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GATA: a graphic alignment tool for comparative sequence analysis

Sometimes a potential target for a drug seems very promising on paper; things are often very different in reality. Its the case of telomerase inhibitors to treat cancer; they are supposed to strip the "immortal" (able to divide indefinitely) aspect of cancer cells. Yet, something in the cell seems to block their function, preventing them to inhibit completely the telomerase. What to do then? Scrap the project? Look for something else? Hell no! Look out for whats stopping the drug! Perseverance is sometimes worth it, as we can see. A new research study published in the January issue of Cancer Cell provides exciting new information about how to boost the effectiveness of a promising cancer treatment that targets telomeres in an attempt to interfere with the ability of a cancer cell to continuously divide.

Telomeres are DNA sequences found at the ends of chromosomes that play a key role in controlling the life span of cells. With every cell division, telomeres get a bit shorter until eventually they become so short that the enzymes that copy DNA for cell division no longer work properly and the cell stops dividing. In a sense, telomeres function as a kind of counting mechanism that regulates how many times a cell can divide. In contrast to normal cells, cancer cells divide continuously and uncontrollably. Scientists know that cancer cells produce an enzyme, called telomerase, which prevents telomeres from getting too short so cells can keep dividing. Telomerase is not used by healthy cells, and has been identified as a logical target for anticancer therapeutics. However, recent studies indicate that for this therapy to be effective, telomeres must be in a critically short state, requiring an extended treatment duration that can lead to drug resistance and other problems. Dr. Hiroyuki Seimiya from the Japanese Foundation for Cancer Research in Tokyo and colleagues examined what happens to cancer cells when telomerase inhib ition is combined with inhibition of an enzyme called tankyrase 1 that is involved in making telomeres accessible to telomerase. The researchers found that both tankyrase 1 activity and telomere shortening decrease the effects of telomerase inhibitors. Importantly, tankyrase inhibition enhanced telomere shortening upon treatment with a telomerase inhibitor and accelerated cancer cell death. "This study provides insight into strategies for telomere-based molecular cancer therapeutics. We expect that inhibition of tankyrase 1 will compensate for incomplete inhibition of telomerase. Consequently, this strategy would shorten the time period of drug treatment that is required for the onset of telomere crisis and reduce the potential risk of acquired drug resistance, " writes Dr. Seimiya. Hiroyuki Seimiya, Yukiko Muramatsu, Tomokazu Ohishi, and Takashi Tsuruo: "Tankyrase 1 as a target for telomere-directed molecular cancer therapeutics".
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