We are proud to support the development of bright, young ALS researchers through our Milton Safenowitz Postdoctoral Fellowship Program. Established in memory of Milton Safenowitz by the Safenowitz family, this impactful program has encouraged early career scientists to enter and, importantly, remain in the ALS field for the last 20 years. Today, we are shining a spotlight on one of our current fellows, Suleyman Can Akerman, Ph.D., a postdoctoral researcher at Johns Hopkins University.
Dr. Akerman’s journey to becoming an ALS researcher has taken him around the world, from academic institutions in Turkey, Switzerland, and Canada, to his current position in the lab of Dr. Jeffrey Rothstein at Johns Hopkins University in Baltimore, Maryland. But no matter where his lab equipment has been located, Dr. Akerman has been focused on untangling the underlying causes of neurodegenerative diseases to help find new ways to treat them.
Dr. Akerman has been interested in a common feature of neurodegenerative diseases since he began his undergraduate studies—a process known as protein aggregation. Proteins are important molecules that play an essential role in the structure, function, and regulation of the body. In neurodegenerative diseases like ALS, though, some proteins start to stick together in ways they usually wouldn’t. These clumps of damaged, abnormal, or misfolded proteins increase over time, interfering with normal cell functions and eventually becoming toxic.
“The fact that these proteins, usually recognized by the cell’s degradation machinery, manage to escape it and affect the physiology of their surroundings captivates me. And I believe it is key to our efforts of developing better therapies,” Dr. Akerman said.
ALS researchers have begun to suspect that disease-causing clumps of abnormal proteins might also be able to spread from cell to cell through tiny, bubble-like structures called extracellular vesicles or EVs. EVs act like tiny envelopes that help facilitate cellular communication. One cell will fill an EV envelope with various biological molecules. Then, this cellular "mail" will be delivered to and opened up by a different cell.
“Some studies suggest that the formation of EVs in ALS could be increased, which could result in further spreading of toxic protein clumps associated with the disease,” Dr. Akerman explained. It is this process that Dr. Akerman is exploring with the support of his Safenowitz Fellowship.
“What excites me most is the dual potential of EVs,” he continued. “On one hand, they may act as carriers of toxic molecules, suggesting a possible target for therapeutic intervention to slow down or perhaps even halt disease progression. On the other hand, EV cargo content could change dramatically depending on the cellular health, making them promising candidates for biomarker development.”
Dr. Akerman continues to be inspired by the “vibrant” ALS research community of which he now finds himself a part. And it is the “extensive collaboration and collective thought leadership” he’s experienced that makes him believe in a future without ALS.
“Above all, what gives me hope is the dedication of the incredible academic and industrial research community working relentlessly to not only make ALS a livable disease, but also defeat it by developing cures.”
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