Parkinson’s disease possibly originates in gastrointestinal tract

Parkinson’s disease has been attributed the clumping together of a protein called alpha-synuclein that are generally found at the ending of the nerve cells. When the protein clumps together, the nerve cells get damaged and it deteriorates the dopamine system and results in issues with movement and speech.

New research suggests that Parkinson’s disease may start off in the gut. The study was conducted on mice and it confirms the theory that the abnormally folded alpha-synuclein may originate in the gut and then eventually spread to the brain. This transmission happens through the vagus nerve, a nerve bundle that sends signals to and from the brain to several of the body’s organs, including the gut, reported recently.

“It supports and really provides the first experimental evidence that Parkinson’s disease can start in the gut and go up the vagus nerve,” said a professor of neurology and co-author of the research.

The research also discovered that the folding of the protein has similar effects on the brain of mice as well as humans, and the symptoms it causes in both are similar. “We have what we think is a really accurate [animal] model that can be used to work out mechanisms – but also to test therapies,” said the Prof.

The Prof. reckoned the possibility of undoing the misfolds in the protein at the gut itself to stop Parkinson’s disease early on. Another reason the researchers believe that the disease origins in the gut is because those who had an appendicitis surgery early in life had a reduced risk of developing Parkinson’s disease later in life.

Through this experiment on mice, they also recorded a drop in dopamine levels in mice. It resulted in the progressive loss of neurons for seven months. The mice also showed a significant deterioration on their motor skills and also developed memory, behavioural and anxiety issues.

Through this research, it was discovered that when the proteins in the gut becomes misfolded, it results in a domino effect that led to the misfold of the same alpha-synuclein protein in the brain as well.

“This study adds support to a growing base of evidence [implying] that changes in the gut play a key role in the initiation of Parkinson’s, although it is not believed to be the only place where the condition may start,” said a Dr.

“By identifying and halting these changes before they reach the brain, we may be able to prevent the majority of Parkinson’s symptoms ever appearing and improve the lives of people who will be affected,” she concluded.

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BP drug shows promise for treating Parkinson's

Felodipine, a prescribed drug to treat high blood pressure, has shown promise against Parkinson's, Huntington's and forms of dementia in studies carried out in mice and zebra-fish.

In a study, scientists have shown in mice that felodipine may be a candidate for re-purposing.

A common feature of neuro-degenerative diseases is the build-up of misfolded proteins.

These proteins, such as huntingtin in Huntington's disease and tau in some dementias, form "aggregates" that can cause irreversible damage to nerve cells in the brain.

A team led by a Prof. used mice that had been genetically modified to express mutations that cause Huntington's disease or a form of Parkinson's disease, and zebra-fish that model a form of dementia.

Felodipine was effective at reducing the build-up of "aggregates" in mice with the Huntington's and Parkinson's disease mutations and in the zebrafish dementia model.

The treated animals also showed fewer signs of diseases.

"This is the first time that we're aware of that a study has shown that an approved drug can slow the build-up of harmful proteins in the brains of mice using doses aiming to mimic the concentrations of the drug seen in humans," said the Prof.

The hypertension drug was able to slow down the progression of these potentially devastating conditions and "so we believe it should be trialed in patients," he added.

In healthy individuals, the body uses a mechanism to prevent the build-up of such toxic materials.
This mechanism is known as autophagy, or 'self-eating', and involves cells eating and breaking down the materials.

"This is only the first stage, though. The drug will need to be tested in patients to see if it has the same effects in humans as it does in mice. We need to be cautious, but I would like to say we can be cautiously optimistic," said the Prof. 

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New skin test detects prion infection before symptoms appear

Prions can infect both humans and animals, causing Creutzfeldt-Jakob disease (CJD) in humans, mad cow disease in cattle, and chronic wasting disease in elk and deer. The infectious, misfolded protein particles often go undetected as they destroy brain tissue, causing memory loss, mobility issues, and ultimately death. Preclinical detection of prions has proven difficult, but new research suggests skin samples hold early signs of prion disease that precede neurologic symptoms. 

"Currently a definitive diagnosis of Creutzfeldt-Jakob disease is dependent on the examination of diseased brain tissue obtained at biopsy or autopsy. It has been impossible to detect at the early preclinical stage," said an associate professor of pathology.

In a ground-breaking study, an international team of researchers successfully used two methods to detect prions in skin samples collected from inoculated rodents. The study provides the first proof-of-concept evidence that readily accessible skin samples could be used to detect prion disease early—before clinical symptoms appear.

