Scientists at Washington University School of Medicine (WUSM) in St. Louis have spent some years investigating the links between circadian rhythm and Alzheimer’s, and have recently been making some real inroads. Following a 2018 study demonstrating how disrupted sleep can accelerate the buildup of toxic plaques associated with the disease, the team has now identified a protein implicated in the progression of the disease that appears highly regulated by the circadian rhythm, helping them join the dots and providing a potential new therapeutic target.
A protein, previously found to be an effective blood-based biomarker of neurodegenerative diseases such as Alzheimer’s, has for the first time been detected in the eye. The discovery lays the foundation for promising new diagnostic eye tests hoping to catch neurodegenerative diseases years before symptoms appear.
Scientists are already struggling to make headway in the fight against dementia, and the discovery of a new more aggressive form of neurodegeneration that’s often misdiagnosed as Alzheimer’s disease further complicates the problem.
A new study from the University of Kentucky has described a novel form of dementia characterized by the toxic accumulation of four different proteins in the brain. The research suggests many patients diagnosed with Alzheimer’s disease may be suffering from this different, and more complex, neurodegenerative condition.
An international team of scientists has designed a novel antibody that can accurately detect the toxic oligomers suspected to cause the neurodegeneration associated with Alzheimer’s disease. It’s hoped the breakthrough will lead to improved drug design and clinical testing by offering researchers a new way to measure these protein aggregations.
Research into treatments for Alzheimer’s disease has primarily focused on eliminating toxic accumulations of amyloid proteins, known as plaques. Some studies have recently suggested the main neurodegenerative damage associated with dementia and Alzheimer’s may happen at an earlier point, before these amyloid proteins have formed into larger plaques.
The earliest stages of amyloid protein dysfunction in Alzheimer’s disease appear to be when the proteins begin misfolding and clumping together. As these misfolding proteins begin clustering they initially form what are called oligomers. And these amyloid oligomers can begin forming more than a decade before larger plaques appear.
“There is an urgent unmet need for quantitative methods to recognize oligomers – which play a major role in Alzheimer’s disease, but are too elusive for standard antibody discovery strategies,” explains Michele Vendruscolo, lead on the new research from the University of Cambridge’s Centre for Misfolding Diseases. “While the amyloid hypothesis is a prevalent view, it has not been fully validated in part because amyloid-beta oligomers are so difficult to detect, so there are differing opinions on what causes Alzheimer’s disease.”
While its exact causes are unknown, Alzheimer’s disease is commonly associated with clumps of toxic amyloid plaques in the brain, and researchers are continuing to understand the different components that help them take shape. Scientists at the University of Illinois at Urbana-Champaign have developed a new compound that attacks a number of the key players in the formation of amyloid plaques, significantly decreasing the level of plaques and reducing inflammation in the brain.
The presence of amyloid plaque buildup is considered a hallmark of Alzheimer’s, but it is thought that damage begins to occur in the brain long before these clumps appear. A great deal of research into the disease seeks to attack the building blocks of amyloid plaques. This includes protein fragments called beta-amyloid peptides, which may pose an even greater threat than the plaques themselves.
“Studies have found strong evidence that these soluble peptides are the most neurotoxic species and are causing memory loss and neuron cell death,” says Liviu Mirica, who led the new research. “Plaque formation might be an attempt by the brain to neutralize the threat.”
Along with beta-amyloid peptides, recent research has begun to illuminate the role metal ions might play in driving Alzheimer’s progression. Post-mortem studies have uncovered elevated levels of copper, iron, and zinc in the brains of sufferers, which are thought to interact with and stabilize the beta-amyloid peptides, as well as increasing oxidative stress and brain inflammation.
A new UT Southwestern study has offered yet more evidence affirming the value of exercise in slowing the brain degeneration associated with dementia and Alzheimer’s disease. The research is suggesting aerobic exercise may be more effective than mild flexibility training in directly reducing hippocampal deterioration.
Alkahest, a California-based biotech start-up, has just revealed some compelling early results from an ongoing Phase 2 trial into the efficacy of its novel formulation of plasma proteins derived from young blood, developed to slow, or even stop, the cognitive decline associated with Alzheimer’s disease.
Alzheimer’s is a disease with a number of potential causes and therefore a number of potential targets for prevention. One of those centers on a protein call tau, which can gather in long tangles that kill off neurons in the brain. Scientists have developed what they describe as a vaccine to keep the brain clear of these dangerous clumps, and found that treating mice in this way helped stave off the kind of memory decline associated with the disease.
Researchers from the Mayo Clinic have identified a new target in the battle against dementia and age-related cognitive decline – zombie cells. More formally known as senescent cells, these are cells that have stopped dividing but don’t die, and tend to accumulate with age. The new research reveals that many pathological signs of neurodegenerative disease can be eliminated by removing these cells from the brain.
from Sky News:
Patients have been implanted with a tiny “brain pacemaker” in an attempt to slow the progress of Alzheimer’s disease.