Health
LAKEPORT, Calif. – The Sutter Lakeside Hospital Foundation announced that donors met the Sutter Health matching grant challenge and raised over $50,000 in 2012 to purchase medical equipment for the Women’s Imaging Department.
“I am constantly amazed at the level of giving in our community,” said Foundation Chair Dr. Mark Buehnerkemper. “This new medical technology will allow patients to remain close-to-home, instead of having to travel outside of our community for breast cancer and bone loss testing. This is a tremendous benefit for all women in our community.”
Sutter Health’s matching grant program allows each affiliate to choose a program or a piece of technology to fund through philanthropy.
If the hospital can raise funds through charity for half the cost of the program or medical equipment within a year, Sutter Health will match these donations dollar-for-dollar.
In 2012, Lake County donors decided to fund a Mammatome Breast Biopsy System and a GE Lunar Prodigy DexaScanner for the Women’s Imaging Department at Sutter Lakeside Hospital.
The Mammatome allows clinicians to conduct breast biopsies as an outpatient procedure under either X-ray, MRI or ultrasound technology, increasing test result accuracy.
The DexaScanner assesses bone loss caused by osteoporosis, chemotherapy and radiation therapy.
Both pieces of equipment are slated to arrive by mid-summer and should be available for patients by early fall.
“We pride ourselves on providing the absolute best patient care possible and having state-of-the-art technology is an important piece of the puzzle,” said Imaging Director Jose Aponte. “The fact that donors made this all possible makes this even more of a blessing.”
“Sutter Health’s matching grant program has given our donors a powerful partner over the past several years,” said Sutter Lakeside Development Officer Rebecca Southwick. “Through their matching grant program, our donors have been able to purchase the Mobile Health Services Unit, the stroke telemedicine equipment in our emergency department, and we’ve been able to underwrite the creation of the mobility park. Donors continue to allow us to do great things for our community.”
Siri Nelson, Sutter Lakeside chief administrative officer, agreesd. “We’ve received terrific support from our donors over the past several years and the Women’s Imaging Campaign is one more sign that charitable giving is strong in Lake County. Our 2013 matching grant focus is the Heart Health Campaign. Our county has a high incidence of heart disease and we’d like to purchase a new echocardiogram for the hospital. Our goal is $85,000 in cash and pledges by this December.”
To learn more about the 2013 Heart Health Matching Grant Campaign, contact Rebecca Southwick at 707-262-5121 or by sending an email to
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Clumps of proteins that accumulate in brain cells are a hallmark of neurological diseases such as dementia, Parkinson’s disease and Alzheimer’s disease.
Over the past several years, there has been much controversy over the structure of one of those proteins, known as alpha synuclein.
MIT computational scientists have now modeled the structure of that protein, most commonly associated with Parkinson’s, and found that it can take on either of two proposed states – floppy or rigid.
The findings suggest that forcing the protein to switch to the rigid structure, which does not aggregate, could offer a new way to treat Parkinson’s, said Collin Stultz, an associate professor of electrical engineering and computer science at MIT.
“If alpha synuclein can really adopt this ordered structure that does not aggregate, you could imagine a drug-design strategy that stabilizes these ordered structures to prevent them from aggregating,” said Stultz, who is the senior author of a paper describing the findings in a recent issue of the Journal of the American Chemical Society.
For decades, scientists have believed that alpha synuclein, which forms clumps known as Lewy bodies in brain cells and other neurons, is inherently disordered and floppy. However, in 2011 Harvard University neurologist Dennis Selkoe and colleagues reported that after carefully extracting alpha synuclein from cells, they found it to have a very well-defined, folded structure.
That surprising finding set off a scientific controversy. Some tried and failed to replicate the finding, but scientists at Brandeis University, led by Thomas Pochapsky and Gregory Petsko, also found folded (or ordered) structures in the alpha synuclein protein.
Stultz and his group decided to jump into the fray, working with Pochapsky’s lab, and developed a computer-modeling approach to predict what kind of structures the protein might take.
Working with the structural data obtained by the Brandeis researchers, Stultz created a model that calculates the probabilities of many different possible structures, to determine what set of structures would best explain the experimental data.
The calculations suggest that the protein can rapidly switch among many different conformations. At any given time, about 70 percent of individual proteins will be in one of the many possible disordered states, which exist as single molecules of the alpha synuclein protein.
When three or four of the proteins join together, they can assume a mix of possible rigid structures, including helices and beta strands (protein chains that can link together to form sheets).
“On the one hand, the people who say it’s disordered are right, because a majority of the protein is disordered,” Stultz said. “And the people who would say that it’s ordered are not wrong; it’s just a very small fraction of the protein that is ordered.”
The MIT researchers also found that when alpha synuclein adopts an ordered structure, similar to that described by Selkoe and co-workers, the portions of the protein that tend to aggregate with other molecules are buried deep within the structure, explaining why those ordered forms do not clump together.
Stultz is now working to figure out what controls the protein’s configuration. There is some evidence that other molecules in the cell can modify alpha synuclein, forcing it to assume one conformation or another.
“If this structure really does exist, we have a new way now of potentially designing drugs that will prevent aggregation of alpha synuclein,” he said.
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