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Albany Med Awards Prize To Distinguished Scientists

This year's $500,000 Albany Medical Center Prize in Biomedicine and Biomedical Research is being shared by three recipients.

The prize, one of the nation’s largest for science and medicine, is given to scientists who have altered the course of medical research.

The 2016 recipients are:  Dr. F. Ulrich Hartl, managing director of the Max Plank Institute for Biochemistry in Germany;  "I'm immensely grateful to the jury. I'm sure it was a difficult task with so many excellent nominations that they must have received, and it's fantastic that they selected the three of us."  Dr. Arthur L. Horwich, a professor of genetics and pediatrics and an investigator at the Howard Hughes Medical Institute of Yale University School of Medicine in Connecticut;   "I am really honored and humbled to be recognized with the Albany Medical Center Prize. Dean Verdile's phone call took me completely by surprise. Thanks so much to you and to the jury members. I'm delighted to be sharing this recognition with my long-time colleagues in the field, Ulrich and Susan."  That would be Susan Lee Lindquist, Ph.D., professor of biology at Massachusetts Institute of Technology, who telephoned in:  "It's such an important prize. The people who've been recognized for it in the past have done such inspiring work, I'm just deeply touched to think that my work is of that same level and inspires other people. And I think maybe perhaps I'll also just say that any one person can only do so much."

The winners have made discoveries that will lead to creating new drugs that could slow down or possibly eliminate symptoms indicative of Alzheimer's, Parkinson’s disease and even some forms of cancer.

Albany Med's Dr. Vincent Verdile acted as master of ceremonies, telling the audience that the three researchers each worked to unlock some of the secrets of "protein folding," which is critical to deploying the genetic codes that give individual cells their unique characteristics.  "Protein folding is one of the most ancient and most fundamental processes in biology, and disruption of this folding process can lead to disease. These three researchers have shown that protein folding is not spontaneous as we once believed, but instead is achieved with once unrecognized molecular assistance, or helpers."

Credit Albany Medical Center
The Albany Medical Center Prize was established in 2000 by the late Morris “Marty” Silverman, a New York City businessman and philanthropist who grew up in Troy, N.Y., to honor scientists whose work has demonstrated significant outcomes that offer medical value of national or international importance.

So what will the awardees do with the prize money?  

Horwich: "We're pretty well funded for the research, so I think in my case, the money'll go to further education of my kids and grandkids."

Hartl:  "In my case i think you should better discuss this with my wife" (audience laughter)

Lindquist:  "The nice thing about this prize is that it isn't directly to go towards the funding and the research, but it's really to go towards us and to just be an honor for us and a joy."

That joy, shared by recipients over the last 16 years, is courtesy of the late Morris "Marty" Silverman, a Troy-born New York City businessman and philanthropist who gave Albany Med $50 million from the Marty and Dorothy Silverman Foundation, which allows for the prize to be awarded annually for 100 years.

BONUS content - More about the research: 

It had been universally believed that folding was a spontaneous process. However, Dr. Horwich noticed in his experiments that a class of proteins imported into mitochondria was not folding spontaneously as expected.

Intrigued, he contacted Dr. Hartl in Germany, an expert in this area of mitochondrial biology. Together and independently, they turned conventional science on its head by discovering a complex system of specialized proteins inside cells, called molecular chaperones, which guide proteins during the folding process by binding them and transiently shielding them so that they cannot misfold or aggregate (clump together with other molecules in a dysfunctional fashion) with each other. One form of such shielding occurs inside tiny ring-shaped compartments inside one type of chaperone called a chaperonin. Folding occurs in a large encapsulated cavity inside these "machines" ensuring that proteins do not misfold or aggregate. In the case of the original situation in the mutant mitochondrion, the function of a chaperonin, called hsp60, was missing.

These revolutionary findings were reported in 1989 in two papers in Nature magazine.

