Articles tagged with Prions
A 30-year-old man died of variant Creutzfeldt-Jakob disease (vCJD) with a unique genetic profile, highlighting potential cases with long incubation periods. His heterozygous PRNP gene may indicate silently infected individuals, posing concerns for public health.
A new treatment route for bovine spongiform encephalopathy (BSE) and its human form Creutzfeldt Jakob disease (CJD) may be closer based on new findings from the University of Leeds. Glypican-1 has been shown to cause abnormal prion proteins to rise, and reducing levels in infected cells can lower their levels.
Researchers discovered that Srebp2 regulates cholesterol biosynthesis in prion-infected neuronal cells, leading to increased cholesterol levels and potential disease promotion. This finding may lead to new therapy approaches for prion-dependent diseases.
Researchers at the University of Edinburgh have discovered specific immune cells that attract corrupted proteins, increasing the risk of variant CJD in younger individuals. This finding may lead to better diagnosis methods and potential vaccine development.
Scientists have characterized the detailed structure of prions using unconventional X-ray diffraction methods. The results show significant structural differences between natural and synthetic prions, which may explain their infectious behavior.
Researchers have characterized the detailed structure of prions using unconventional X-ray diffraction methods. The study found surprisingly large structural differences between natural prions and synthetic analogs, shedding new light on their infectious behavior.
A University of Toronto-led team has identified the evolutionary ancestry of the prion gene, revealing its connection to ZIP family metal ion transporters. This discovery may provide new insights into prion protein function and underlying mechanisms of diseases like BSE and Creutzfeldt-Jakob disease.
Researchers at Whitehead Institute have shown that a single gene mutation can cause a transmissible neurodegenerative disease in mice, similar to human fatal familial insomnia. The study demonstrates that mutations associated with prion diseases are sufficient to cause the disease and the spontaneous generation of transmissible prions.
Researchers at Case Western Reserve University School of Medicine have discovered the prion protein as a novel biomarker for pancreatic cancer. The study found that the prion binds to filamin A in human pancreatic cancer cells, disrupting cell organization and signaling, and leading to aggressive tumor growth.
Researchers discovered that prion proteins bind more stably to copper in human bodies, which may prevent their misfolding. The study suggests that copper binding could play a beneficial role in early stages of prion diseases such as Alzheimer's and Parkinson's.
Researchers at Scripps Florida have created a faster method to distinguish between different infectious prion strains, which can cause diseases in animals and humans. The new approach reduces the time lag for identification from six months to four months, allowing scientists to accelerate research and better understand disease risks.
Researchers found a key role for disrupted copper regulation in prion disease progression, suggesting that the loss of copper binding ability contributes to neurodegeneration. The study identified a threshold at four extra octarepeats, beyond which changes in molecular properties lead to toxic effects.
Whitehead Institute researchers have identified 24 prion candidates in yeast, shifting the view from biological anomalies to mediators of trait inheritance. Prions in yeast appear to prepare individual organisms for environmental changes, sometimes providing a survival advantage.
A study found that iron homeostasis is disrupted in prion disease-affected brains, leading to a vicious cycle of increased iron uptake. The misfolded protein PrP-scrapie causes this imbalance by altering cellular iron metabolism, paving the way for novel therapeutic strategies.
Scientists have identified a new, infectious prion in yeast that can affect the expression of hundreds of genes. The discovery raises questions about the role of these proteins in degenerative brain diseases and their potential impact on human cells.
A recent study found that oral quinacrine does not increase survival in patients with prion disease, but may slow progression and improve symptoms. However, the treatment was associated with increased incidence of adverse events, which were mostly mild and manageable.
Researchers from the University of Konstanz found that normal protein PrP helps cells communicate during embryonic development. Without it, physiological abnormalities occur, and cell-to-cell contact is disrupted. This discovery may aid in understanding prion diseases and developing effective treatments.
Researchers at the University of Liverpool have determined the atomic structure of the binding between an antibody and a brain protein that could be key to treating vCJD. The study found that this antibody, ICSM18, has therapeutic potential in preventing brain cell infection and reversing early damage caused by the disease.
Researchers at Yale University have identified a key role for cellular prion proteins in triggering the damage caused by amyloid-beta peptides in Alzheimer's patients. The study suggests that these proteins act as early targets for new therapies, offering promising hope for the treatment of this debilitating disease.
A team of Wisconsin researchers has discovered that birnessite, a common soil mineral, can penetrate and degrade the prion's armor. This finding may provide new methods for decontaminating soil and other environments where prions reside.
