• Food Science and Biotechnology
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• v.17 no.2
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• pp.247-250
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• 2008

The $CHCl_3$, EtOAc, and n-BuOH fractions showed a marked inhibition of 5% fatal bovine serum (FBS)-induced cell proliferation. The $IC_{50}$ values of the chloroform fractions from leaf, stem, and root as well as the n-BuOH and EtOAc fraction from root on cell proliferation were $1.2{\pm}0.4$, $17.2{\pm}6.4$, $81.8{\pm}33.2$, $40.8{\pm}8.0$, and $237.1{\pm}85.6\;{\mu}g/mL$, respectively. On the other hand, the EtOAc fractions, and the $CHCl_3$ fraction significantly inhibited collagen-, arachidonic acid-, U46619-, and thrombin-induced platelet aggregations. The $IC_{50}$ values of EtOAc fraction from leaf, and the $CHCl_3$ and EtOAc fraction from stem were $214.1{\pm}12.2$, $134.3{\pm}2.5$, and $42.6{\pm}7.0\;{\mu}g/mL$ with collagen, $312.4{\pm}7.5$, $158.9{\pm}1.7$, and $82.2{\pm}2.7\;{\mu}g/mL$ with arachidonic acid, $31.1{\pm}2.4$, $48.7{\pm}0.3$, and $29.7{\pm}1.1\;{\mu}g/mL$ with U46619, and $36.7{\pm}2.4$, $69.1{\pm}11.3$, and $34.2{\pm}0.1\;{\mu}g/mL$ with thrombin, respectively. Taken together, these data provide new evidence that fractions from Allium victorialis var. platyphyllum (AVP) are able to inhibit vascular smooth muscle cell (VSMC) proliferation and platelet aggregation, which may be a novel resource for the development of anti-atherothrombotic agents.

• The Korean Journal of Mycology
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• v.36 no.2
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• pp.178-182
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• 2008

Although the number of patients with Acanthamoeba keratitis has increased dramatically since the widespread use of contact lens, it is still very hard to cure the disease. The proteases from the Acanthamoeba were reported to play important role in the pathogenesis of keratitis. In this study, the inhibitors for extracellular serine proteases of A. castellanii were screened from the extracts of 230 mushroom samples collected from various regions of Korea. The mushrooms were extracted with methanol and water ($65^{\circ}C$). Filtered and concentrated extracts (0.3 mg/ml) were preincubated with proteases before addition of peptide substrate N-succinyl-ala-ala-pro-phe p-anilide. The selected extracts showing strong inhibitory effects were characterized. Although inhibition with single extract was not so high enough, the complete inhibition was achieved with combination of two extracts. The selected extract showed little effect on other serine proteases such as thrombin (human and bovine) and on general protease such as protease K.