STANFORD, Calif. Investigators at the Stanford University School of Medicine have found a way to quickly and reversibly fine-tune the activity of individual proteins in cells and living mammals, providing a powerful new laboratory tool for identifying more precisely than ever before the functions of different proteins.
The new technique also could help to speed the development of therapies in which cancer-fighting proteins are selectively delivered to tumors.
The procedure, described in a Nature Medicine paper to be published online Sept. 28, appears to be broadly applicable to efforts to understand the biological roles of all kinds of proteins, including those that are secreted by cells. This category includes many potent intercellular signaling proteins that can influence the immune system, for example by attracting its attention to an existing tumor.
"We have yet to find a protein the system doesn't work with," said senior author Steve Thorne, PhD, an assistant professor at the University of Pittsburgh who was involved in the work while a research associate at Stanford. The work was conducted under the direction of Chris Contag, PhD, associate professor of pediatrics, of radiology and of microbiology and immunology; and Tom Wandless, PhD, assistant professor of chemical and systems biology.
This technique, which was tested in mice, involves pairing specially bioengineered proteins with a drug, aptly named Shield-1, that prevents the proteins from being degraded.
This approach stands in contrast to current ways of learning about
proteins' functions, which are largely based on impeding a cell's
production of the protein. Unfortunately, that cellular process can be
slow and cumbersome, meaning that scientists get a sluggish response to
such manipulations. In addition, current methods to perturb protein
function are either irreversible once a protein's product
|Contact: Bruce Goldman|
Stanford University Medical Center