A genome-wide association study has identified two new genetic risk factors for variant Creutzfeldt–Jakob disease, including a SNP near the beta receptor for retinoic acid and a region close to STMN2. These findings suggest that genetic susceptibility plays a significant role in prion diseases.
Researchers developed a transgenic mouse model expressing mutant prion protein, resulting in a fatal neurological disorder. The discovery may help unravel the mystery of this progressive disease affecting humans and animals.
Researchers have discovered novel prion infectivity in white and brown fat tissues of mice, shedding new light on the pathogenesis of prion diseases. This finding may have significant implications for preventing prion infection in animals and humans, particularly in ruminants suspected of exposure to or infection with prions.
In response to environmental stress, yeast cells trigger a protein-misfolding mechanism that reveals hidden genetic variation, allowing them to adapt and evolve rapidly. This 'prion switching' enables cells to digest previously inaccessible materials, such as certain nutrients and antibiotics, without prior genetic mutation.
Researchers discovered that misfolded proteins trigger a mechanism in yeast cells, allowing them to adapt to stress and evolve more quickly. Under stressful conditions, the cells create prions, which can induce beneficial changes, such as enhanced growth on energy sources or resistance to antibiotics.
Researchers at TU Munich and ETH Zurich develop a new method to synthesize anchored proteins, enabling in-depth studies of prions and their influence on conversion to pathogenic forms. The team successfully produces a synthetic GPI-anchored protein, which attaches to cell membranes, helping to track down the infectious form of the prion.
Scientists have detected changes in prion protein production and accumulation in brains of cattle with a rare neurological disorder. The study suggests an association between abnormally high levels of prion protein and the disease, but differs from BSE and CJD.
A genetic mutation in the Prion Protein Gene is linked to mad cow disease, according to a new study by Kansas State University researcher Juergen A. Richt. The mutation affects less than 1 in 2,000 cattle and can be combated through selective breeding and culling of genetically affected animals.
Researchers have successfully created new strains of infectious proteins called prions by mixing infectious prions from one species with normal prion proteins from another. This breakthrough could provide insight into the risk of prion diseases spreading between species and has significant implications for public health.
Researchers identified a prion protein characteristic unique to certain natural sheep scrapie cases, which may help study prion diversity and changes during cross-species transmission. The findings distinguish these isolates from bovine BSE cases.
Researchers have identified a new form of fatal dementia in 16 Americans, with 10 victims already deceased, characterized by brain damage caused by misfolded protein accumulation, differing from known CJD, prompting genetic and environmental investigation
A team of researchers found that infectious prions have highly flexible loops, absent in non-infectious forms, which differ significantly in their molecular structure. The study suggests that the molecular structure is a key factor in determining a protein's infectiousness.
Normally functioning prions prevent neurons from self-destruction by inducing overactive brain cells that respond longer and more vigorously to stimulation. This hyperactivity eventually leads to neuron death, potentially explaining why misfolded prions cause dementia.
Scientists have identified a crucial portion of a protein responsible for hereditary cerebral amyloid angiopathy (CAA), a disease linked to stroke and dementia. The study used solid-state nuclear magnetic resonance (NMR) spectroscopy to reveal the structure of CAA fibrils, which form plaques in blood vessels in the brain.
Researchers developed a special filter that quickly removes prion proteins, causing mad cow disease and Creutzfeldt-Jakob disease, from blood. The device has been approved for use in Europe and is expected to be commercialized in Ireland and the UK in mid 2008.
A new study has identified four distinct biochemical subgroups in Creutzfeldt-Jakob disease, potentially representing different prion strains. These subgroups were found in both sporadic and iatrogenic cases of the disease, with no correlation to the prion protein gene.
A new study reveals that prion infection increases free cholesterol content in cell membranes, affecting phospholipase A2 activation and neuronal depletion. This finding suggests a crucial role for cholesterol regulation in prion diseases and other neurodegenerative disorders.
Researchers at Scripps Research Institute have developed two new tests that can identify lethal prion strains quickly and accurately. The tests, the Standard Scrapie Cell Assay and the Cell Panel Assay, significantly accelerate prion research by producing results in under two weeks.
Research reveals lymph nodes facilitate neuroinvasion of prions at low doses, accelerating infection after node removal. The study's findings have important implications for developing new prevention and treatment strategies for prion diseases.
Fernandez-Funez will study ways to protect brain cells from damage by prions using genetically engineered flies that produce proteins like those found in 'mad cow' disease. His goal is to find new mechanisms of prion neurotoxicity and develop protective chaperone proteins.
