A study shows new method of inhibiting cancer genes

Researchers at the University of Illinois at Chicago have discovered a new way to stop the mutations in nearly 30% of cancer patients through recombinant human proteins. Gene mutations in the RAS family of proteins are present in nearly 90% of pancreatic cancer patients and are also prevalent in patients with colon, lung and melanoma (the most dangerous skin cancer). The histone consists of three members: K-RAS, H-RAS and N-RAS.

The prevalence of RAS mutations in human cancers and the dependence of RAS on tumor survival make RAS a major target for cancer research and drug discovery. Scientists and drug developers have long sought RAS oncogene to find a new way to treat cancer, but they have yet to find a drug that can safely inhibit the activity of oncogenes.

A team led by John O'Bryan, an associate professor of pharmacology at the University of Chicago School of Medicine, took a different approach to RAS and found that a synthetic binding protein called NS1 monobody which they synthesized in the laboratory can block the activity of RAS protein.

"We did not find a drug or a specific inhibitor," says O'Bryan, a member of the University of Illinois Cancer Center, who met at the Jesse Brown VA Medical Center in Chicago, "We use monoclonal antibody technology, a protein engineering technique, to identify regions of RAS that are critical to its function. Unlike traditional antibodies, which do not rely on their environment and can easily be used as inhibitors of gene coding Agent."

"The beauty of this technique is that when a mAb binds to a protein, it's usually acting as an inhibitor of the protein," he said. The monoclonal antibody was developed by Shohei Koide, a professor of biochemistry and molecular pharmacology at New York University and co-author of the study. They are used for different proteins, including enzymes and receptors.

The researchers found that NS1 monobody binds to a region of the RAS protein molecule that is not previously thought to be important for carcinogenic activity. NS1 strongly inhibits carcinogenic K-RAS and H-RAS by blocking the ability of the protein to interact with another identical protein to form a molecule. NS1 does not affect gene N-RAS.

O'Bryan said these findings of biology and chemistry published in The Wall Street Journal provides important insight into the long-standing problem of RAS protein function in cells. These insights can help to guide the development of new methods of treating cancer by interfering with cancer cell mutations in RAS function.

"Developing an effective RAS inhibitor represents a holy grail in cancer biology," O'Bryan said. "We now have a powerful tool that we can use to further investigate RAS functions. Although these findings will require much research and effort to be used outside of the laboratory, this study provides new insights on how RAS slows down tumor growth." Flarebio offers recombinant proteins of good quality like recombinant Phex.