July 2001 - Newsletter
In this issue:
I am pleased to acknowledge a grant of $3861.00 from Statewide & Non-government Health Services, Queensland Health for costs associated with the Seminar.
The Association is supporting Cathy Dart to attend the International Huntington Association Meeting to be held in Copenhagen, Denmark in August. Cathy is looking forward to bringing back details of all the latest advances in the research for a treatment for HD.
Many of our existing Committee members have been active supporters for a very long time and are deserving of a break. We always encourage members to join our Management Committee and invitations have been issued through the Newsletter and by word of mouth. However, we understand the challenges affecting many family members that often make commitment to the Association more difficult. For this reason we are considering reducing the size of the Management Committee, and also reducing the number of fundraising activities, thus relieving some of the workload we are currently experiencing.
Financial members of the Association contribute a percentage of the necessary funds to maintain the services we provide. Enclosed in this Newsletter is the annual membership request and I encourage everyone to renew or join the Association's membership and consider including a tax-deductible donation.
After 10 years at the helm, Tim McCarthy, the C.E.O. of the Huntington's Association in Victoria, has chosen to move on to pursue other interests. On behalf of the Association I would like to thank Tim for his significant contribution to Huntington's Disease, not only in Victoria, but Australia wide, and wish him all the best in the future. Glenys Frankly has been appointed as the new C.E.O. and we extend our congratulations to her.
I look forward to meeting with you during the 25th Anniversary Celebrations.
One of the issues I feel we need to address at this time is the structure of the Association's Management Committee as it operates at present, and a reflection on the past, from when this organisation was formed 25 years ago.
For those of you who were involved in those very early days, you will no doubt recall the effort required to raise awareness and money to assist families confronting Huntington's Disease. From that point of view, not a lot has changed. We are still constantly reviewing our strategies on how to promote services offered by the Association, be they very different from those early days, and our need to raise funds to maintain our existing services and look at expanding our network across Queensland.
Currently our Association consists of 12 Committee members; 2 full-time welfare staff, 2 part-time administration staff and 3 part-time Day Respite staff; a small band of volunteers, some of whom are members of support groups in Townsville and Bundaberg; and 483 members, a number of whom are not financial.
During the years we have raised money and awareness by way of street stalls, lamington drives, raffles, excursions, movie evenings, and linen parties to name but a few. In recent times these activities have not been well supported, thus requiring greater effort from less people to carry the load.
The Committee feels it is time for a change. One of the avenues we have to maintain our firm financial base is, for each one of us who value the Association and its membership to consider an annual donation in addition to yearly membership. If we were to be successful in this regard, we would reduce the pressure on the volunteers and contributors currently involved.
Providing we can maintain our level of income, regardless of its source, we are at least able to continue offering the existing services. If we all were to take up the challenge and elevate the needs of the Association in our list of financial priorities, we would be in a position to increase our services, particularly in the area of welfare in regional Queensland. Let us consider ourselves "Team Members" and see what we can achieve together.
An area of work which does not receive a lot of attention in our Newsletter is the valuable contribution of the volunteers involved in the respite program in Brisbane and the social program offered in Townsville, Bundaberg and the Gold Coast. The outings and regular contact enjoyed by people affected by HD in these areas would not be possible without the commitment, care and concern shown by many people, and I would like to express my appreciation to all involved.
You will read in this Newsletter about a recent respite holiday provided by the Townsville Support Group. From all accounts the effort involved was greatly appreciated by clients and carers alike.
Your welfare staff continues to keep busy and during July, Cathy will be visiting the Bundaberg and Maryborough districts and I will visit Townsville. In September Cathy will visit Mackay. We will contact the families and supporters we are aware of to arrange appointments. If you would like us to work with those who are providing services for you, please phone the Brisbane office. Kind regards to you all.
Townsville Support Group - Respite Camp at South Mission Beach from the 25th to 29th May, 2001. Another successful camp was held with nine people attending, including three carers. Vic, Joan and Gavin travelled by road, transporting all luggage and food while Joyce, Belinda, Jenny, Julie-Ann, Rod and Lynn travelled by train.
On arrival at Tully, Vic was assisted by Ann, a local resident, with transporting everyone to our units at South Mission Beach. Vic was a superb organiser and meal planner, plus a great chef serving up hearty and delicious evening meals.