Researchers found that prion infection influences the expression of endogenous retroviruses in mouse cells, with some sequences increasing and others decreasing. The effects could be suppressed by an anti-prion drug, suggesting a possible link between prions and retrovirus production.
Researchers have discovered a second prion protein called 'Shadoo' that coexists with the well-known PrP protein, potentially shedding light on brain function in mad cow disease. The study, published in the EMBO Journal, reveals an unexpected alteration in prion infections where Shadoo disappears as PrP accumulates.
Researchers have successfully propagated a prion from one organism into another, expanding our understanding of these infectious proteins and their role in fatal neurodegenerative diseases. The discovery opens up new avenues for studying prion propagation and highlights the need to search for additional prions.
Scientists have developed a method to amplify vCJD prions from human brain tissue extracts, enabling recognition by existing detection methods. This breakthrough could aid in confirming whether someone is infected with variant CJD, crucial for preventing further disease spread through infected blood donations.
A study by University of Wisconsin-Madison researchers found that soil particles can increase the infectious nature of rogue proteins causing CWD. Binding to common soil minerals like montmorillonite significantly increases oral transmissibility, with a nearly 700-fold difference observed.
Researchers have developed a method to amplify prions from brain tissue samples using normal blood cells, improving detection test sensitivity. This breakthrough may lead to a blood test for screening individuals at risk of passing variant CJD through blood transfusion or surgery.
Researchers have identified a protective role for normal prion proteins in preventing the formation of beta-amyloid plaques in the brain, a hallmark of Alzheimer's disease. High levels of PrPc reduced beta amyloid formation, while low or absent levels allowed it to return.
Researchers have discovered critical regions within prions that determine much of their behavior, providing a new framework for exploring prion biology. These regions, known as recognition elements, can be activated by environmental conditions and amino acid sequence alterations.
Researchers have developed an oral vaccine that can prevent mice from developing brain diseases similar to mad cow disease. The vaccine stimulates the immune system, resulting in delayed onset of symptoms even in mice with low antibody levels.
A Scripps research study reveals the dynamic structural details of single prion molecules, shedding light on normal folding mechanisms and abnormal amyloid fibril conversion. The findings may lead to novel therapeutic targets for neurodegenerative diseases.
Researchers found that early brain degeneration can be reversed if prions are depleted in neurons, leading to improved cognitive function and reversal of neurological pathology. This discovery opens new avenues for targeting neuronal prion protein as a therapeutic approach and may enable early intervention in human prion disease.
A Brown University study finds that a single protein plays a major role in the spread of deadly prion diseases by fragmenting clusters of infectious proteins. This process could be slowed or inhibited with a drug, potentially slowing progression of diseases like Alzheimer's and Parkinson's as well.
Researchers developed a method to selectively bind and remove prion protein, effectively eliminating disease-causing agents. The approach could significantly reduce the risk of transmission through blood donation, particularly in cases of variant Creutzfeldt-Jakob disease (vCJD).
A new case of variant Creutzfeldt-Jakob disease (vCJD) linked to a blood transfusion has been confirmed in the UK. The patient developed symptoms six years after receiving a contaminated blood sample from a donor who later died from vCJD. Early diagnosis and monitoring are crucial for affected individuals.
Researchers successfully tested a new method of treatment for fatal brain diseases like scrapie and Creutzfeld-Jakob, slowing disease progression by up to 97% in mice. The approach uses RNA interference to reduce production of the pathogenic prion protein.
Researchers at CReSA have made significant advances in tests using DNA vaccines on animal models, enabling a delay in symptom appearance and paving the way for human treatment. The vaccine induces a complete immune response, including humoral and cellular responses, overcoming the tolerance barrier faced by prions.
Researchers found infectious misfolded prion protein in heart muscle, decreasing the heart's ability to pump blood. High levels of scrapie infectivity were also identified in the blood of mice used in the study.
Researchers found that brittle prion particles can spread infection quickly by breaking into new seeds. This discovery boosts basic understanding of prion infections and could lead to new ideas for designing drugs to prevent or discourage prion seeding.
Researchers develop IMPY tracer to visualize abnormal protein in Alzheimer's and prion diseases, providing new directions for future research. The tracer may also aid in early diagnosis of Alzheimer's with single photon emission computed tomography (SPECT) imaging.
Scientists at the University of Wisconsin-Madison discovered that certain soil types serve as natural prion repositories, potentially contributing to CWD transmission. The study found that prions bind tightly to montmorillonite clay and remain infectious after boiling in a detergent solution.