Kim, Seon-Hwa;Kim, Kyu-Bong;Um, So-Young;Oh, Yun-Nim;Chung, Myeon-Woo;Oh, Hye-Young;Choi, Ki-Hwan
Biomolecules & Therapeutics
/
v.17
no.3
/
pp.299-304
/
2009
Rosiglitazone maleate (RGM) is widely used for improving insulin resistance. RGM is a moderate inhibitor of cytochrome P450 2C8 (CYP2C8) and is also mainly metabolized by CYP2C8. The aim of this study was to determine whether the effect of RGM on CYP2C8 is altered by co-treatment with other drugs, and whether amlodipine camsylate (AC) changes the pharmacokinetics (PK) of RGM. Of the 11 drugs that are likely to be co-administered with RGM in diabetic patients, seven drugs lowered the $IC_{50}$ value of RGM on CYP2C8 by more than 80%. In vitro CYP2C8 inhibitory assays of RGM in combination with drugs of interest showed that the $IC_{50}$ of RGM was decreased by 98.9% by AC. In a pharmacokinetic study, Sprague-Dawley (SD) rats were orally administered 1 mg/kg of RGM following by single or 10-consecutive daily administrations of 1.5 mg/kg/day of AC. No significant changes in the pharmacokinetic parameters of RGM were observed after a single administration of AC, but the AUC and $C_{max}$ values of RGM were significantly reduced by 36% and 31%, respectively, by multiple administrations of AC. In conclusion, RGM was found to be affected by AC by in vitro CYP2C8 inhibition testing, and multiple dosing of AC appreciably changed the pharmacokinetics of RGM. These findings suggest that a drug interaction exists between AC and RGM.
Benzalkonium chloride, diazolidinyl urea, and imidazolidinyl urea are commonly used preservatives in cosmetics. Recent reports suggested that these compounds may have cellular and systemic toxicity in high concentration. In addition, diazolidinyl urea and imidazolidinyl urea are known formaldehyde (FA) releasers, raising concerns for these cosmetic preservatives. In this study, we investigated the effects of benzalkonium chloride, diazolidinyl urea, and imidazolidinyl urea on ROS-dependent apoptosis of rat neural progenitor cells (NPCs) in vitro. Cells were isolated and cultured from embryonic day 14 rat cortices. Cultured cells were treated with 1-1,000 nM benzalkonium chloride, and $1-50{\mu}M$ diazolidinyl urea or imidazolidinyl urea at various time points to measure the reactive oxygen species (ROS). PI staining, MTT assay, and live-cell imaging were used for cell viability measurements. Western blot was carried out for cleaved caspase-3 and cleaved caspase-8 as apoptotic protein markers. In rat NPCs, ROS production and cleaved caspase-8 expression were increased while the cell viability was decreased in high concentrations of these substances. These results suggest that several cosmetic preservatives at high concentrations can induce neural toxicity in rat brains through ROS induction and apoptosis.
Lee, Dong Kyu;Min, Young Sil;Yoo, Seong Su;Shim, Hyun Sub;Park, Sun Young;Sohn, Uy Dong
Biomolecules & Therapeutics
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v.26
no.6
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pp.546-552
/
2018
A comprehensive collection of proteins senses local changes in intracellular $Ca^{2+}$ concentrations ($[Ca^{2+}]_i$) and transduces these signals into responses to agonists. In the present study, we examined the effect of sphingosine-1-phosphate (S1P) on modulation of intracellular $Ca^{2+}$ concentrations in cat esophageal smooth muscle cells. To measure $[Ca^{2+}]_i$ levels in cat esophageal smooth muscle cells, we used a fluorescence microscopy with the Fura-2 loading method. S1P produced a concentration-dependent increase in $[Ca^{2+}]_i$ in the cells. Pretreatment with EGTA, an extracellular $Ca^{2+}$ chelator, decreased the S1P-induced increase in $[Ca^{2+}]_i$, and an L-type $Ca^{2+}$-channel blocker, nimodipine, decreased the effect of S1P. This indicates that $Ca^{2+}$ influx may be required for muscle contraction by S1P. When stimulated with thapsigargin, an intracellular calcium chelator, or 2-Aminoethoxydiphenyl borate (2-APB), an $InsP_3$ receptor blocker, the S1P-evoked increase in $[Ca^{2+}]_i$ was significantly decreased. Treatment with pertussis toxin (PTX), an inhibitor of $G_i$-protein, suppressed the increase in $[Ca^{2+}]_i$ evoked by S1P. These results suggest that the S1P-induced increase in $[Ca^{2+}]_i$ in cat esophageal smooth muscle cells occurs upon the activation of phospholipase C and subsequent release of $Ca^{2+}$ from the $InsP_3$-sensitive $Ca^{2+}$ pool in the sarcoplasmic reticulum. These results suggest that S1P utilized extracellular $Ca^{2+}$ via the L type $Ca^{2+}$ channel, which was dependent on activation of the $S1P_4$ receptor coupled to PTX-sensitive $G_i$ protein, via phospholipase C-mediated $Ca^{2+}$ release from the $InsP_3$-sensitive $Ca^{2+}$ pool in cat esophageal smooth muscle cells.
