olaparib CAS NO.763113-22-0

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Olaparib is a new oral polyadenosine polyphosphate ribose polymerase [PARP] inhibitor. PARP includes the most important members of three protein families: PARP1, PARP2 and PARP3. PARP enzymes are involved in normal cell homeostasis, such as DNA transcription, cell cycle regulation and DNA repair. The results of the olaparib in vitro test showed that monotherapy or platinum-based chemotherapeutics after the treatment showed inhibition of the growth of tumor cell lines selected by Chemicalbook and reduced tumors in human cancer mouse xenograft models Grow. After treatment with olaparib, the cytotoxicity and anti-tumor activity of the tumor model cell lines in BRCA-deficient mice with ovarian cancer were increased. In vitro experimental studies have also shown that the cytotoxicity induced by olaparib may be related to the inhibition of PARP enzyme activity and the increase of PARP-DNA complex formation, which leads to the destruction of cell homeostasis and cell death.

Olaparib is a new type of poly ADP ribose polymerase (PARP) inhibitor, including PARP1, PARP2, and PARP3. PARP mediates a DNA repair mechanism that plays an important role in DNA damage repair and cell apoptosis. Therefore, olaparib specifically acts on the DNA damage repair mechanism of targeted cells by attacking cancer cells carrying BRCA1 and BRCA2 mutations. The key loopholes of ovarian cancer play a role and can be used for the maintenance treatment of patients with breast cancer susceptibility gene (BRCA) mutations and recurrent severe ovarian cancer who are sensitive to platinum drugs. A study by scientists from the Dana-Farber Cancer Institute at Harvard Medical School in the United States has found that the site of action of olaparib is polymerase Q (POLQ, also known as POLθ). These scientists found that a large number of ovarian cancer patients with ovarian cancer have defects in the repair pathway genes of homologous recombination (HR), and the protein expression of POLQ is greatly up-regulated. HR is an important repair pathway to repair DNA broken chains. They speculate that POLQ is to make up for the lack of HR and participate in DNA repair. Experiments have shown that in cells with normal HR, knocking out POLQ will significantly increase the activity of HR; while in cells with HR missing, knocking out POLQ will cause cell death. POLQ contains RAD51 binding membrane body, which can block RAD51-mediated DNA repair. Relevant research results were published in "Nature" on February 12, 2015. Raphael Ceccaldi is the first author of the research results.