@article{APS7811,
author = {Wen Liu and Zhi-juan Song and Nian-ci Liang and Ji She and Li-er Mo},
title = {Inhibitory effects of sodium quercetin monosulfate on pig platelet aggregation induced by thrombin},
journal = {Acta Pharmacologica Sinica},
volume = {20},
number = {7},
year = {2016},
keywords = {},
abstract = {AIM: To study the inhibitory effects of sodium quercetin monosulfate (SQMS) on pig platelet aggregation induced by thrombin.
METHODS: Platelet aggregation was analyzed by turbidimetry. Cytosolic free calcium concentration ([Ca2+]i) was determined by Fura-2 fluorescence. Activity of protein kinase C (PKC) was assayed by incubating PKC with histone III S and [gamma-32 P] ATP. The cytoskeletal proteins were precipitated by Triton X-100 and separated by SDS-PAGE.
RESULTS: SQMS inhibited the platelet aggregation induced by thrombin 500 U.L-1 with IC50 132 (50-347) mumol.L-1. SQMS inhibited Ca2+ influx in blood platelets induced by thrombin 500 U.L-1 in the presence of extracellular Ca2+ 1 mmol.L-1 with IC50 20 (9-46) mumol.L-1; SQMS inhibited the internal Ca2+ release in the absence of extracellular Ca2+. SQMS also decreased [Ca2+]i level in quiescent blood platelets. SQMS (10-160 mumol.L-1) inhibited the activity of cytosolic PKC from blood platelets in a concentration-dependent manner, but had no effect on membrane PKC. SQMS (20-80 mumol.L-1) inhibited the actin polymerization induced by thrombin 500 U.L-1 inblood platelets in a concentration-dependent manner.
CONCLUSION: SQMS inhibited pig platelet aggregation induced by thrombin and its mechanism might be due to its inhibitions of Ca2+ influx, internal Ca2- release, PKC activity, and actin polymerization.},
issn = {1745-7254}, url = {http://www.chinaphar.com/article/view/7811}
}