Identification of Three Competitive Inhibitors for Membrane­Associated, $Mg^{2+}-Dependent$ and Neutral 60 kDa Sphingomyelinase Activity

Kim Seok Kyun; Jung Sang Mi; Ahn Kyong Hoon; Jeon Hyung Jun; Lee Dong Hun; Jung Kwang Mook; Jung Sung Yun; Kim Dae Kyong

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자료유형: 학술저널

저자정보: Kim Seok Kyun (Department of Environmental & Health Chemistry, College of Pharmacy, Chung-Ang University) Jung Sang Mi (Department of Environmental & Health Chemistry, College of Pharmacy, Chung-Ang University) Ahn Kyong Hoon (Department of Environmental & Health Chemistry, College of Pharmacy, Chung-Ang University) Jeon Hyung Jun (Department of Environmental & Health Chemistry, College of Pharmacy, Chung-Ang University) Lee Dong Hun (Department of Environmental & Health Chemistry, College of Pharmacy, Chung-Ang University) Jung Kwang Mook (Department of Environmental & Health Chemistry, College of Pharmacy, Chung-Ang University) Jung Sung Yun (Department of Environmental & Health Chemistry, College of Pharmacy, Chung-Ang University) Kim Dae Kyong (Department of Environmental & Health Chemistry, College of Pharmacy, Chung-Ang University)

저널정보: 대한약학회 Archives of pharmacal research : a publication of the Pharmaceutical Society of Korea Archives of pharmacal research : a publication of the Pharmaceutical Society of Korea 제28권 제8호

발행연도: 2005.1

수록면: 923 - 929 (7page)

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Methanol extracts of domestic plants of Korea were evaluated as a potential inhibitor of neutral pH optimum and membrane-associated 60 kDa sphingomyelinase (N-SMase) activity. In this study, we partially purified N-SMase from bovine brain membranes using ammonium sulfate. It was purified approximately 163-fold by the sequential use of DE52, Butyl-Toyopearl, DEAE-Cellulose, and Phenyl-5PW column chromatographies. The purified N-SMase activity was assayed in the presence of the plant extracts of three hundreds species. Based on the in vitro assay, three plant extracts significantly inhibited the N-SMase activity in a time- and concentration-dependent manner. To further examine the inhibitory pattern, a Dixon plot was constructed for each of the plant extracts. The extracts of Abies nephrolepis, Acer tegmentosum, and Ginkgo biloba revealed a competitive inhibition with the inhibition constant (Ki) of $11.9 {\mu}g/mL,\;9.4{\mu}g/mL,\;and\;12.9{\mu}g/mL$, respectively. These extracts also inhibited in a dose-dependent manner the production of ceramide induced by serum deprivation in human neuroblastoma cell line SH-SY5Y.

#Neutral sphingomyelinase #Abies nephrolepis #Acer tegmentosum #Ginkgo biloba #Sphingomyelinase inhibitor

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