Raleigh Neurology/Flickr

Flexibility testing at a Parkinson's clinic.

A possible breakthrough has happened in the treatment of Parkinsons disease. UCLA researchers have found a way to stop the progression of the disease in animal tests.

Parkinsons is a disease that strikes the nervous system, affecting ones movements. So far, there are no treatments to stop its progression. Medical professionals aren't even sure what actually causes it.

But researchers do believe one particular protein in the brain plays a role. Its found in clumps in all Parkinson's patients.

Researchers at UCLA have created a compound that prevents the protein from clumping. They call it a "molecular tweezer." In live animal tests, the compound binds to that protein, prevents it from aggregating and even breaks up existing clumps.

Most importantly, the compound did this without appearing to harm normal brain cells.

The study was done with transparent zebrafish. Now the findings are being applied to mice. Human trials, they hope, will be next.

Continue reading here:
UCLA researchers stop Parkinson's progression in animal tests

Raleigh Neurology/Flickr

Flexibility testing at a Parkinson's clinic.

A possible breakthrough has happened in the treatment of Parkinsons disease. UCLA researchers have found a way to stop the progression of the disease in animal tests.

Parkinsons is a disease that strikes the nervous system, affecting ones movements. So far, there are no treatments to stop its progression. Medical professionals aren't even sure what actually causes it.

But researchers do believe one particular protein in the brain plays a role. Its found in clumps in all Parkinson's patients.

Researchers at UCLA have created a compound that prevents the protein from clumping. They call it a "molecular tweezer." In live animal tests, the compound binds to that protein, prevents it from aggregating and even breaks up existing clumps.

Most importantly, the compound did this without appearing to harm normal brain cells.

The study was done with transparent zebrafish. Now the findings are being applied to mice. Human trials, they hope, will be next.

Continue reading here:
UCLA researchers stop Parkinson's progression in animal tests

Australia's nursing homes will be swamped by a tidal wave of Parkinson's sufferers unless governments act now, an expert warns.

A Sydney-based Parkinson's disease expert says rates are expected to jump 80 per cent over the next 20 years because of Australia's aging population.

Currently 64,000 people have the progressive brain disease that causes uncontrollable tremors, loss of movement and bowel and bladder problems.

Associate Professor Simon Lewis from the University of Sydney is expected to present new research on the benefits of community-based Parkinson's nurses at a nursing conference on the Gold Coast on Friday.

Professor Lewis says Australia must adopt the UK approach of employing the specialist nurses or pay the price in nursing home care costs.

'You have to have a way of addressing this tidal wave of patients who are coming over the next 20 years,' he told AAP.

His research indicates that access to specialist nurses in the community can stave off the need for nursing home accommodation.

He compared the health of Parkinson's sufferers and their carers in Shoalhaven, NSW, before and six months after they were placed in the care of a specialist nurse.

'Very clearly what we saw is that during the time they had been seeing the nurse the patient's health had improved,' he said.

'More importantly, the carers themselves reported that their own health had improved.'

Here is the original post:
Parkinson's patients to swamp homes

Australia's nursing homes will be swamped by a tidal wave of Parkinson's sufferers unless governments act now, an expert warns.

A Sydney-based Parkinson's disease expert says rates are expected to jump 80 per cent over the next 20 years because of Australia's aging population.

Currently 64,000 people have the progressive brain disease that causes uncontrollable tremors, loss of movement and bowel and bladder problems.

Associate Professor Simon Lewis from the University of Sydney is expected to present new research on the benefits of community-based Parkinson's nurses at a nursing conference on the Gold Coast on Friday.

Professor Lewis says Australia must adopt the UK approach of employing the specialist nurses or pay the price in nursing home care costs.

'You have to have a way of addressing this tidal wave of patients who are coming over the next 20 years,' he told AAP.

His research indicates that access to specialist nurses in the community can stave off the need for nursing home accommodation.

He compared the health of Parkinson's sufferers and their carers in Shoalhaven, NSW, before and six months after they were placed in the care of a specialist nurse.

'Very clearly what we saw is that during the time they had been seeing the nurse the patient's health had improved,' he said.

'More importantly, the carers themselves reported that their own health had improved.'