Kim, Mikyung;Acharya, Srijan;Botanas, Chrislean Jun;Custodio, Raly James;Lee, Hyun Jun;Sayson, Leandro Val;Abiero, Arvie;Lee, Yong Soo;Cheong, Jae Hoon;Kim, Kyeong-man;Kim, Hee Jin
Biomolecules & Therapeutics
/
v.28
no.2
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pp.137-144
/
2020
Epilepsy is a brain disorder that affects millions of people worldwide and is usually managed using currently available antiepileptic drugs, which result in adverse effects and are ineffective in approximately 20-25% of patients. Thus, there is growing interest in the development of new antiepileptic drugs with fewer side effects. In a previous study, we showed that a Rehmannia glutinosa (RG) water extract has protective effects against electroshock- and pentylenetetrazol (PTZ)-induced seizures, with fewer side effects. In this study, the objective was to identify the RG components that are responsible for its anticonvulsant effects. Initially, a number of RG components (aucubin, acteoside, catalpol, and mannitol) were screened, and the anticonvulsant effects of different doses of catalpol, mannitol, and their combination on electroshock- and chemically (PTZ or strychnine)-induced seizures in mice, were further assessed. Gamma-aminobutyric acid (GABA) receptor binding assay and electroencephalography (EEG) analysis were conducted to identify the potential underlying drug mechanism. Additionally, treated mice were tested using open-field and rotarod tests. Catalpol, mannitol, and their combination increased threshold against electroshock-induced seizures, and decreased the percentage of seizure responses induced by PTZ, a GABA antagonist. GABA receptor binding assay results revealed that catalpol and mannitol are associated with GABA receptor activity, and EEG analysis provided evidence that catalpol and mannitol have anticonvulsant effects against PTZ-induced seizures. In summary, our results indicate that catalpol and mannitol have anticonvulsant properties, and may mediate the protective effects of RG against seizures.
Kim, Kyung-Soon;Yea, Sung-Chul;Yoo, Byong-Chul;Cho, Chong-Kwan;Lee, Yeon-Weol;Yoo, Hwa-Seung
The Journal of Internal Korean Medicine
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v.32
no.1
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pp.33-42
/
2011
Background : Despite recent advances in cancer management, prognosis of ovarian cancer is poor. Anticancer effects of herbal medicine, such as Euonymus alatus Sieb, Oldenlandia diffusa (Willd.) Roxburgh, and Orostachys japonicus A. Berger, have been reported in treatment of ovarian and cervical cancers, but the systematic approaches to explain their molecular mechanism(s) have not yet been established. Objectives : To establish a basis of understanding for anti-cancer mechanisms of herbal medicine, we profiled protein expression in human ovarian and cervical cancer cells treated with the extracts from Euonymus alatus Sieb, Oldenlandia diffusa (Willd.) Roxburgh and Orostachys japonicus A. Berger. Methods : Human ovarian cancer cell line NIH:OVCAR-3, and human cervical cancer cell line HeLa were employed in the present study. Whole protein was obtained from the cells harvested at 48 hours after the treatment with herbal water-extract, and analyzed by 2DE-based proteomic approach. Results : Various changes of protein expression induced by the herbal treatment were monitored : down-regulation of molecular chaperone (calreticulin variant), glycolytic enzymes (D-3-phosphoglycerate dehydrogenase, glyceraldehyde 3-phosphate dehydrogenase and alpha-enolase), RNA processing molecules (hnRNP A2/B1), and antioxidant protein (peroxiredoxin 1). Conclusions : Repression of glycolysis has been accepted as the mechanism to increase anticancer reagent's effect. Thus, down-regulation of glycolytic enzymes by the herbal extracts suggested a possible synergistic effect of herbs in the presence of platinum-based therapeutics. In further study, as well as the synergistic effect of the herbs, it has to be further validated whether artificial regulation of hnRNP A2/B1 in ovarian cancer cells affects various cancer survival factors, since RNA processing can be interrupted by deranged expression of hnRNP subtypes, and it results in an inhibition of cancer cell growth.
