UCSF Nobel laureate Stanley B. Prusiner, MD, UCSF professor of neurology and director of the Institute for Neurodegenerative Diseases, today (Oct. 15, 2010) was named to receive the National Medal of Science, the nation's highest honor for science and technology.
Prusiner was among 10 recipients named by President Barack Obama. In addition, three individuals and one team were named as recipients of the National Medal of Technology and Innovation. All of the awardees will receive their medals at a White House ceremony later this year.
The National Medal of Science honors individuals in a variety of fields for pioneering scientific research that has led to a better understanding of the world, as well as to the innovations and technologies that give the United States its global economic edge. It is administered by the National Science Foundation, established by Congress in 1959.
Prusiner received the medal for his discovery of and ongoing research on a novel infectious agent, which he named the prion (PREE-on). The prion, composed solely of protein, causes bovine spongiform encephalopathy, or "mad cow" disease, and other related fatal neurodegenerative diseases in animals and humans. Prusiner and colleagues are working on better methods for detecting prions and on the development of effective treatments for prion diseases.
In 1997, Prusiner won the Nobel Prize in Physiology or Medicine for his discovery.
In recent years, Prusiner has intensified his focus on developing preventions and cures for the neurodegenerative diseases that include the prion diseases as well as the more common disorders, Alzheimer's and Parkinson's diseases, at the Institute for Neurodegenerative Diseases (IND), involving faculty at six University of California campuses. He considers Alzheimer's disease one of the most devastating and underfunded illnesses affecting society, and is advocating strongly for a substantial increase in federal funding for research.
"Alzheimer's disease afflicts 5.3 million people in America," said Prusiner. "Each year, about 500,000 people die with cancer and about the same number die with Alzheimer's. Yet, Alzheimer's research receives only $450 million annually from the National Institutes of Health, about 1/15th that devoted to cancer research. We urgently need to increase funding to make substantial breakthroughs."
Pioneering Prion Research Noting Prusiner's "vision, perseverance and courage in the face of skeptics as he pioneered prion research two decades ago," UCSF Chancellor Susan Desmond-Hellman, MD, MPH, called him an "inspiration to us all."
"His revelations regarding prions have dramatically impacted scientists' understanding not only of prion diseases, but also of the more common neurodegenerative diseases, including Alzheimer's disease, Parkinson's disease and amyotrophic lateral sclerosis," she said. "He represents the best in translational science - driving basic research toward therapies for patients."
Prusiner's discovery that a protein alone could be infectious was considered heretical when he reported it in 1982. At the time, scientists believed that infections could only be transmitted by bacteria, viruses, fungi and parasites, all which have genomes composed of either DNA or RNA. Protein is composed of amino acids.
Prusiner determined that a normal form of prion protein exists in all mammals, including humans, and that the protein becomes lethal when it acquires an aberrant shape in brain cells. He showed that a particular segment of the normal prion protein loses its corkscrew-shape structure (known as an alpha helix) and flattens into so-called beta sheets. Once it does, the beta sheet form latches on to a neighboring prion protein, twisting its normal spiral tendrils flat. This activity occurs throughout the brain in a domino effect. The damaged proteins ultimately cause death of nerve cells in the brain.
His research has informed scientists' understanding that all neurodegenerative diseases - including Alzheimer's disease, frontotemporal dementias, Parkinson's disease, amyotrophic lateral sclerosis and Huntington's disease - involve the accumulation of proteins that have lost their normal shape. Each disease is caused by a different protein, but research on the abnormal prion protein has fueled scientists' understanding of a prion-like phenomenon in each of the diseases.