

The test is based on measuring both genetic markers of risk and protection for ASD. The risk markers increase the score on the genetic test, while the protective markers decrease the score. The higher the overall score, the higher the individual risk.

“This has been a multidisciplinary team effort with expertise across fields providing new ways of investigating this complex condition,” Professor Pantelis said.

The study was undertaken in collaboration with Professor Ian Everall, Cato Chair in Psychiatry and Dr Gursharan Chana from the University of Melbourne and Melbourne Health, and Dr Daniela Zantomio from Austin Health.

The next step is to further assess the accuracy of the test by monitoring children who are not yet diagnosed over an extended study. 

The study has been published in the journal Molecular Psychiatry.

Source: Science Alert

One step closer to ‘Mad Cow’ test

A simple blood test for Creutzfeldt-Jakob Disease and Mad Cow disease is a step closer, following a breakthrough by medical researchers at the University of Melbourne.

Using newly available genetic sequencing scientists discovered cells infected with prions (the infectious agent responsible for these diseases) release particles which contain easily recognised ‘signature genes’.

Associate Professor Andrew Hill — from the Department of Biochemistry and Molecular Biology at the Bio21 Institute — said these particles travel in the blood stream, making a diagnostic blood test a possibility.

“This might provide a way to screen people who have spent time in the UK, who currently face restrictions on their ability to donate blood,” he said.

“With a simple blood test nurses could deem a prospective donor’s blood as healthy, with the potential to significantly boost critical blood stocks.”

Mad Cow disease was linked to the deaths of nearly 200 people in Great Britain who consumed meat from infected animals in the late 1980s.

Since 2000, the Australia Red Cross Blood Service has not accepted blood from anybody who lived in the UK for more than six months between 1980 and 1996, or who received a blood transfusion in the UK after 1980.

The research is published in this week’s Oxford University Press Nucleic Acids Research journal.

Lead author Dr Shayne Bellingham said the breakthrough might also help detect other human neurodegenerative diseases, such as Alzheimer’s and Parkinson’s.

“This is an exciting new field where we can test for conditions in the brain and throughout the body, without being invasive,” he said.

The researchers’ genetic testing focused on a form of cell discharge called exosomes.

If exosomes were infected with prions (the pathogen that causes Creutzfeldt-Jakob Disease and Bovine Spongiform Encephalopathy, commonly known as Mad Cow Disease) they were found to also carry a specific signature of small genes called microRNA’s.

The research was undertaken at the University of Melbourne, with assistance from the Mental Health Research Institute of Victoria, the National Health and Medical Research Council and the Australian Research Council.

Source: Science Alert

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