Here is the original post:
Parkinson's patients to swamp homes

Swim coach Laurie Lawrence.

APN

OLYMPIC and world champion swim coach Laurie Lawrence will add his support to a call for the establishment of a national network of community-based nurses following the publishing of new research into Parkinson's disease.

The findings of the Australian-first Shoalhaven Project reveal the valuable role played by community-based nurses in supporting people living with this devastating, neurodegenerative disease.

This study reveals the crucial role nurses play in significantly improving the quality of life of more than 1-in-350 (64,000) Australians affected by this disease.

One of those 64,000 is Ian Findlay, the former Australian butterfly champion and life-long friend of Lawrence. Findlay was diagnosed with young onset Parkinson's at 40 years of age in 2004.

Lawrence is now urging the Government to fund more community-based Parkinson's nurses in support of Findlay and other sufferers.

"I coached Ian as a young athlete and I know of no one who trained harder than he did. Once he finished his competitive career, I asked Ian to become my assistant coach. We've been friends for 28 years.

"He is a true champion. Ian has tremendous courage and has overcome many obstacles - physical and mental - throughout his distinguished career. Since his diagnosis, he has changed from being an outgoing, bouncy fella to someone who is more introspective and cautious.

"He works incredibly hard to fight the symptoms of Parkinson's with assistance from his hospital-based nurse and his wife, Nicole, who has given up her career as a school teacher to care for him. Both are integral to his physical and mental wellbeing. Having access to a local, community-based nurse would further complement his support network," said Mr Lawrence.

Original post:
Lawrence dives in for Parkinson's

Swim coach Laurie Lawrence.

APN

OLYMPIC and world champion swim coach Laurie Lawrence will add his support to a call for the establishment of a national network of community-based nurses following the publishing of new research into Parkinson's disease.

The findings of the Australian-first Shoalhaven Project reveal the valuable role played by community-based nurses in supporting people living with this devastating, neurodegenerative disease.

This study reveals the crucial role nurses play in significantly improving the quality of life of more than 1-in-350 (64,000) Australians affected by this disease.

One of those 64,000 is Ian Findlay, the former Australian butterfly champion and life-long friend of Lawrence. Findlay was diagnosed with young onset Parkinson's at 40 years of age in 2004.

Lawrence is now urging the Government to fund more community-based Parkinson's nurses in support of Findlay and other sufferers.

"I coached Ian as a young athlete and I know of no one who trained harder than he did. Once he finished his competitive career, I asked Ian to become my assistant coach. We've been friends for 28 years.

"He is a true champion. Ian has tremendous courage and has overcome many obstacles - physical and mental - throughout his distinguished career. Since his diagnosis, he has changed from being an outgoing, bouncy fella to someone who is more introspective and cautious.

"He works incredibly hard to fight the symptoms of Parkinson's with assistance from his hospital-based nurse and his wife, Nicole, who has given up her career as a school teacher to care for him. Both are integral to his physical and mental wellbeing. Having access to a local, community-based nurse would further complement his support network," said Mr Lawrence.

Original post:
Lawrence dives in for Parkinson's

ScienceDaily (Mar. 2, 2012) Millions of people suffer from Parkinson's disease, a disorder of the nervous system that affects movement and worsens over time. As the world's population ages, it's estimated that the number of people with the disease will rise sharply. Yet despite several effective therapies that treat Parkinson's symptoms, nothing slows its progression.

While it's not known what exactly causes the disease, evidence points to one particular culprit: a protein called -synuclein. The protein, which has been found to be common to all patients with Parkinson's, is thought to be a pathway to the disease when it binds together in "clumps," or aggregates, and becomes toxic, killing the brain's neurons.

Now, scientists at UCLA have found a way to prevent these clumps from forming, prevent their toxicity and even break up existing aggregates.

UCLA professor of neurology Jeff Bronstein and UCLA associate professor of neurology Gal Bitan, along with their colleagues, report the development of a novel compound known as a "molecular tweezer," which in a living animal model blocked -synuclein aggregates from forming, stopped the aggregates' toxicity and, further, reversed aggregates in the brain that had already formed. And the tweezers accomplished this without interfering with normal brain function.

The research appears in the current online edition of the journal Neurotherapeutics.

