Person: YILMAZ, BETÜL
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YILMAZ
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BETÜL
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Publication Open Access Resveratrol: French paradox revisited(FRONTIERS MEDIA SA, 2012) YILMAZ, BETÜL; Catalgol, Betul; Batirel, Saime; Taga, Yavuz; Ozer, Nesrin KartalResveratrol is a polyphenol that plays a potentially important role in many disorders and has been studied in different diseases. The research on this chemical started through the French paradox, which describes improved cardiovascular outcomes despite a high-fat diet in French people. Since then, resveratrol has been broadly studied and shown to have antioxidant, anti-inflammatory, anti-proliferative, and anti-angiogenic effects, with those on oxidative stress possibly being most important and underlying some of the others, but many signaling pathways are among the molecular targets of resveratrol. In concert they may be beneficial in many disorders, particularly in diseases where oxidative stress plays an important role. The main focus of this review will be the pathways affected by resveratrol. Based on these mechanistic considerations, the involvement of resveratrol especially in cardiovascular diseases, cancer, neurodegenerative diseases, and possibly in longevity will be is addressed.Publication Open Access Proteasomal System Related Stress Response in Different Cancer Cell Lines(MARMARA UNIV, INST HEALTH SCIENCES, 2020-12-03) YILMAZ, BETÜL; Jannuzzi, Ayse Tarbin; Arslan, Sema; Alpertunga, Buket; Yilmaz, Betul KarademirObjective: Proteasomal system is the primary protein degradation mechanism and important for cellular homeostasis. On the other hand, increased proteasome activity protects cancer cells from cell death. The objective of this preliminary study was to determine the response of the proteasomal system to oxidative stress in human cancer cell lines including K562 chronic myelogenous leukemia, U251 glioblastoma, DU145 prostate cancer, HepG2C3A hepatoma, and MCF7 breast cancer. Methods: Cells were exposed to hydrogen peroxide (H2O2) as a stressor. 20S and 26S proteasome activities and K48-linked protein ubiquitination levels were determined immediately and 3 hours after exposure. Results: As an immediate response, 20S proteasome activities decreased in only K562 and U251 cells and 20S+26S proteasome activities decreased only in K562 cells. Following 3h of incubation, all cells showed a significant decrease in both 20S and 20S+26S proteasome activities. K48-linked protein ubiquitination levels increased immediately in K562 and DU145 cells. After 3h of incubation, ubiquitination levels increased in all cell lines except MCF7 cells. Conclusion: The difference in the response of the proteasomal system to stress could be the reason for differential adaptation to oxidative stress in different cancer types.