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하현수,이세은,이현석,김길형,윤찬종,한종수,이지윤,Uy Dong Sohn 대한약학회 2017 Archives of Pharmacal Research Vol.40 No.12
Protease-activated receptors (PARs) are a familyof G protein-coupled receptors with a unique activationmechanism involving proteolytic cleavage of the extracellularN-terminal domain of the receptor. PAR2 has acontractile effect on esophageal smooth muscle. Weinvestigate the signaling pathways of the PAR2-activatingpeptide (PAR2-AP) induced contraction in cat esophagealsmooth muscle cells. The length of freshly isolated smoothmuscle cells and permeabilized cells from feline esophaguswere measured by scanning micrometry, and by confirmingmolecular basis via western blot analysis. The responses toPAR2-AP were initial and sustained contractions,depending on time. The maximum contraction of the initialphase occurred at 60 s. The PAR2-AP-induced contractionwas mediated by Gai1, Gai3, and Gaq protein activation,leading to phospholipase-c (PLC) and myosin light chainkinase (MLCK) activation. 20 kDa myosin light chain(MLC20) was phosphorylated by PAR2-AP. Rho kinase-2(ROCK-2), an activator of 17 kDa C-kinase potentiatedProtein phosphatase-1 Inhibitor (CPI-17), was increased byPAR2 receptor activation. In conclusion, PAR2-AP producedan initial contraction mediated by Gai1, Gai3, andGaq protein activation, resulting in PLC and MLCKactivation. The sustained contraction by PAR2-AP wasmediated by the Rho/Rho kinase-dependent pathway.