Monthly Archives: May 2011

HELP 4 HD ~ The Huntingtons Disease Project



An Email


8:10 PM, May. 26, 2011

The upcoming Republican primary election in Raritan prompts me to write this letter.

I am Mayor Jo-Ann Liptak’s aunt and I am, naturally, very much in favor of her re-election. I have known her since the day she was born and she was then, and is now, a very special person. I am proud of her accomplishments.

She was a teacher for 34 years; served a three-year term in 1995 to 1998 on the Borough Council; served as mayor since 2006 and, is a mother who experienced the most unthinkable tragedy of losing her 28-year-old son to Huntington’s disease in 2004. Such an experience, unless you have had a similar loss, cannot be described. I know the pain because I shared it with her. It would have been the end for a weaker person.

Jo-Ann is first and foremost honest, intelligent and totally devoted to her town and office of mayor. Her male opponents are frightened by her honesty, intelligence and gender. She is, after all, a woman who is strong, capable, and not easily intimidated, which is a very rare commodity these days.

They should be frightened, for she has done more for Raritan than any other male who has ever held the position of mayor. She will continue to put Raritan and the office of mayor first.

The residents of Raritan are not stupid. They know a good thing when they see it and they know that brain beats brawn every time. Please join me for voting for my niece, Jo-Ann Liptak, on June 7.

Ann Navatto



Article at:

Public release date: 26-May-2011


Public release date: 26-May-2011

Contact: Paul Francuch
University of Illinois at Chicago

Study finds 2 gene classes linked to new prion formation


Unlocking the mechanisms that cause neurodegenerative prion diseases may require a genetic key, suggest new findings reported by University of Illinois at Chicago distinguished professor of biological sciences Susan Liebman.

Prions can turn a normal protein into a misfolded form. One prion in mammals promotes progressive neurodegenerative disorders like “mad cow” disease that often prove fatal. But how this process happens remains an open question for scientists.

Prions have been found to exist in a wide range of organisms. Those in brewer’s yeast, which researchers like Liebman study, provide critical insight into how prions work.

Prion proteins in yeast aggregate, while non-prion proteins do not. Aggregation of new prions happens spontaneously — but, in the natural world, very slowly.

Anita Manogaran, a former UIC research assistant professor in biological sciences, working with Liebman, sped-up prion formation to identify genes important in the process. The researchers were also able to monitor different stages of prion appearance by tagging prion proteins with another protein that fluoresces green. Cells in the process of forming prions had fluorescent rings, which could give rise to cells with prions.

“We learned there are some genes important for the generation of prions,” Liebman said.

Some 400 yeast genes were screened for the ability to prevent the new appearance of yeast prion proteins.

“Through a number of screens, we came down to a much smaller number (of genes) that inhibited prion appearance,” Liebman said. These genes fell into two classes — one that could still make the rings, which is the hallmark of the beginning of prion aggregation. But the other class of genes had trouble forming rings, Liebman said.

Liebman and Manogaran also looked beyond new prion formation to see if these same genes had an effect on toxicity associated with a protein that causes Huntington’s disease — a fatal human neurodegenerative disorder.

“We found that genes that could make rings also were more toxic in the presence of the Huntington’s disease protein,” Liebman said. “If no rings were made, they were less toxic.”

The full implications of the findings are not yet understood, Liebman cautioned.

“The more we understand about these mechanisms and the genes that are involved, the more we’ll be able to understand the new appearance of prion disease — like Creutzfeldt-Jakob and ‘mad cow’ — and Huntington’s disease. The more we understand what affects toxicity, the more we’ll understand why these are toxic.”


The findings were reported in the May 19 issue of PLoS Genetics.

Manogaran, now at the University of Wisconsin-Milwaukee, UIC research assistant Joo Hong and former UIC undergraduate student Joan Hufana worked with Liebman on the project. Other co-authors of the paper include Jens Tyedmers of the University of Heidelberg and Susan Lindquist of the Massachusetts Institute of Technology.


Article at:

HDSA National Call-in Day


Dear Friend,


HDSA National Call-in Day is finally here! This is the chance for advocates across the country to raise their voices for the Huntington’s Disease Parity Act (S. 648/H.R. 718). Will you take a few minutes to call your Senators and Representative for HD?


Making your calls is easy, and fast! Go to  for phone numbers and talking points for your two Senators and your U.S. Representative! You will also be able to leave feedback, so that HDSA can follow up. After you make your calls, use the ‘Tell A Friend’ link at the bottom of the page to ask up to ten people to call Congress for HD!


HDSA is sending a press release to Congress, so your Senators and Representative will be expecting your call! The Huntington’s Disease Parity Act (S. 648/H.R. 718) would have a huge impact on the HD community. It will make it easier for people with HD to access Social Security Disability Insurance (SSDI) and Medicare benefits. By calling Congress today, you have a chance to truly make a difference.


Don’t Wait! Make Your Calls Today!


If you have any questions about National Call-in Day, please contact Jane Kogan at



Jane Kogan