Lunches were special times as we had found a tropical paradise at Wongaling Beach Park nestled under huge trees where we ate freshly made sandwiches followed by hotly contested games of bocce. The winning team of Joyce, Belinda, Julie-Ann and Lynn shared their just rewards of Kit Kats with the others who finished strongly with Joan scoring them at 15-14.
On Sunday morning Vic drove Jenny, Julie-Ann, Belinda and Lynn to the monthly markets where the crafts were interesting and affordable.
We were invited to the home of Ann and Neil for lunch. They have a lovely position where you can enjoy both incredible sunrises and sunsets; most of us would have liked to take up residence if we were asked. Unfortunately we all had to leave after a very relaxing afternoon being entertained by their two staffordshire terriers, Bart and Maggie, who were loved by Belinda. Their cockatil, Caesar, was a favourite of Gavin, who is very keen to own a pair of them.
Ann and Neil were very warm and caring people who helped with our holiday providing transport and fresh fruit.
Our daily beach walks were popular and our only casualty happened on the beach when Rod dislocated his finger while getting up, after he slipped near an old tree trunk. Thank goodness Vic was able to transport us to the Wongaling Ambulance then the Tully Hospital for treatment. The timing was spot on, as Vic had already prepared another delicious meal before the emergency.
Train travelling was great, especially the return journey in the Queenslander with its roomier seating and punctual arrival.
It was a very busy and exciting time for us all, and well worth the effort.
Scientists Find Solution to a Mystery Surrounding Alzheimer's, Huntington's and other Neurological Diseases
Source: Stanford University (http://www.stanford.edu/dept/news/)
Stanford researchers have found an answer to a long-standing mystery surrounding Huntington's, Alzheimer's, Parkinson's and other neurodegenerative diseases.
Their discovery, published in the May 25 issue of the journal Science, focuses on one of the telltale signs of neurodegenerative illness: the mysterious buildup of defective proteins in and around nerve cells.
Healthy cells have the ability to break down and eliminate unwanted proteins. But in neurodegenerative diseases, abnormal proteins clump together to form clusters - called aggregates - that interfere with the cell's normal functions.
"It's been known for years that most neurodegenerative diseases are associated with protein aggregates," says Ron R Kopito, professor of biological Sciences and co-author of the study, "but no one had a clue as to the exact relationship. Do aggregates cause the disease, or are they the result of the disease?"
To find out, Kopito and graduate student Neil F. Bence designed a laboratory experiment to assess the impact of protein aggregates on the inner workings of a cell.
Their specific target was the proteasome - a barrel-shaped enzyme that Kopito calls the master controller of the cell.
"The proteasome is like a salami slicer that cuts protein molecules into little bits," he says. "It gets rid of abnormal proteins, and it breaks down and recycles regulatory proteins no longer needed by the cell."
Human cells contain thousands of proteins, each with a unique three-dimensional shape determined by specific genes. But random genetic errors and mutations may cause proteins to fold into the wrong 3-D configuration - often with devastating results.
One example is huntingtin - a protein found in healthy nerve cells. A slight genetic mutation may cause huntingtin proteins to fold incorrectly and accumulate inside the nerve. Defective huntingtin aggregates are common in patients with Huntington's Disease.
Proteasomes are supposed to slice misfolded proteins into harmless pieces before they have a chance to form aggregates, but how does a proteasome recognize an abnormal protein?
The answer: A tiny molecule called ubiquitin latches onto the damaged protein and carries it to the proteasome, where the protein is sliced and diced.
But in some diseases, the ubiquitin-proteasome system breaks down. Huntingtin aggregates, for example, contain thousands of misfolded proteins with ubiquitin flags attached to them. So why doesn't the proteasome recognize and destroy these ubiquitin-labeled proteins?
"People have speculated that the reason these proteins accumulate is because the proteasome isn't functioning properly. In our study, we put that to the test," Kopito says.
In their lab experiment, Kopito and Bence used human embryonic kidney cells instead of neurons.
To observe proteasome activity in the kidney cells, the researchers devised a genetic tool that causes specific cells to change color. Here's how it worked: They took advantage of a molecule called green fluorescent protein (GFP), which emits a green fluorescence when placed under a special light.
