Two Gene Classes Linked to New Prion Formation: Research

by Kathy Jones on  May 29, 2011 at 2:07 PM Genetics & Stem Cells News
RSS Email Print This Page Comment bookmark
Font : A-A+

New findings reported by University of Illinois at Chicago distinguished professor of biological sciences Susan Liebman suggest that unlocking the mechanisms that cause neurodegenerative prion diseases may require a genetic key.
 Two Gene Classes Linked to New Prion Formation: Research
Two Gene Classes Linked to New Prion Formation: Research

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."

Source: Eurekalert

Post a Comment

Comments should be on the topic and should not be abusive. The editorial team reserves the right to review and moderate the comments posted on the site.
Notify me when reply is posted
I agree to the terms and conditions

So mad cow disease [BSE] can be a naturally occurring disease,and not an infectious disease,so beef is (was)safe in the all world. WHY? The BSE was tested in dairy cows, see"nutritonal experiment" performed in England; published in Veterinary Record (MOORBY et al., 2000) and in Journal of Dairy Science (MOORBY et al., 2000; DEWHURST et al., 2000). Long-term dietary crude protein surpluss, significantly higher than the norm (NRC, 2001; if about daily 30 kg of milk production was recorded and six of the 47 animals (13 percent !!!) developed clinical signs of BSE... In addition about the BSE/ vCJD diseases; this was never justified scientifically! It was pure, math-model-driven science fiction. See more about ; BSE/ vCJD mathematical- models, see my large three comments in ( February 8th 2010; Does vCJD still pose a major public health threat?). According to my opinion; what is the common denominator of the neurodegenerative diseases, including Alzheimer's disease?This was ten years ago (end of March 2001), when I published an alternative theory ( BSE ammonia- magnesium theory), where the main role of NMDA receptors was described. According to this theory, the cause of BSE is an excess of protein and the magnesium deficiency, in the feed rations of ruminants. Such conditions were developed in the mid of 1980s , especially in Great Britain... In addition, on the web of U.S. NATIONAL INSTITUTES OF HEALTH, Aging(December 2010)there was described the effect of drugs,in Alzheimer's disease in humans,on the principle of control hyperfunction of NMDA receptors,which is consistent with my BSE alternative theory of BSE, published 10 years ago. See more about the Nameda; A medication known as Namenda® (memantine), an N-methyl D-aspartate (NMDA) antagonist, is prescribed to treat moderate to severe Alzheimer’s disease... However, less well-known circumstances can be show (as a detective story); in documenting the first case of disease transmission, by blood transfusion. For more informations see my large comments in The Western Star (January 6th 2011; Woman's death in northern Italy is nation's 2nd fatal case of mad cow disease) See also other relationships according to my web and recent presentation at 29th World Veterinary Congress in Vancouver;Neurodegenerative Diseases and Schizophrenia as a Hyper or Hypofunction of the NMDA Receptors.

More News on:

DNA Finger Printing Epigenetics 

News A - Z


News Search

Medindia Newsletters

Subscribe to our Free Newsletters!

Terms & Conditions and Privacy Policy.

Find a Doctor

Stay Connected

  • Available on the Android Market
  • Available on the App Store

News Category

News Archive