Telomerase Could Assist in Cure for Cancer

According to a news release, researchers at Wistar Institute who have been studying the telomerase molecule have discovered how the molecule is actually structured and how it participates in the formation of damaged cells seen in 90% of all cancers. The new findings on this molecule are published in the November 13 journal Structure and the researchers are hopeful that the new study will be beneficial in the development of medications to stop the multiplication of the cancer cells.

Since telomerase was discovered in the mid 1990's, researchers have been trying to find a way to stop this enzyme from forming, but the lack of knowledge about the structure of the molecule has been problematic. Emmanuel Skordalakes, PhD. states, "Knowing the physical structure of this complex will give pharmaceutical companies a direct target for designing drugs that disrupt a mechanism that telomerase uses to assemble itself. Such drugs could well have significant anti-cancer activity." Skordalakes is an assistant professor in the Gene Expression and Regulation Program at Wistar and he is the senior author of the study.

Telomerase is an enzyme that is important in the human cell and its function is to prevent damage and preserve gene patterns in DNA duplication. This function is needed for embryonic development, stem cells and limited other cells. However, the enzyme is almost non-functioning in healthy adults so that cells that do not need to be duplicated will not be duplicated. In an individual with cancer, the damaged cells produce telomerase, which allows them to duplicate abnormally.

In 1990, Carl Woese introduced the now accepted concept that single cells are made up of three-dimensional structures, which he called domains. One of the domains in telomerase is called the TRBD domain. It is a combination of multiple proteins and RNA (Answer.com defines this as a "polymeric constituent of all living cells") that have to interact and form a more stable substance in order for DNA to duplicate itself. "Studies show that if you delete the TRDB domain from telomerase, the enzyme is inactive because it can no longer assemble with RNA. Without the RNA, the enzyme can no longer replicate telomeres", states Skordalakes.

This research may also be helpful for the scientists who study aging and its effects. However, it is hoped that the most immediate benefit from this new information will be in the development of new medications to fight the epidemic of cancer.

The Commonwealth Universal Research Enhancement Program of the Pennsylvania Department of Health was also one of the supporters of the study.

Sources used:
Newswise.com #535205 Telomerase Enzyme Structure Provides Significant New Target for Anti-Cancer Therapies
http://www.answers.com/topic/three-domain-system

http://www.answers.com/RNA