The objective of the present study was to evaluate the effect of a mixed extract of three herbs, Panax Notoginseng, Rehmanniae Radix and Acanthopanacis cortex (AIF), for the treatment of horses with experimentally induced osteoarthritis. Twelve healthy male horses were included in this study. Horses were assigned to one of two groups: the AIF group (n=6) or the control group (n=6). Osteoarthritis was induced in all horses by intraarticular injection of sodium monoiodoacetate (0.12 mg/kg). Horses in the AIF group received 3 g of AIF with food daily, and those in the control group received food only. Treatment began on the day of intraarticular injection. Clinical and radiographic evaluations were performed every 2 weeks. At week 12, horses were euthanatized, and postmortem gross pathologic and histologic examinations of the middle carpal joint were performed. There were no significant differences in clinical values between the two groups. Radiographic evaluation revealed that the percentages of narrowness of joint space width in the control group were significantly higher than those in the AIF group (p<0.02). On gross pathologic examination, the mean total dimensions of articular cartilage erosions and fibrillations in the control group ($101.5{\pm}41.5mm^2$) were significantly wider than those in the AIF group ($29.3{\pm}39.7mm^2$; p<0.01). On histopathologic evaluation, significantly higher grades of staining intensity and lower empty lacunae (EL) ratios were found in the AIF group (p<0.03). The present study revealed that AIF had significant disease modifying effects in horses with experimentally induced osteoarthritis.
This study was to investigate the effect of apigenin on the bioavailability of paclitaxel after oral and intravenous administration in rats. The effect of apigenin on P-glycoprotein (P-gp), cytochrome P450 (CYP)3A4 activity was evaluated. The pharmacokinetic parameters of paclitaxel were determined in rats after oral (40 mg/kg) or intravenous (5 mg/kg) administration of paclitaxel with apigenin (0.4, 2 and 8 mg/kg) to rats. Apigenin inhibited CYP3A4 activity with 50% inhibition concentration ($IC_{50}$) of 1.8 ${\mu}M$. In addition, apigenin significantly inhibited P-gp activity. Compared to the control group, apigenin significantly increased the area under the plasma concentration-time curve (AUC, p<0.05 by 2 mg/kg, 59.0% higher; p<0.01 by 8 mg/kg, 87% higher) of oral paclitaxel. Apigenin also significantly (p<0.05 by 2 mg/kg, 37.2% higher; p<0.01 by 8 mg/kg, 59.3% higher) increased the peak plasma concentration ($C_{max}$) of oral paclitaxel. Apigenin significantly increased the terminal half-life ($t_{1/2}$, p<0.05 by 8 mg/kg, 34.5%) of oral paclitaxel. Consequently, the absolute bioavailability (A.B.) of paclitaxel was significantly (p<0.05 by 2 mg/kg, p<0.01 by 8 mg/kg) increased by apigenin compared to that in the control group, and the relative bioavailability (R.B.) of oral paclitaxel was increased by 1.14- to 1.87-fold. The pharmacokinetics of intravenous paclitaxel were not affected by the concurrent use of apigenin in contrast to the oral administration of paclitaxel. Accordingly, the enhanced oral bioavailability by apigenin may be mainly due to increased intestinal absorption caused via P-gp inhibition by apigenin rather than to reduced renal and hepatic elimination of paclitaxel. The increase in the oral bioavailability might be mainly attributed to enhanced absorption in the gastrointestinal tract via the inhibition of P-gp and reduced first-pass metabolism of paclitaxel via the inhibition of the CYP3A subfamily in the small intestine and/or in the liver by apigenin. It appears that the development of oral paclitaxel preparations as a combination therapy is possible, which will be more convenient than the i.v. dosage form.
Drug interactions with food, on occasion, lead to serious nutritional and functional changes in the body as well as alterations of pharmacological effect. It, therefore, should be necessary to take drug interactions with food into consideration for effective and safe therapeutics. Diabetes mellitus is a heterogeneous group of disorders characterzed by abnormal glucose homeostasis, resulting in hyperglycemia, and is associated with increased risk of microvascular, macrovascular, and neuropathic complications. However, the precise mechanism of diabetes mellitus remains unclear. Three basic objectives in the care of diabetic patients are maintaining optimal nutrition, avoiding hypo- or hyperglycemia and preventing complications. Laminaria japonica is a brown macroalgae which can be used as a functional diet due to high content of diatery fiber. The purpose of this study was to investigate the effect of Laminaria japonica diet on the pharmacokinetics of metformin which are frequently used in the treatment of diabetes. Diabetic rats induced by streptozotocin were employed in this study. Blood concentrations of oral hypoglycemic agent, metformin, were measured by HPLC and resultant pharmacokinetic parameters were calculated by RSTRIP. The mechanisms of drug interaction with food were evaluated on the basis of pharmacokinetic parameters such as $k_{a},\;t_{1/2},\;C_{max},\;t_{max}$, and AUC. Administration of metformin in normal and diabetic rats treated with Laminaria japonica diet showed significant decrease in AUC, $C_{max},\;and\;k_a$, and increase in $t_{max}$, compared to those with normal diet. This might result from adsortion of metformin on components of Laminaria japonica, causing delayed absorption. The oral glucose test showed that Laminaria japonica diet could lower blood glucose level probably through either inhibiting the activity of disaccharidases, intestinal digestive enzymes, or delaying the absorption of glucose. More studies should be followed to fully understand pharmacokinetic changes of metformin caused by long-term Laminaria japonica diet.
