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. 2022 Oct 17;13:1002363. doi: 10.3389/fphar.2022.1002363

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Copyright © 2022 Wang, Ali, Liu, Cheng, Wu, Saleem, Zheng, Wei, Chu, Xie, Shen and Peng.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Graphical presentation of anti-proliferative effect of quercetin along with inhibition of JAK/STAT activation in VSMCs. AngII binds to the angiotensin II type 1 receptor (AT1R), which mediates phosphorylation of JAK2, and phosphorylated JAK2 activates the inactivated form of STAT3 by phosphorylation of tyrosine residues. The phosphorylated complex activated by JAK2 and STAT3 assists STAT3 in dimerization. After dimerization of STAT3 protein, it is translocated to the nucleus, where it binds to the gene promoter, and the altered protein expression may lead to proliferation of VSMCs and consequently hypertension. Quercetin treatment inactivates the activated form of JAK2 and STAT3 by dephosphorylation as well as by blocking the dimerization of both proteins. Created with BioRender.com.