In the new study, the researchers successfully detected prions in rodent skin samples as early as two weeks post-infection. They also detected prions in the skin of uninoculated rodents that were housed alongside inoculated cage mates, demonstrating that prion transmission can occur between cohabitating rodents.

Prions were detected in skin samples from the inoculated rodents before they showed any clinical signs of prion disease. The researchers first inoculated the brains of hamsters and humanized transgenic mice with rodent or human prion samples, respectively. Then, they collected skin and brain samples at different time points, and used two different methods to detect disease-associated prion proteins in the tissues. In both hamsters and mice, the researchers detected prions in skin before they could be detected in brain tissue. The researchers concluded that skin prions could serve as a useful biomarker for preclinical diagnosis of prion diseases.

The study compared two highly-sensitive prion detection methods: RT-QuIC (real-time quaking-induced conversion) and sPMCA (serial protein misfolding cyclic amplification). "Both assays were able to efficiently amplify trace amounts of disease-associated prion protein found in the skin tissues of infected animals," said the study's first author. The tests use prions in tissue samples as a template and either normal brain tissue or synthetic prion protein as "building blocks" to dramatically amplify minute amounts of prions to detectable levels.

One of the methods, RT-QuIC, has been used to detect prion particles in symptomatic CJD patients. However, it normally requires invasive cerebrospinal fluid (CSF) sampling that may be contraindicated for certain patients. Additionally, "The CSF-based prion test results could be uncertain in some cases and not all CSF specimens from patients with prion disease are RT-QuIC positive," said an associate professor of pathology. "Although skin samples may not replace CSF in routine RT-QuIC-based prion disease diagnosis, they may be helpful when prion disease is suspected but CSF is either unavailable or RT-QuIC-negative."

The study results build upon previous work by the researchers showing that autopsy skin samples from human prion disease patients exhibit prion seeding and infectivity. The next step will be to develop and validate the skin prion tests for clinical use.

Said the researcher, "Since the skin is readily accessible and skin biopsy is minimally invasive, detection of skin prions will be very useful for monitoring disease progression and assessing therapeutic efficacy during clinical trials or treatments when prion therapy becomes available in the future."

 The researchers were recently awarded a $2.9 million grant to validate the test methods using human skin samples. They will determine if skin prions could serve as a diagnostic biomarker for CJD or a source of prion transmission.

The researchers believe the methods may also be adapted for diagnosis of other diseases involving misfolded proteins. "Sensitive, minimally invasive detection of various misfolded proteins in skin, such as tau in Alzheimer's disease and alpha-synuclein in Parkinson's disease, could be highly valuable for disease diagnosis and monitoring of disease progression and efficacy of treatments," the researcher said. "It's possible that the skin will ultimately serve as a mirror for us to monitor these misfolded proteins that accumulate and damage the brain in patients with these conditions." 
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New Caffeine-Based Drugs May Prevent Parkinson's Progression

Scientists have developed novel caffeine-based chemical compounds that show promise in preventing the progression of Parkinson's disease.

Parkinson's disease attacks the nervous system, causing uncontrolled shakes, muscle stiffness, and slow, imprecise movement, chiefly in middle-aged and elderly people.

It is caused by the loss of brain cells (neurons) that produce dopamine, an essential neurotransmitter that allows neurons to "talk" to each other.

Researchers from the University of Saskatchewan in Canada focused on a protein called a-synuclein (AS), which is involved in dopamine regulation.

In Parkinson's sufferers, AS gets misfolded into a compact structure associated with the death of dopamine-producing neurons. AS appears to act like a prion disease. In prion diseases, one mis-folded protein triggers mis-folding in others, spreading like falling dominos.

"Many of the current therapeutic compounds focus on boosting the dopamine output of surviving cells, but this is effective only as long as there are still enough cells to do the job," said Jeremy Lee, a biochemist from Saskatchewan. "Our approach aims to protect dopamine-producing cells by preventing a-synuclein from mis-folding in the first place," said Lee.

Although the chemistry was challenging, Lee explained the team synthesised 30 different "bifunctional dimer" drugs, that is, molecules that link two different substances known to have an effect on dopamine-producing cells.

They started with a caffeine "scaffold," guided by literature that shows the stimulant has a protective effect against Parkinson's.

 From this base, they added other compounds with known effects: nicotine, the diabetes drug metformin, and aminoindan, a research chemical similar to the Parkinson's drug rasagiline.

Using a yeast model of Parkinson's disease, researchers discovered two of the compounds prevented the AS protein from clumping, effectively allowing the cells to grow normally. "Our results suggest these novel bifunctional dimers show promise in preventing the progression of Parkinson's disease," Lee said.

The findings were published in the journal ACS Chemical Neuroscience. 

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