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The Effect of Galangin on the Regulation of Vascular Contractility via the Holoenzyme Reactivation Suppressing ROCK/CPI-17 rather than PKC/CPI-17

Authors
Yoon, Hyuk-JunJung, Won PillMin, Young SilJin, FanxueBang, Joon SeokSohn, Uy DongJe, Hyun Dong
Issue Date
Mar-2022
Publisher
KOREAN SOC APPLIED PHARMACOLOGY
Keywords
CPI-17; Fluoride; Galangin; MYPT1; Phorbol ester; ROCK
Citation
BIOMOLECULES & THERAPEUTICS, v.30, no.2, pp.145 - 150
Journal Title
BIOMOLECULES & THERAPEUTICS
Volume
30
Number
2
Start Page
145
End Page
150
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/151332
DOI
10.4062/biomolther.2021.087
ISSN
1976-9148
Abstract
In this study, we investigated the influence of galangin on vascular contractibility and to determine the mechanism underlying the relaxation. Isometric contractions of denuded aortic muscles were recorded and combined with western blot analysis which was performed to measure the phosphorylation of phosphorylation-dependent inhibitory protein of myosin phosphatase (CPI-17) and myosin phosphatase targeting subunit 1 (MYPT1) and to evaluate the effect of galangin on the RhoA/ROCK/CPI-17 pathway. Galangin significantly inhibited phorbol ester-, fluoride-and thromboxane mimetic-induced vasoconstrictions regardless of endo-thelial nitric oxide synthesis, suggesting its direct effect on vascular smooth muscle. Galangin significantly inhibited the fluoride-dependent increase in pMYPT1 and pCPI-17 levels and phorbol 12,13-dibutyrate-dependent increase in pERK1/2 level, suggest-ing repression of ROCK and MEK activity and subsequent phosphorylation of MYPT1, CPI-17 and ERK1/2. Taken together, these results suggest that galangin-induced relaxation involves myosin phosphatase reactivation and calcium desensitization, which appears to be mediated by CPI-17 dephosphorylation via not PKC but ROCK inactivation.
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