"The level of green fluorescence indicated how efficiently the proteasome was breaking down proteins," says Bence, lead author of the Science study. "If the cell glowed bright green, then we knew the proteasome was not functioning."
The researchers wanted to see what would happen to unstable GFP if normal huntingtin genes were inserted into the kidney cells. The result was clear: The cells did not change color - a strong indication that the proteasome enzymes were doing their job slicing up GFP and other unwanted proteins.
But when Bence and Kopito inserted a mutant huntingin gene, the cells turned bright green in a matter of hours. The change in color was accompanied by a buildup of defective protein aggregates inside the cells.
They tried the same experiment using genes that produce mutant forms of CFTR - a protein that has been linked to the disease cystic fibrosis. The results were the same: Cells containing mutant CFTR proteins also formed aggregates and became brightly fluorescent.
"The key finding in our study is that the function of a proteasome can be impaired by the presence of protein aggregates," Kopito says. "These results provide the first well-documented linkage between protein aggregation and a critical cellular function. If the proteasome isn't working properly, it is unable to perform its regulatory function, which is very bad for the cell."
Cause or effect?
Returning to the original question, do aggregates cause diseases, such as Huntington's and cystic fibrosis, or are they a consequence of disease?
It is a vicious circle, he points out: "The disease produces defective proteins that clump together into aggregates. Then the aggregates build up and interfere with proteasome function, which results in the production of more aggregates that further impair the proteasome."
The relatively slow buildup of aggregates in and around nerve cells could explain the latency of many neurodegenerative diseases, adds Kopito.
"The effects of aggregate formation can remain silent for a long time until aggregates build up to the point where onset of the disease occurs suddenly," he says. "That may be why these diseases usually appear in adults. The same is true with ALS, or Lou Gehrig's disease. Gehrig was a spectacular athlete who lost the use of his muscles in the prime of life and ended up paralyzed."
If it turns out that aggregate proteins are the toxic agents that kill cells, then one treatment would be to dissolve the aggregates or prevent them from forming, notes Kopito.
"Our study shows that a cell turns brightly fluorescent when the proteasome shuts down. That's simple. But the study doesn't tell us why it shuts down," says Bence.
"We believe there are complex causes for the impairment of the proteasome," adds Kopito. "A likely cause is a problem inside the proteasome that prevents proteins from passing through. Imagine a rope with a knot in it. The aggregate can function very much like a knot. Other studies have shown that proteins that do not unfold properly can get stuck inside the proteasome. We want to conduct another experiment to see if aggregates get stuck, too."
In addition to Bence and Kopito, the May Science study was co-authored by Roopal M. Sampat, a graduating senior in biological sciences at Stanford.
Latest Research Findings May Yield New Approach for Developing Effective Therapeutics for Huntington's Disease
Source: Huntington's Disease Society of America - www.hdsa.org
New York, NY, June 14, 2001 - Elena Cattaneo, Ph.D., (University of Milan) a member of the Huntington's Disease Society of America's (HDSA) Coalition for the Cure research group, has uncovered a role for normal huntingtin protein within the brain - to stimulate production of a protein that can protect nerve cells from damage. This significant discovery may lead to the development of effective therapeutics for Huntington's Disease (HD).
HD is an inherited, degenerative brain disorder that results in the progressive loss of control of both the mind and the body. Each child of an affected parent has a 50% chance of inheriting the disease. Currently, there is no effective treatment or cure for the 30,000 Americans and 200,000 who are at risk to inherit this deadly illness.
HD is caused by the presence of an abnormal mutant huntingtin protein in striatal nerve cells, which causes them to die. However, the nerve cells also possess a normal version of huntingtin protein whose full function in the cell is not yet understood.
Mutant huntingtin protein causes striatal neurons to die, although the precise way that this happens is not yet known, causing the symptoms of Huntington's Disease. Cattaneo's team found that one role played by the normal huntingtin protein is to help regulate the production of BDNF, a protein essential for the survival of striatal nerve cells. This activity was not provided by mutant huntingtin, suggesting that in HD patients the nerve cells have less BDNF to promote their survival.
Much additional research must be completed before these findings can help patients, and we want to be clear that this is not a cure," says Cattaneo. "But, we're optimistic that our work will help guide the development of new therapies, such as drugs to replace or boost the activity of normal huntingtin, or to increase levels of another brain protein, BDNF."
