Health
The major antioxidants in green tea can increase levels of natural anti-cancer proteins
Antioxidants in green tea can increase levels of p53, a natural anticancer protein known as the “guardian of the genome,” with its ability to repair DNA damage and destroy cancer cells. ..Released today Nature CommunicationsStudies of the direct interaction of p53 with the green tea compound epigallocatechin gallate (EGCG) represent a new target for antineoplastic discovery.
Both the p53 and EGCG molecules are very interesting. Although p53 mutations are found in more than 50% of human cancers, EGCG is the major antioxidant in green tea, a popular beverage worldwide. Now we have discovered that there is a previously unknown direct interaction between the two. This represents a new path for developing anti-cancer drugs. Our work helps explain how EGCG can enhance the anti-cancer activity of p53 and open the door to drug development with compounds like EGCG. “
Chunyu Wang, corresponding author and professor of biological sciences at Rensselaer Polytechnic Institute
Wang, a member of the Rensselaer Center for Biotechnology and Interdisciplinary Studies, is an expert in research using nuclear magnetic resonance spectroscopy. Specific mechanisms of Alzheimer’s disease And cancer containing p53, which he described as “probably the most important protein in humans.” cancer.. “
P53 contains several well-known anti-cell deaths, including arresting cell growth to allow DNA repair, activating DNA repair, and initiating programmed cell death called apoptosis when DNA damage cannot be repaired. It has a cancer function. Because one end of the protein, known as the N-terminal domain, has a flexible shape, it can perform several functions depending on how it interacts with multiple molecules.
EGCG is a natural antioxidant. That is, it helps to undo the near-constant damage caused by the use of oxygen metabolism. EGCG, which is abundant in green tea, is also packaged as an herbal supplement.
Wang’s team found that the interaction between EGCG and p53 prevented protein degradation. Normally, p53 is produced in the body and then rapidly degraded when the N-terminal domain interacts with a protein called MDM2. This regular cycle of production and decomposition keeps p53 levels low and constant.
“EGCG and MDM2 both bind to the same location on p53, the N-terminal domain, so EGCG competes with MDM2,” Wang said. “When EGCG binds to p53, the protein is not degraded via MDM2, so direct interaction with EGCG raises p53 levels, which means more p53 for anticancer function. This is a very important interaction. “”
“EGCG binds to the essentially chaotic N-terminal domain of p53 and disrupts the interaction of p53-MDM2” was published with the support of multiple grants from the National Institutes of Health. In Renseria, Lauren Gandhi, Weifa Jin, Rufen Yang, Shin Yue Liu and Yuan Yuan Xiao participated in the study.
Lead author Jing Zhao is a former member of Wang’s lab and is now a faculty member at China Agricultural University in Beijing, China. Co-lead author Alan Blaney is MD-Ph.D. A student at Upstate Medical College. The researchers also contributed from the SUNY Upstate Medical Center. University of Massachusetts Amherst. New York University; New York State University Binghamton. NYU Shanghai; and Merck Institute.
Source:
Journal reference:
Zhao, J. , et al. (2021) EGCG binds to the essentially chaotic N-terminal domain of p53 and interferes with the interaction of p53-MDM2. Nature Communications. doi.org/10.1038/s41467-021-21258-5..
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