CFTR is part of a family of thousands of active transporter proteins called ABC proteins. Although CFTR may share many structural features with its ABC "cousins," as Hwang calls them, it has been unclear as to whether CFTR and its cousins may work in a similar manner.
The new idea of how the CFTR utilizes ATP to carry out its function may bear a broader implication because of the evolutionary relationship between CFTR and other ABC transporter proteins. It opens up a wide variety of therapeutic possibilities for other common diseases, such as cancer, heart disease and diabetes, Hwang said, since many other ABC proteins play critical roles in those human illnesses.
"It's taken years for scientists to solve this particular puzzle about the CFTR protein," Hwang said. "Our recent study provides evidence that these ABC transporter proteins and CFTR, a chloride channel, are two peas in a pod. Mother nature employs the same structural framework with just a little bit of modification to do two totally different things. From a basic science perspective, it's a big deal."
Using electrophysiology techniques available at MU's Dalton Cardiovascular Research Center, Hwang's lab studied the opening and closing, or "gating," of the CFTR at the single-molecule level. By measuring the electrical current that reflects directly the movement of chloride ions through one single CFTR channel as it opens and closes, Hwang's lab is able to monitor the activity of a single CFTR molecule in real time.
|Contact: Michael Muin|
University of Missouri School of Medicine