• Proceedings of the Korean Nutrition Society Conference
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• 2001.11a
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• pp.52-52
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• 2001

• Proceedings of the PSK Conference
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• 2001.10a
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• pp.162-163
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• 2001

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 2000.10a
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• pp.178-180
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• 2000

• Proceedings of the Korean Nutrition Society Conference
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• 2001.05a
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• pp.311.2-311
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• 2001

• Biomedical Science Letters
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• v.23 no.2
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• pp.80-88
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• 2017

Ginkgo biloba extract (EGb 761) is a standardized extract of Ginkgo biloba leaves and has anti- atherosclerosis properties. Many patients with atherosclerosis disorders take Ginkgo biloba extracts to supplement current therapy. In addition, normal healthy individuals also take Ginkgo biloba extracts for prophylactic purposes. However, it is unknown whether supplementation of Gingko biloba extracts in healthy individuals offer a benefit. In this study, we assessed whether EGb 761 could provide beneficial effects on serum cholesterol levels in normal mice. Wild-type C56Bl/6 mice were orally administered EGb 761 at 25 mg/kg (Group 3) or 50 mg/kg (Group 4) every other day for 40 days. We found that the serum levels of HDL-cholesterol (HDL-C) were significantly increased in EGb 761 and lovastatin treated groups. Treatment with EGb 761 and lovastatin resulted in reduced serum total cholesterol and LDL-cholesterol (LDL-C) compared to control group. Serum lecithin cholesterol acyltransferase (LCAT) levels were higher in EGb 761 and lovastatin treated group compared to the control group. However, no difference was observed in serum APO A-I levels between the control group and treatment group. These results suggest that EGb 761 can increase HDL-C resulting in increased serum LCAT levels.

• The Korean Journal of Physiology and Pharmacology
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• v.24 no.2
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• pp.137-147
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• 2020

Ulcerative colitis (UC) is associated with intestinal immune imbalance and inflammatory response. Because dehydrolovastatin (DLVT), a derivative of lovastatin, has been recently shown to inhibit inflammation and relieve immune arthritis induced by chemical stimuli, we studied its effect and possible mechanism on UC induced by dextran sulfate sodium. The BALB/c mice were classified into six groups: normal control group, model group, DLVT high dose group, DLVT low dose group, salazosulfapyridine (SASP) group and lovastatin (LVT) group. The disease activity indices of UC and pathological changes were investigated. The myeloperoxidase (MPO) activity in colon tissue and inflammatory factors such as IL-6, IL-10, IL-17, and TNF-α in the serum were analyzed by ELISA, while the expression of NF-κB p65 protein in colon tissue was detected by immunohistochemistry and western blot. DLVT relieved the disease activity indices and pathological damage of the UC mice. Furthermore, DLVT significantly decreased MPO activity and improved the imbalance of inflammatory cytokines through inhibiting the expression of NF-κB p65. Meanwhile, the positive drug of SASP has a similar effect to DLVT, but the effect of DLVT in both decreasing IL-17, TNF-α, and increasing IL-10 was significantly stronger than that of SASP. These results suggest that DLVT may ameliorates the symptoms of UC.

• YAKHAK HOEJI
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• v.42 no.5
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• pp.473-479
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• 1998

Lovastatin (LOVA), a fungal metabolite isolated from cultures of Aspergillus terreus, is a competitive HMG-CoA reductase inhibitor used for the treatment of primary hyper cholesterolemia, and has also been shown to suppress growth in a variety of non-glioma tumor cell lines. A sensitive reversed-phase high-perfonnance liquid chromatographic method with ultraviolet (UV) absorbance detection has been developed to quantitate LOVA in human plasma and urine samples using liquid-liquid extraction procedure. Baseline separation of LOVA and internal standard, simvastatin was achieved on a Novapak $C_{18}$ analytical column with a mobile phase containing 0.025M $NaH_2PO_4$: CAN (35:65, v/v%), adjusted pH to 4.5. The flow rate was set at 1.5ml/min, and the column effluent was monitored by a UV detection at 238nm. The limit of quantification was determined to be 0.5${\mu}$g/ml while extraction efficiency of LOVA ranged from 73.4-82.9% at LOVA concentrations of 0.5 to 10${\mu}$g/ml. Good linearity with correlation coefficients greater than 0.999 was obtained in the range of LOVA concentrations from 0.5 to 10${\mu}$g/ml. The accuracy and the precision were proven excellent with relative standard deviation (RSD, %) and relative error (RE, %) of less than 4.2 and 4.0, respectively. Intraday precision, evaluated at five LOVA concentrations (0.5, 1, 2, 5, 10${\mu}$g/ml) and expressed as RSD ranged from 0-1.82% while the interday precision at the same concentrations ranged from 0.7-10.5%. The analytical method described was then successfully employed for the determination of LOVA concentrations in plasma samples obtained during a phase II clinical trial using high doses of LOVA (30-40mg/kg/day). This method could be further utilized for the ongoing pharmacolkinetic studies and therapeutic drug monitoring of the high-dose LOVA therapy in adenocarcinoma patients.

• Journal of Life Science
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• v.16 no.4
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• pp.598-604
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• 2006

The $Ca^{2+}-activated$ neutral protease calpain induced proteolysis has been suggested to play a role in certain cell growth regulatory proteins. Cyclin proteolysis is essential for cell cycle progression. D-type cyclins, which form an assembly with cyclin-dependent kinases (cdk4 and cdk6), are synthesized earlier in G1 of the cell cycle and seem to be induced in response to external signals that promote entry into the cell cycle. Here we show that cyclin D3 protein levels are regulated at the posttranscriptional level by calpain protease. Treatment of human breast carcinoma MDA-MB-231 cells with lovastatin and actinomycin D resulted in a loss of cyclin D3 protein that was completely reversible by the peptide aldehyde calpain inhibitor, LLnL. The specific inhibitor of the 26S proteasome, lactacystin, the lysosome inhibitors, ammonium chloride and chloroquine, and the serine protease inhibitor, phenylmethylsulfonylfluoride (PMSF), did not block the degradation of cyclin D3 by lovastatin and actinomycin D. Results of in vitro degradation of cyclin D3 by purified calpain showed that cyclin D3 protein is degraded in a $Ca^{2+}-dependent$ manner, and the half-life of cyclin D3 protein was dramatically increased in LLnL treated cells. These data suggested that cyclin D3 protein is regulated by the $Ca^{2+}-activated$ protease calpain.

• 한국생물공학회:학술대회논문집
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• 2005.04a
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• pp.138-138
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• 2005

• 대한임상약리학회:학술대회논문집
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• 1996.12a
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• pp.28-28
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• 1996