But when the expression of B23 was lowered, most of the cells moved towards apoptosis, which has already been established in previous studies, he said.
When the expression of both proteins was lowered simultaneously, D'Agostino noted, no apoptosis occurred, leading the researchers to conclude that at least in this model of in-vitro Hela cells, NSP 5a3a, working in association with B23, may have a role in apoptosis.
"Since these NSP isoforms have similar structural characteristics of known structural proteins such as spectrins, they may act as scaffolding proteins to help B23 interact with whoever it needs to interact with inside the cells," he said. A spectrin is a cytoskeletal protein that lines the intracellular side of the plasma membrane of many cell types in pentagonal or hexagonal arrangements, forming scaffolding that plays an important role in maintenance of plasma membrane integrity and cytoskeletal structure.
D'Agostino said the next step for researchers is to examine exactly how the NSP isoforms are interacting with the B23 protein. "We have an idea, but we still have to confirm it," he said.
D'Agostino added that these NSP isoforms may also have diagnostic value.
"Eventually, we have to screen different types of cancers, different grades and stages, to see if there is a difference in the expression of NSP5a3a and 5a3b, and if they have an application in the clinical field," he said. "With the 5a3a, if we see a pattern of expression when we do screenings of tissue biopsies, it could be useful as a diagnostic tool."
|Contact: Preston M. Moretz|