Journal of the Korean Society of Food Science and Nutrition
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v.39
no.1
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pp.8-13
/
2010
The angiotensin converting enzyme (ACE) inhibition effect of soybean protein isolate hydrolysate was studied using protease. Soybean protein isolate was hydrolysed by seven enzymes (Alcalase 2.4 L, Flavourzyme 500 MG, GC 106, Multifect Neutral, Neutrase 0.8 L, Papain 30,000 and Protamex), enzyme concentrations (0, 0.5, 1.0 and 1.5%), at various hydrolysis times (0, 1, 2, 3, 4, 5 and 6 hr) and suspension concentrations (1, 5, 7, 10 and 15%). Absorbance at 280 nm, brix and ACE inhibitory activity of soybean protein isolate hydrolysates were investigated. Absorbance at 280 nm and brix of Alcalase 2.4 L treatment were higher than other enzyme treatments. The optimum condition of hydrolysis was Alcalase 2.4 L, 1% enzyme concentration, 5% suspension concentration for 4 hr. $IC_{50}$ value of ACE inhibitory activity of soybean protein isolate hydrolysate was $79.94 {\mu}g/mL$. These results suggest that soybean isolate protein hydrolysate from Alcalase 2.4 L may be of benefit for developing antihypertensive therapeutics.
Ondansetron is a potent, highly selective 5-hydroxytryptamin $e_3$(5-H $T_3$) receptor-antagonist, for the management of nausea and vomiting induced by cytotoxic chemotherapy and radiography, and the treatment of post-operative nausea and vomiting. The purpose of the present study was to evaluate the bioequivalence of two ondansetron tablets, Zofran (Glaxo Smithcline Korea Ltd.) and Onfran (Korea United Pharmaceutical Co., Ltd.), according to the guidelines of Korea Food and Drug Administration (KFDA). Eighteen normal male volunteers, 24.39$\pm$1.69 year in age and 69.00$\pm$6.74kg in body weight, were divided into two groups and a randomized 2${\times}$2 cross-over study was employed. After one tablet containing 8mg of ondansetron was orally administered, blood was taken at predetermined time intervals and the concentrations of ondansetron in plasma were determined using HPLC with UV detector. Pharmacokinetic parameters such as AVC, $C_{max}$ and $T_{max}$ were calculated and ANOVA test was utilized for the statistical analysis of the parameters. The results showed that the differences in AUC, $C_{max}$ and T max between two tablets were 5.83%, 5.75% and -5.71%, respectively when calculated against the Zofran, tablet. The powers (1-$\beta$) for AUC, $C_{max}$ and $T_{max}$ were above 90%, above 90% and below 60%, respectively. Minimum detectable differences($\Delta$) at alpha=0.1 and 1-$\beta$=0.8 were less than 20% (e.g., 12.74% and 11.78% for AUC and $C_{max}$ respectively). But minimum detectable differences($\Delta$) at alpha=0.1 and 1-$\beta$=0.8 for $T_{max}$ were more than 20% (e.g., 34.22%). The 90% confidence intervals were within $\pm$20% (e.g., -2.73∼14.39 and -2.16∼13.67 for AUC and $C_{max}$ respectively). But 90% confidence intervals for $T_{max}$ were not within $\pm$20% (e.g., -28.71∼17.28). Another ANOVA test was conducted for logarithmically transformed AUC and $C_{max}$. These results showed that there are no significant difference in AUC and $C_{max}$ between the two formulations: The differences between the formulations in these log transformed parameters were all for less than 20% (e.g., 5.83% and 5.75% for AUC and $C_{max}$ respectively). The 90% confidence intervals for the log transformed data were the acceptance range of log 0.8 to log 1.25 (e.g., log 0.99∼log 1.15 and log 0.98∼log 1.15 for AUC and $C_{max}$ respectively). The major parameters, AUC and $C_{max}$, met the criteria of KFDA for bioequivalence although $T_{max}$ did not meet the criteria of KFDA for bioequivalence, indicating that Onfran tablet is bioequivalent to Zofrm1 tablet.t is bioequivalent to Zofrm1 tablet.m1 tablet.m1 tablet.m1 tablet.
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