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Oncologists could gain therapeutic advantage by targeting telomere protein

NA during replication and signaled the cell to stop its growth cycle if damage was detected. That role is not supported by this current research, and it has become evident that Rad9 directs the repair of DNA damage instead, according to Pandita,.

"We saw that Rad9 stabilizes telomeres, and because we aren't yet sure how it does it, we will continue to study how Rad9 influences the telomere structure," Pandita says. "We speculate that without Rad9, some of the other proteins associated with the telomeric structure become delocalized, exposing the DNA at the ends of chromosomes."

In addition to being able to enhance radiosensitization of cancerous tissues by inactivating Rad9, the researchers would like to be able to identify people with mutations in Rad9 because such mutations could predispose a person to cancer.

"If Rad9 isn't functioning properly in cells, it can lead to genomic instability and result in the malignant transformation of cells," Pandita says. "In fact, fusions at the telomeric ends of chromosomes like those seen in the absence of Rad9 appear frequently in tumor tissues."

The study's findings place Rad9 at an important juncture: its function is vital to the health of cells, and this makes it a key vulnerability to exploit for cancer therapy.


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Contact: Gwen Ericson
ericsong@wustl.edu
314-286-0141
Washington University School of Medicine
16-Feb-2006


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