At this same time, Dr. Lindquist, a biologist working at the University of Chicago and then MIT, was making discoveries that paralleled the work of Drs. Hartl and Horwich. Studying biological responses in diverse organisms from yeast to plants to fruit flies, she too discovered previously unknown proteins playing a vital role in protein folding. She also discovered these so-called "heat shock" proteins were synthesized in mass quantities when organisms were experiencing stress from overheating. It turned out they were playing an emergency protective role, acting in clever and diverse ways to make sure that protein folding occurred correctly. Later, Dr. Lindquist would find that heat shock proteins were present in all organisms, including humans.

She focused on two of these proteins, called hsp90 and hsp104. She found hsp90 is required to help an organism grow under normal and stressful circumstances like heat and oxidative stress, while hsp104 is an extreme survival protein, called in to fix protein folding under very harsh conditions. Though the proteins have very different functions both act to fuel the evolution of new biology.

While the work of these researchers was stunning from a biological standpoint, it later became clear that chaperone-mediated protein folding had profound medical implications, as protein misfolding plays a role in several of the most devastating diseases of humans, especially neurodegenerative conditions such as Alzheimer's disease, Parkinson's disease, Huntington's disease, amyotrophic lateral sclerosis (ALS), some forms of cancer, as well as the evolution of microbial drug resistance.

For instance, Dr. Lindquist found that while hsp90 plays a beneficial role in helping normal proteins fold properly, cancer can hijack this process using hsp90 to fold mutated proteins that drive malignancy. This is also true for drug resistance, which can develop as proteins evolve. Some of her studies now focus on how to inhibit this process.

Also she is developing drugs to manipulate the protein misfolding that drives neurodegenerative diseases like Alzheimer's and Parkinson's, where proteins misfold as people age.

Dr. Lindquist has successfully used yeast cells to study the process and to search for drugs that could combat these diseases.

“In a career spanning three decades, Susan Lindquist has made numerous and invaluable contributions to the study of protein folding, demonstrating that the shape shifting of proteins can have profound and unexpected influences in fields as wide-ranging as human disease, evolution and biomaterials,” said Li-Huei Tsai, director of MIT’s Picower Institute for Learning and Memory.

Dr. Hartl’s studies have also raised the hope that manipulating the chaperone process with drugs or other treatments could delay or alter disease. For instance, he is currently studying how protein aggregates may be destroying nerve cells in neurodegenerative disease, and how increasing the number of chaperones may reverse this process.

His work on molecular chaperones, and their ability to prevent aggregation of proteins, has particular promise for development of drugs for Parkinson's disease or Alzheimer’s disease, diseases where these “clumped up” protein aggregates deposit in the brain, disrupting the function of neurons.

Additionally, Dr. Hartl continues to work on the basic understanding of how molecular chaperones function in cells to cause correct folding, including studies involving the role molecular chaperones play in photosynthesis and implications this can have on agriculture.

Dr. Horwich has studied ALS for several years, focusing on protein quality control mechanisms, among other things, trying to understand exactly what is causing the motor failure and paralysis, hallmarks of the disease.

“Over the last two decades, working at first together and later independently, Hartl and Horwich have succeeded—through rigor, incisiveness and sheer brilliance of their work—in advancing the understanding of physiological protein folding from a barely glimpsed landscape to a clear view rich in illuminating details,” said Alexander Varshavsky, Ph.D., the Smits Professor of Cell Biology at Caltech, and recipient of the 2014 Albany Medical Center Prize.

Dave Lucas is WAMC’s Capital Region Bureau Chief. Born and raised in Albany, he’s been involved in nearly every aspect of local radio since 1981. Before joining WAMC, Dave was a reporter and anchor at WGY in Schenectady. Prior to that he hosted talk shows on WYJB and WROW, including the 1999 series of overnight radio broadcasts tracking the JonBenet Ramsey murder case with a cast of callers and characters from all over the world via the internet. In 2012, Dave received a Communicator Award of Distinction for his WAMC news story "Fail: The NYS Flood Panel," which explores whether the damage from Hurricane Irene and Tropical Storm Lee could have been prevented or at least curbed. Dave began his radio career as a “morning personality” at WABY in Albany.
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