Health
Saskatchewan, US researchers discover protein could lead to improved cancer treatment
A team of researchers from universities in Saskatchewan, Wisconsin and Oregon has made a major breakthrough that could improve cancer treatments in the future.
Oleg Dmitriev is a professor in the Department of Biochemistry, Microbiology and Immunology at the University of Saskatchewan, where his lab focuses on the regulation of copper and iron in cells.
Iron is essential for a variety of roles, including helping blood carry oxygen around the body, but iron and copper also have a dark side, Dmitriev said.
“In their free state, they can generate reactive oxygen species,” says Dmitriev, “which are very harmful small molecules that indiscriminately attack everything in their path inside the cell, ultimately causing cell death. This means that the flow of iron and copper inside the cell must be tightly controlled.”
Dmitriev says iron is a good target for research because cancer cells depend on it to grow rapidly.
“The question then is whether we can disrupt iron metabolism, the distribution and flux of iron within cells, to unleash the destructive power of the iron atom and selectively kill cancer cells.”
The team found that a specific cellular protein marker with the catchy name ERBB2-driven cell motility mediator 1 (MEMO1) binds iron and regulates its flow in and out of cells. MEMO1 also appears at high levels in lung and prostate cancer samples, but is most highly expressed in triple-negative breast cancer cells.
“This is very interesting from a medical point of view, because this is a very difficult type of cancer to treat,” Dmitriev said.
“Lung cancer is also a high-mortality cancer, so it's a potentially very important area of medical importance. And then there's prostate cancer. So those three types of cancer are produced at very high levels.”
Using the Canadian Light Source, the researchers were able to map the protein at an atomic level.
“We used CLS to solve the high-resolution structure. In other words, [to] “We can get a molecular snapshot of what the protein looks like at the atomic level, and exactly where iron and copper are bound in the protein,” Dmitriev says.
Dmitriev hopes that by mapping the cellular protein MEMO1, new drugs may be developed to target it.
“It is certainly possible to use the structure of this protein to fit the puzzle pieces together and find small molecules that fit the structure of this protein so that, for example, it cannot take part in interactions with other proteins,” he said.
“But we can also target other unrelated proteins that are only needed when MEMO1 is produced in large amounts in cancer cells. This is very specific because it attacks cancer cells where MEMO1 is present in very large amounts, while leaving normal cells unaffected.”
According to the Canadian Cancer Society, two in five Canadians will be diagnosed with cancer in their lifetime and one in four will die from the disease. Current treatments are effective but toxic and leave negative effects on patients.
Dmitriev hopes that targeting MEMO1 may lead to the development of new cancer treatments with fewer adverse reactions.
“This would allow us to use much lower doses of anti-cancer drugs, which would kill the cancer cells but not have as much effect on healthy cells.”
The article was published in May in the online journal Elife.
Dmitriev says continued research on this topic will evaluate the role of copper in the MEMO1 protein.
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