There are currently more than 30 diseases with no cure that are caused by protein aggregation and the resulting toxicity to the brain or other organs, including Parkinson's, Alzheimer's and Type 2 diabetes. It is therefore critical, Bronstein said, to find a way to stop this aggregation process. Over the last two decades, researchers and pharmaceutical companies have attempted to develop drugs that would prevent abnormal protein aggregation, but so far, they have had little or no success.

While these aggregates are a natural target for a drug, finding a therapy that targets only the aggregates is a complicated process, Bronstein said. In Parkinson's, for example, the protein implicated in the disorder, -synuclein, is naturally ubiquitous throughout the brain.

"Its normal function is not well understood, but it may play a role in aiding communication between neurons," Bronstein said. "The trick, then, is to prevent the -synuclein protein aggregates and their toxicity without destroying -synuclein's normal function, along with, of course, other healthy areas of the brain.

Molecular tweezer

Bronstein collaborated with Bitan, who had been working with a particular molecular tweezer he had developed called CLR01. Molecular tweezers are complex molecular compounds that are capable of binding to other proteins. Shaped like the letter "C," these compounds wrap around chains of lysine, a basic amino acid that is a constituent of most proteins.

Read more:
Parkinson's disease stopped in animal model: Molecular 'tweezers' break up toxic aggregations of proteins

ScienceDaily (Mar. 2, 2012) Millions of people suffer from Parkinson's disease, a disorder of the nervous system that affects movement and worsens over time. As the world's population ages, it's estimated that the number of people with the disease will rise sharply. Yet despite several effective therapies that treat Parkinson's symptoms, nothing slows its progression.

While it's not known what exactly causes the disease, evidence points to one particular culprit: a protein called -synuclein. The protein, which has been found to be common to all patients with Parkinson's, is thought to be a pathway to the disease when it binds together in "clumps," or aggregates, and becomes toxic, killing the brain's neurons.

Now, scientists at UCLA have found a way to prevent these clumps from forming, prevent their toxicity and even break up existing aggregates.

UCLA professor of neurology Jeff Bronstein and UCLA associate professor of neurology Gal Bitan, along with their colleagues, report the development of a novel compound known as a "molecular tweezer," which in a living animal model blocked -synuclein aggregates from forming, stopped the aggregates' toxicity and, further, reversed aggregates in the brain that had already formed. And the tweezers accomplished this without interfering with normal brain function.

The research appears in the current online edition of the journal Neurotherapeutics.

There are currently more than 30 diseases with no cure that are caused by protein aggregation and the resulting toxicity to the brain or other organs, including Parkinson's, Alzheimer's and Type 2 diabetes. It is therefore critical, Bronstein said, to find a way to stop this aggregation process. Over the last two decades, researchers and pharmaceutical companies have attempted to develop drugs that would prevent abnormal protein aggregation, but so far, they have had little or no success.

While these aggregates are a natural target for a drug, finding a therapy that targets only the aggregates is a complicated process, Bronstein said. In Parkinson's, for example, the protein implicated in the disorder, -synuclein, is naturally ubiquitous throughout the brain.

"Its normal function is not well understood, but it may play a role in aiding communication between neurons," Bronstein said. "The trick, then, is to prevent the -synuclein protein aggregates and their toxicity without destroying -synuclein's normal function, along with, of course, other healthy areas of the brain.

Molecular tweezer

Bronstein collaborated with Bitan, who had been working with a particular molecular tweezer he had developed called CLR01. Molecular tweezers are complex molecular compounds that are capable of binding to other proteins. Shaped like the letter "C," these compounds wrap around chains of lysine, a basic amino acid that is a constituent of most proteins.

Read more:
Parkinson's disease stopped in animal model: Molecular 'tweezers' break up toxic aggregations of proteins

Newswise Millions of people suffer from Parkinson's disease, a disorder of the nervous system that affects movement and worsens over time. As the world's population ages, it's estimated that the number of people with the disease will rise sharply. Yet despite several effective therapies that treat Parkinson's symptoms, nothing slows its progression.

While it's not known what exactly causes the disease, evidence points to one particular culprit: a protein called -synuclein. The protein, which has been found to be common to all patients with Parkinson's, is thought to be a pathway to the disease when it binds together in "clumps," or aggregates, and becomes toxic, killing the brain's neurons.

