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Inhibition of cytochrome P450 2B6 by Astragalus extract mixture HT042
Kim Harim,Lee Yejin,Kim Vitchan,Lee Rowoon,Bae Soo Kyung,Kwak Mi-Kyoung,Lee Sung Hoon,Kim Donghak 한국독성학회 2020 Toxicological Research Vol.36 No.3
Astragalus extract mixture (AEM) HT042 is a functional food approved by the MFDS (Korean FDA) for increasing height. It comprises a mixture of three standardized extracts from Astragalus membranaceus root, Eleutherococcus senticosus stem, and Phlomis umbrosa root. In this study, drug–functional food interaction was analyzed using six major human cytochrome P450 enzymes. The inhibitory effect of AEM HT042 on P450 activities was studied using a P450–NADPH P450 reductase reconstitution system. Among the six P450 enzymes (1A2, 2A6, 2B6, 2D6, 2C9, and 3A4), only P450 2B6 activity was markedly decreased by AEM HT042 addition. The bupropion hydroxylation activity of P450 2B6 was analyzed using ultraperformance liquid chromatography-tandem mass spectrometry (UPLC–MS/MS). A calculated IC50 value of 10.62 μg/ml was obtained. To identify the inhibitory compounds in the mixture, four active compounds in AEM HT042 were analyzed. Shanzhiside methylester exhibited inhibitory effects on P450 2B6, whereas formononetin, eleutheroside E, and sesamoside did not affect P450 2B6 activity at all. Our results suggest that shanzhiside methylester in AEM HT042 is responsible for the inhibitory effect on P450 2B6 metabolism. Characterization of the inhibitory effect on P450 can help determine the safe administration of functional foods along with many clinical drugs that are metabolized by P450.
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Past and Future Epidemiological Perspectives and Integrated Management of Rice Bakanae in Korea
Soobin Shin,류현주,Jin-Yong Jung,윤윤주,Gudam Kwon,Nahyun Lee,Na Hee Kim,Rowoon Lee,Jiseon Oh,Minju Baek,Yoon Soo Choi,Jungho Lee,김광형 한국식물병리학회 2023 Plant Pathology Journal Vol.39 No.1
In the past, rice bakanae was considered an endemic disease that did not cause significant losses in Korea; however, the disease has recently become a serious threat due to climate change, changes in farming practices, and the emergence of fungicide-resistant strains. Since the bakanae outbreak in 2006, its incidence has gradually decreased due to the application of effective control measures such as hot water immersion methods and seed disinfectants. However, in 2013, a marked increase in bakanae incidence was observed, causing problems for rice farmers. Therefore, in this review, we present the potential risks from climate change based on an epidemiological understanding of the pathogen, host plant, and environment, which are the key elements influencing the incidence of bakanae. In addition, disease management options to reduce the disease pressure of bakanae below the economic threshold level are investigated, with a specific focus on resistant varieties, as well as chemical, biological, cultural, and physical control methods. Lastly, as more effective countermeasures to bakanae, we propose an integrated disease management option that combines different control methods, including advanced imaging technologies such as remote sensing. In this review, we revisit and examine bakanae, a traditional seed-borne fungal disease that has not gained considerable attention in the agricultural history of Korea. Based on the understanding of the present significance and anticipated risks of the disease, the findings of this study are expected to provide useful information for the establishment of an effective response strategy to bakanae in the era of climate change.
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초진 당시 허혈성 시신경병증으로 오진되었던 매독성 시신경병증
Rowoon Yi,Tai Kyong Kim,Mee Yon Lee 한국망막학회 2016 Journal of Retina Vol.1 No.2
Purpose: To report a syphilitic optic neuritis case, initially misdiagnosed as arteritic ischemic optic neuropathy (AION), in which prior transient posterior placoid chorioretinitis was an important clue to the correct diagnosis. Case summary: A 50-year-old man presented with blurry vision in the right eye. Funduscopy revealed optic disc swelling. Due to an elevated erythrocyte sedimentation ratio and C-reactive protein, our initial impression was AION. However, the diagnosis was corrected after reviewing a previous fundus photo revealing a large, pale yellow placoid lesion in the macula of the right eye. Serological examinations revealed confirmed syphilis infection. After a 2-week treatment with penicillin G, visual symptoms and signs fully resolved. Conclusions: Optic neuropathy with an elevated erythrocyte sedimentation ratio and C-reactive protein should prompt suspicion for syphilitic optic neuritis. Misdiagnosis as AION could lead to steroid therapy without antibiotics, which can worsen prognosis.
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( Myung-a Cho ),( Jihoon G Yoon ),( Vitchan Kim ),( Harim Kim ),( Rowoon Lee ),( Min Goo Lee ),( Donghak Kim ) 한국응용약물학회 2019 Biomolecules & Therapeutics(구 응용약물학회지) Vol.27 No.6
Human cytochrome P450 2C9 is a highly polymorphic enzyme that is required for drug and xenobiotic metabolism. Here, we studied eleven P450 2C9 genetic variants―including three novel variants F69S, L310V, and Q324X―that were clinically identified in Korean patients. P450 2C9 variant enzymes were expressed in Escherichia coli and their bicistronic membrane fractions were prepared The CO-binding spectra were obtained for nine enzyme variants, indicating P450 holoenzymes, but not for the M02 (L90P) variant. The M11 (Q324X) variant could not be expressed due to an early nonsense mutation. LC-MS/MS analysis was performed to measure the catalytic activities of the P450 2C9 variants, using diclofenac as a substrate. Steady-state kinetic analysis revealed that the catalytic efficiency of all nine P450 2C9 variants was lower than that of the wild type P450 2C9 enzyme. The M05 (R150L) and M06 (P279T) variants showed high k<sub>cat</sub> values; however, their K<sub>m</sub> values were also high. As the M01 (F69S), M03 (R124Q), M04 (R125H), M08 (I359L), M09 (I359T), and M10 (A477T) variants exhibited higher K<sub>m</sub> and lower k<sub>cat</sub> values than that of the wild type enzyme, their catalytic efficiency decreased by approximately 50-fold compared to the wild type enzyme. Furthermore, the novel variant M07 (L310V) showed lower k<sub>cat</sub> and K<sub>m</sub> values than the wild type enzyme, which resulted in its decreased (80%) catalytic efficiency. The X-ray crystal structure of P450 2C9 revealed the presence of mutations in the residues surrounding the substrate-binding cavity. Functional characterization of these genetic variants can help understand the pharmacogenetic outcomes.
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