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New Cancer Drugs on the Anvil After Enzyme Code Cracked
Other scientists who reviewed the study hailed it as a breakthrough in fundamental cancer biology, but cautioned that much work remained before the exploit could be translated into next-generation therapies.
The enzyme, called telomerase, "is an ideal target for chemotherapy because it is active in almost all human cancer tumours, but inactive in most normal cells," said Emmanuel Skordalakes, a professor at the Wistar Institute in Philadelphia who led the study.
"That means that a drug that deactivates telomerase would likely work against all cancers, with few side effects."
In humans, telomerase adds short sequences of DNA known as telomeres to the ends of chromosomes, thus preventing damage and the loss of genetic information when cells divide.
The enzyme is active mainly in cells that multiply frequently, such as embryonic stem cells, but is switched off in normal adult cells to avoid problems caused by runaway cell proliferation.
In cancer cells, however, telomerase is activated, allowing the disease cells to replicate endlessly and achieve what scientists call "cellular immortality," the hallmark of all cancers.
A decade-long search for telomerase inhibitors has, up to now, been hampered by a lack of knowledge of how the enzyme is structured.
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