Now, scientists at UCLA have found a way to prevent these clumps from forming, prevent their toxicity and even break up existing aggregates.

UCLA professor of neurology Jeff Bronstein and UCLA associate professor of neurology Gal Bitan, along with their colleagues, report the development of a novel compound known as a "molecular tweezer," which in a living animal model blocked -synuclein aggregates from forming, stopped the aggregates' toxicity and, further, reversed aggregates in the brain that had already formed. And the tweezers accomplished this without interfering with normal brain function.

The research appears in the current online edition of the journal Neurotherapeutics.

There are currently more than 30 diseases with no cure that are caused by protein aggregation and the resulting toxicity to the brain or other organs, including Parkinson's, Alzheimer's and Type 2 diabetes. It is therefore critical, Bronstein said, to find a way to stop this aggregation process. Over the last two decades, researchers and pharmaceutical companies have attempted to develop drugs that would prevent abnormal protein aggregation, but so far, they have had little or no success.

While these aggregates are a natural target for a drug, finding a therapy that targets only the aggregates is a complicated process, Bronstein said. In Parkinson's, for example, the protein implicated in the disorder, -synuclein, is naturally ubiquitous throughout the brain.

"Its normal function is not well understood, but it may play a role in aiding communication between neurons," Bronstein said. "The trick, then, is to prevent the -synuclein protein aggregates and their toxicity without destroying -synuclein's normal function, along with, of course, other healthy areas of the brain.

Molecular tweezer

Bronstein collaborated with Bitan, who had been working with a particular molecular tweezer he had developed called CLR01. Molecular tweezers are complex molecular compounds that are capable of binding to other proteins. Shaped like the letter "C," these compounds wrap around chains of lysine, a basic amino acid that is a constituent of most proteins.

Continued here:
Parkinson's Disease Stopped in Animal Model

Newswise Millions of people suffer from Parkinson's disease, a disorder of the nervous system that affects movement and worsens over time. As the world's population ages, it's estimated that the number of people with the disease will rise sharply. Yet despite several effective therapies that treat Parkinson's symptoms, nothing slows its progression.

While it's not known what exactly causes the disease, evidence points to one particular culprit: a protein called -synuclein. The protein, which has been found to be common to all patients with Parkinson's, is thought to be a pathway to the disease when it binds together in "clumps," or aggregates, and becomes toxic, killing the brain's neurons.

Now, scientists at UCLA have found a way to prevent these clumps from forming, prevent their toxicity and even break up existing aggregates.

UCLA professor of neurology Jeff Bronstein and UCLA associate professor of neurology Gal Bitan, along with their colleagues, report the development of a novel compound known as a "molecular tweezer," which in a living animal model blocked -synuclein aggregates from forming, stopped the aggregates' toxicity and, further, reversed aggregates in the brain that had already formed. And the tweezers accomplished this without interfering with normal brain function.

The research appears in the current online edition of the journal Neurotherapeutics.

There are currently more than 30 diseases with no cure that are caused by protein aggregation and the resulting toxicity to the brain or other organs, including Parkinson's, Alzheimer's and Type 2 diabetes. It is therefore critical, Bronstein said, to find a way to stop this aggregation process. Over the last two decades, researchers and pharmaceutical companies have attempted to develop drugs that would prevent abnormal protein aggregation, but so far, they have had little or no success.

While these aggregates are a natural target for a drug, finding a therapy that targets only the aggregates is a complicated process, Bronstein said. In Parkinson's, for example, the protein implicated in the disorder, -synuclein, is naturally ubiquitous throughout the brain.

"Its normal function is not well understood, but it may play a role in aiding communication between neurons," Bronstein said. "The trick, then, is to prevent the -synuclein protein aggregates and their toxicity without destroying -synuclein's normal function, along with, of course, other healthy areas of the brain.

Molecular tweezer

Bronstein collaborated with Bitan, who had been working with a particular molecular tweezer he had developed called CLR01. Molecular tweezers are complex molecular compounds that are capable of binding to other proteins. Shaped like the letter "C," these compounds wrap around chains of lysine, a basic amino acid that is a constituent of most proteins.

Continued here:
Parkinson's Disease Stopped in Animal Model