Advertise With UsAdvertise on our extensive network of industry websites and newsletters.
Get the PBR newsletterSign up to our free email to get all the latest PBR
news.Scientists from the University of North Carolina at Chapel Hill School of Medicine and the UNC Lineberger Comprehensive Cancer Center have identified a protein that may inhibit cellular movement, or migration, a key factor in cancer proliferation.
Subscribe to our email newsletter
Cell migration belongs to the most rudimentary of cellular functions that allow processes such as fetal development, new blood vessel formation and wound healing to occur in humans. Increased tumor cell migration also is one of the hallmarks of highly aggressive, rapidly spreading cancer tumors.
The protein, CIB1, or calcium and integrin-binding protein 1, was originally discovered at UNC in 1997 as a blood platelet protein that may play a role in clotting. The new study indicates that CIB1 inhibits cell migration by binding to and activating a protein called PAK1, or p21-activated kinase, in cancer cells. When CIB1 activates PAK1, this kinase then inhibits cell migration by adding a phosphate group to a host of other proteins in the cell.
Thus, the study suggests that CIB1 may be a likely target for new drug development aimed at decreasing tumor metastasis, or spread, throughout the body.
In illustrating the role that CIB1 plays in cell migration and PAK1 activation, the authors used a new method known as RNAi or RNA interference to knock down or reduce CIB1 expression in various cell lines. Cells with less CIB1 had less PAK1 activation and migrated faster. The authors also showed that the more CIB1 these cells had, the less likely they were to move.
“Our study of CIB1 is still very much in its early days, but its role in migration is already very clear,” said Dr Leslie Parise, UNC professor of pharmacology, member of UNC Lineberger and the study’s senior author.