MEDIA ADVISORY
CONTACT: Karen Myers, FSU College of Medicine 
(850) 545-5679; Karen.myers@med.fsu.edu

March 1, 2019

FSUCares SPENDING SPRING BREAK ON MEDICAL OUTREACH TRIP

A number of Florida State University College of Medicine students are looking for more than fun in the sun during spring break. This year, like every year since the College of Medicine welcomed its first class in 2001, students will be traveling to Immokalee to provide health screenings and patient education to migrant farmworkers and local seniors.

Eleven first-year medical and physician assistant students are making the trip. They’re joined by a handful of faculty members, including College of Medicine Dean John P. Fogarty and faculty from the College of Medicine’s Immokalee Health Education Site. 

The trip is sponsored by FSUCares, a student-run organization designed to help the underserved and underprivileged populations both locally and abroad. The trip is made possible through a grant from the Chapman Foundation.

“This trip is a unique opportunity to provide medical outreach to migrant farmworkers who may not have access to care, and expose students to this population and its needs,” said Karen Myers, FSU College of Medicine associate professor and faculty advisor to FSUCares. “Our students are giving up their spring break and prioritizing the mission of our college, and they’re getting a cultural education in return. For as long as we’ve been doing this service-learning trip, nearly every student involved has returned to Immokalee for an additional rotation in their third and fourth years.”

Students and faculty will be available for interviews and photos in Immokalee.

SATURDAY, MARCH 2
9 a.m.-Noon
Immokalee Community Park
321 N. 1st St.
Immokalee 
Providing health information to children and families and assisting with activities at Ciclovia Immokalee.

4-7:30 p.m.
Horizon Village Labor Camp
415 Rose Ave.
Immokalee
Providing health screenings and HIV screenings at local migrant camp for single males.

MONDAY, MARCH 4
8-11:30 a.m.
The Roberts Senior Center
905 Roberts Road
Immokalee
Providing health screenings, medication reconciliation and arts-in-health activity for local seniors.

Please note: The itinerary is subject to change. Contact Karen Myers to make arrangements for interview opportunities March 2-5.
For more about FSUCares, visit med.fsu.edu/fsucares
For more about the College of Medicine’s Immokalee Health Education Site, visit med.fsu.edu/Immokalee

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In a new study, researchers discovered a critical missing step in the production of proteasomes — tiny structures in a cell that dispose of protein waste — and found that carefully targeted manipulation of this step could prove an effective recourse for the treatment of cancer.

Their findings were published in the journal Cell Reports.

“Proteasomes are kind of like the cell’s recycling center for proteins,” said study co-author Robert Tomko, an assistant professor of biomedical sciences in FSU’s College of Medicine. “Typically, proteins inside the cell are produced to fulfill a certain function, and once that function is fulfilled, they are no longer needed and need to be removed.”

Proteasomes collect those unneeded, damaged or defective proteins and decompose them into amino acid building blocks, which are subsequently repurposed for the production of new proteins. Proteasomes are assembled from more than 60 protein subunits, “however, they don’t just form spontaneously from these parts,” Tomko said.

“They require assistance from dedicated helper proteins called assembly chaperones,” he said. “These chaperones act as factory workers to build proteasomes. Once the proteasome is built, the chaperones have to release it so that it can function properly and they can then begin work on the next one.”

It’s this stage of the assembly process — the chaperone’s release of the fully completed proteasome — that interested Tomko and his team. Before their study, the signaling mechanisms responsible for triggering the release of assembled proteasomes was a mystery, limiting scientists’ understanding of the critical final phase of proteasome assembly.

Tomko’s group found that the answer to this puzzle has to do with a strange feat of molecular contortion. When a proteasome is nearly finished assembling, it temporarily changes its shape, making room for the chaperone protein as the proteasome’s final building blocks are linked together. When assembly is complete, the proteasome suddenly snaps back into its original shape, crowding out the chaperone protein and eventually popping it entirely free.

“This finding explains how this seemingly impossible process happens, and importantly, it suggests that by controlling it, we could regulate proteasome assembly to help treat certain types of cancers,” Tomko said.

Cancer cells, just like healthy cells, rely on proteasomes to collect and dispense with toxic proteins. Because cancer cells produce large amounts of damaged proteins, they compensate by overproducing proteasome assembly chaperones, which build more proteasomes to meet the cancer cells’ needs. These fleets of diligent proteasome cleanup crews keep the cancer cells from self-destructing and allow them to propagate more effectively.

In addition, the specific chaperone protein Tomko and his team studied, called gankyrin, is an oncogene — a piece of genetic material that is present at elevated levels in some tumors and has been shown to promote cancer growth.

Tomko said that if scientists can devise a way of interfering with the “popping off” of gankyrin chaperone proteins from assembling proteasomes, they may be able to mitigate the cancer-causing effects of gankyrin while also condemning harmful cancer cells to death by their own toxic proteins.

“First, we can trap gankyrin and prevent it from performing its pro-cancer functions,” he said. “Second, by trapping gankyrin and preventing completion of proteasome assembly, we can sensitize these cancer cells to the toxic, damaged proteins they are already overproducing. Gankyrin is important for several types of cancer, including liver, colon and cervical, so this approach might help to treat cancers of multiple organ types.”

The next step, Tomko said, is to confirm that trapping gankyrin is toxic to cancer cells but nontoxic to healthy cells. If this is found to be the case, he and his team could begin developing candidate drugs for preclinical testing.

Tomko and FSU researcher Antonia Nemec spearheaded the study, with additional contributions from graduate students Randi Reed and Jennifer Warnock and FSU researcher Anna Peterson. The research was funded by the Florida State University College of Medicine and The National Institutes of Health.