• Biomedical Science Letters
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• v.14 no.4
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• pp.249-255
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• 2008

In this study we investigated the biological activities of Crataegi Fructus, including antioxidative, fibrinolytic, $\alpha$-glucosidase inhibitory, and thrombin inhibitory activities. Crataegi Fructus, hot water extract was fractionated into hexane, $CHCLl_3$, ethyl acetate, butanol, and water fractions, and each of these was assayed individually. The water fraction showed the highest extraction yield at 4.08% (w/w). The antioxidative activities of the water, ethyl acetate, and butanol fractions were 31.07%, 45.87%, 50.28%, and 91.74%, respectively. Assays for fibrinolytic activity indicated that only the butanol fraction has significant efficacy at 1.93 plasmin units/ml. Thrombin inhibitory assays indicated that the 10-fold dilutions of the $CHCLl_3$, ethyl acetate, and butanol fractions had inhibitory activities of 34.97%, 41.43%, and 58.10%, respectively. The 10-fold dilutions of the only ethyl acetate fraction demonstrated $\alpha$-glucosidase inhibitory activities of 75.07%. From the above results, we propose that extracts of Crataegi Fructus can be used as a material for the development of biofunctional foods.

• Journal of Physiology & Pathology in Korean Medicine
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• v.16 no.5
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• pp.1060-1065
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• 2002

LC20 phosphorylation and PKC α play an important role in modulation of contractile activity of smooth muscle. Besides, myosin phosphatase is also related with smooth muscle contraction in signaling pathways. We previously demonstrated that Crataegi Fructus inhibited phenylephrine-induced contraction and which might be implicated in nitrite formation(Son et al., 2002). In this study, we investigated the effects of butanol fraction of Crataegi Fructus(BFFC) on the localization of α-protein kinease C(PKC α) and myosin phosphatase subnits(MPs) in freshly isolated single ferret potal vein cells, and phosphorylation of LC20 during phenylephrine stimulation. In PKC α and MPs localization, BFFC blocked its translocation from the cytosol to the cell membrane by treatment of phenylephrine. BFFC have also dephosphorylated LC20 phosphorylation by phenylephrine stimulation under basal level, but no significant. These results indicate that the relaxation effect of BFFC is associated with inhibition of PKC α activation and MPs dissociation, and thus myosin phosphatase activity may be increased.

• Journal of Physiology & Pathology in Korean Medicine
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• v.17 no.2
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• pp.461-466
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• 2003

The primary mechanism of smooth muscle contraction is phosphorylation of the 20 kDa myosin light chains(LC20) by a myosin light chain kinase(MLCK). Relaxation, then, is generally the result of dephosphorylation of LC20 by myosin phosphatase(MP). Changes in MP activity is one of the important mechanisms in the regulation of Ca2+-sensitivity. Inhibition of MP activity is linked to an increase in phosphorylated myosin light chain(MLC) without an increase in [Ca/sup 2+/]i-levels. It is now generally accepted that Rho-kinase phosphorylates 130 kDa regulatory and myosin binding subunits(M130, MYPT) of MP, which results in an inhibition of MP activity. In addition Rho-kinase can also directly phosphorylate MLC. In the present study, LC20 phosphorylation and MP subunits translocation to the cell membrane were investigated in freshly isolated ferret portal vein smooth muscle single cells treated with PGF2α. We also examined the effect of Y27632(10-5mol/L), Rho-kinase inhibitor, in the MP subunits localization to compare with butanol fraction of Fructus Crataegi in its effect. Butanol fraction of Fructus Crataegi(BFFC; 1㎎/㎖) was more effective in PGF2α induced contraction than those of phenylephrine in its vasodilation effect. It significantly(P<0.05) dephosphorylated the LC20 at time indicated. In addition, the dissociation of subunits are inhibited by BFCF treatment. The results indicate that, in the smooth muscle cells, the relaxation effect of BFFC is associated with increase of MP activity based on inhibition of dissociation of the catalytic and targeting subunits of the phosphatase, and thus decrease the sensitivity of LC20 phosphorylation for Ca/sup 2+/.

• The Korean Journal of Food And Nutrition
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• v.25 no.4
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• pp.897-902
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• 2012

The purpose of this study is to determine the possibility of using Crataegi fructus as natural health food source. The research was conducted to determine the biofunctional activities of Crataegi fructus extract. Methanolic extract from Crataegi fructus was partitioned by using organic solvents, including n-hexane, ethyl acetate, n-butanol, and water. Ethyl acetate soluble fraction was shown to have the strongest antioxidant activity ($RC_{50}=4.39{\mu}g/m{\ell}$) among the fractions. In the antimicrobial activity assays, ethyl acetate soluble fraction was effective in bacterial inhibition, against the cases of Escherichia coli and Klebsiella pneumonia, with minimum inhibitory concentrations in $125{\mu}g/m{\ell}$. In the anticomplementary activity assays, water soluble fraction was the most effective exhibiting 18.4% inhibitory activity.