The basis of Cattaneo's research was to determine how normal huntingtin may protect cultured rat striatal nerve cells from death that is initiated by mutant huntingtin and to test whether neurons sickened by the mutant protein had lost the potential 'protective' pathway.
Through further examination of cultured CNS cells and animal models of HD, Cattaneo's research team revealed that the mutant huntingtin leaves neurons vulnerable to damage as the transcription of the BDNF gene is impaired, resulting in lower levels of this neuron-protecting protein.
Cattaneo speculates that loss of other essential proteins in neurons already sickened by defective gene products may play a role in several other neurodegenerative diseases. The federal government has recently recognized Huntington's Disease as a "model" for other neurodegenerative diseases. The answers we find for HD today may lead to therapies, and ultimately a cure, for Parkinson's, ALS (Lou Gehric's disease), Alzheimer's and other related diseases.
"The momentum in HD research continues to accelerate and we are very hopeful that effective therapies, and ultimately a cure, for Huntington's Disease are well within our reach," says Barbara Boyle, National Executive Director/CEO, HDSA.
For more information, please contact the Huntington's Disease Society of America at 800-345-HDSA, [email protected], or visit the national web site at www.hdsa.org. HDSA is committed to making this the last generation with HD.
International Huntington Association: Spreading the Word around the Globe
By Ralph Walker, Huntington Society of Canada Founder and a Past President of the IHA.
In April Gerrit began a 15 day, 4,5000km trip by car, visiting the Czech Republic, Slovakia, Austria and Slovenia. He addressed family members, doctors and other health professionals and nurtured the creation of an HD Society in Slovenia. Initial contacts received from Argentina, Chile and Turkey. At the joint meeting of the IHA and the WFN in Holland, over 160 scientists and physicians from around the world who are interested in HD research, and 85 representatives from 26 countries share their knowledge and experiences.
The development work of Gerrit has paid off with the creation of an HD Society in both Argentina and Venezuela. Contacts are also identified in Peru, South Korea and Thailand.
Reprinted from "Gateway" March/April 2001, AHDA (NSW) Inc
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Acknowledgement - Article reprinted with permission from ARAFMI from "ARAFMI News" May-July 2001.
A Grieving Child
Children commonly experience grief following the loss of something or someone important in their life. It is often difficult for parents to know how to deal with a child in grief since they are often dealing with their own loss at the same time. But there are practical things parents can do to help their children work through grief.
Although grief is a normal reaction to loss, people grieve differently. While children's grief reactions differ in many ways to adults, under the surface, people of all ages tend to move through similar stages as they deal with their loss.
Seven tips for helping a grieving child:
1. Reassure the child of their own safety (and the safety of other family members) as soon as possible after the child learns of the loss.
This is one of the questions we are most frequently asked. Irrespective of a client's other problems, sleeping difficulties are usually also present, either as a part of their primary condition or as a disorder in its own right.
Sleeping difficulties can have major adverse effects on a person's life. Such difficulties can lead to psychological distress, impairment in daytime functioning, involvement in fatigue-related error-making or accidents, increased use of sick leave, greater irritability and depression, and prolonged use of minor tranqualisers.
If you identify a person with sleep difficulties, don't hesitate to refer them to Psychology Consultants. Often a very brief, targeted intervention will successfully turn their difficulties around. If you would like more information, call Psychology Consultants on 3395 8633. We would be happy to discuss sleep with you over the phone.
Acknowledgement: "A Grieving Child"
The Seven Habits of Highly Effective Carers
Learn as much as possible about your relative
Share the care with family, friends and community services.
Look after your own physical and mental health.
Get as much information as you can on all the types of assistance available and use them.
Attend to your emotions and talk to professionals if necessary.
Plan for the future.
You can contact your Carer Resource Centre by phoning Freecall 1800 242 636.
Thanks to Carers NSW for providing this article.
Edward Everett Hale
Future Fundraising Activities -
Cookie Drive - The Management Committee has decided to postpone the Cookie Drive until later in the year. Look for order forms in a later Newsletter.
Charity Golf Day at Redbank Plains - 26th August - If you are able to form a team of 4 players, or just come along by yourself, please contact Barbara at the office for further details.
August 2 Townsville Family Support Meeting - 7.30 pm at 59 Cambridge St., Vincent