Kim, Hyeon-Jong;Choi, Sang-Mook;Ku, Young;Rhyu, In-Chul;Chung, Chong-Pyoung;Han, Soo-Boo;Lee, Yong-Moo
Journal of Periodontal and Implant Science
/
v.32
no.2
/
pp.389-402
/
2002
BMP can induce ectopic bone formation when implanted into sites such as rat muscle and can greatly enhance healing of bony defects when applied exogenously. In addition, BMP stimulated osteoblastic differentiation in vitro in various types of cells. The aim of this study was to investigate the effect of recombinant human bone morphogenetic protein(rhBMP-2) on the proliferation and osteoblastic differentiation of human periodontal ligament cells and gingival fibroblasts. The cell number and alkaline phosphatase activity were measured in 3 experimental groups of human periodontal ligament cells and gingival fibroblasts (control group, rhBMP-2 50ng/ml group, and rhBMP-2 100ng/ml group) at 1 and 2 weeks after culture. At the same time, total RNA of cultured cells were extracted and reverse trascription polymerase chain reaction(RT-PCR) was performed to determine the expression of mRNA of bone matrix protein. RhBMP-2 had no effect on the cell proliferation of human periodontal ligament cells and gingival fibroblasts. Alkaline phosphatase activity was elevated significantly by rhBMP-2 in both cells. And periodontal ligament cells showed significantly higher alkaline phosphatase activity than gingival fibroblasts. ${\beta}$-actin, type I collagen, alkaline phosphatase, BMP-2 mRNA were expressed in all of the samples. Osteopontin, osteocalcin mRNA were expressed in all periodontal ligament cell groups, and rhBMP-2 50ng/ml group, rhBMP-2 100ng/ml group of 2 week culture period of gingival fibroblasts. Bone sialoprotein mRNA was only expressed in rhBMP-2 50ng/ml group and rhBMP-2 100ng/ml group of 2-week culture period. These results suggest that rhBMP-2 stimulates osteoblastic differentiation in human periodontal ligament cells and gingival fibroblasts in vitro.
Park Young Jun;Jung Woo Cheal;Jeong Dae Young;Lee Yong Un;Lee In;Lee Key Sang;Jeon Byung Hun;Sung Kang Keyng;Moon Byung Soon
Journal of Physiology & Pathology in Korean Medicine
/
v.17
no.6
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pp.1383-1392
/
2003
Apoptosis is a morphologically and biochemically district form of cell death that occurs in many different cell types in a wide variety of organisms. Albizzia julibrissin belonging the family Leguminosae has been used for the treatment of contusion, sore throat, amnesia, and insomnia in oriental traditional medicine. This study investigates whether the water extract of A. julibrissin induce apoptotic cell death in Jurkat T-acute lymphoblastic leukemia (ALL) cells. Jurkat cells were increased inhibitions of cell viability in a concentration-dependent manner by A. julibrissin. This herbal medicine also caused apoptosis as measured by cell morphology and DNA fragmentation. The capability of A. julibrissin to induce apoptosis was associated with proteolytic cleavage of specific target proteins such as poly (ADP-ribose)polymerase (PARP) and beta-catenin proteins suggesting the possible involvement of caspases. Our result showed that Bcl-2 and Bax protein levels were not changed in all A. julibrissin-treated groups compared to control group. These results suggest that A. julibrissin-mediated apoptosis is independent with Bcl-2 related signaling pathway in this cells. The purpose of the present study is also to investigate the Effect of A. julibrissin on cell cycle progression. Our results showed that G1 checkpoint related gene products (cyclin D1, cyclin dependent kinase 4, retinoblastoma, E2F1) were decreased in their protein levels in a dose-dependent manners after treatment of the extract. These results indicate that the increase of apoptotic cell death by A. julibrissin may be due to the inhibition of cell cycle progression in wild type p53-lacking Jurkat cells.
Kim, Young-Il;Hwang, Seong-Ju;Yoo, Han-Ill;Choy, Jin-Ho
The Korean Journal of Ceramics
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v.4
no.2
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pp.95-98
/
1998
We have developed new type of superconducting-superionic conducting nanohybrids, $Ag_xI_wBi_2Sr_2Ca_{n-1}Cu_nO_y$ (n=1 and 2) by applying the chimie douce reaction to the superconducting Bi-based cuprates. These nanohybrids can be achieved by the stepwise intercalation whereby the $Ag^+$ ion is thermally diffused into the pre-intercalated iodine sublattice of $IBi_2Sr_2Ca_{n-1}Cu_nO_y$. According to the X-ray diffraction analysis, the Ag-I intercalates are found to have an unique heterostructure in which the superionic conducting Ag-I layer and the superconducting $IBi_2Sr_2Ca_{n-1}Cu_nO_y$ layer are regularly interstratified with a remarkable basal increment of ~7.3$\AA$. The systematic XAS studies demonstrate that the intercalation of Ag-I accompanies the charge transfer between host and guest, giving rise to a change in hole concentration of $CuO_2$ layer and to a slight $T_c$ change. The Ag K-edge EXAFS result reveals that the intercalated Ag-I has a $\beta$-AgI-like local structure with distorted tetrahedral symmetry, suggesting a mobile environment for the intercalated $Ag^+$ ion. In fact, from ac impedance analyses, we have found that the Ag-I intercalates possess a fast ionic conductivity ($\sigma_i=10^{-1.4}\sim 10^{-2.6}\Omega^{-1}\textrm{cm}^{-1}\;at\;270^{\circ}C$ with an uniform activation energy ($\DeltaE_a=0.22\pm 0.02$ eV). More interesting finding is that these intercalates exhibit high electronic conducting as well as ionic ones ($t_i$=0.02~0.60) due to their interstratified structure consisting of superionic conducting and superconducting layers. In this respect, these new intercalates are expected to be useful as an electrode material in various electrochemical devices.
Crystal structural analyses of the API-TLCK complex revealed that the ${\epsilon}$-amino group (NZ) of the lysyl part of TLCK forms hydrogen bonds with OD1 of $Asp^225$ which is a substrate specificity determinant of API, OG of $Ser^214$, O of $Ser^214$, OG1 of $Thr^189$, and O of $Thr^189$ l89/. The ${\beta}$-carboxyl oxygen of $Asp^225$ forms hydrogen bonds with the NE1 of $Trp^182$. From these observations, it is thought that besides $Asp^225$, $Thr^189$, $Ser^214$, and $Trp^182$ may also contribute to the steric specificity for lysine and high proteolytic activity of API. The side-chain hydroxyl groups of $Thr^189$ and $Ser^214$ were removed to elucidate the role of these hydrogen bonds in the $S_1$-pocket. The $k_{cat}$/$K_m$ of T189V, S214A, and T189V.S214A were decreased to 1/4, 1/3, and 1/46, respectively, of the value for native API. The decreased activities were mainly due to the increase of $K_m$. The CD and fluoroscence spectra of the three mutants were similar to those of wild-type API. With regards to the kinetic parameters ($K_i\;and\;k_2$) of mutants for the reaction involving TLCK and DFP, $k_2$decreased by increase of $K_1$ only. These results suggest that the decreased catalytic activity of these mutants is caused by the partial loss of the hydrogen bond network in the $S_1$-pocket. On the other hand, the similarity of enzymatic properties between W182F and the native enzyme suggests that the hydrogen bond between OD2 of $Asp^225$ and NE1 of $Trp^182$ is not directly related to the reaction of $Asp^225$ with the substrate.
Proliposomal patch of clenbuterol, ${\beta}_2-agonist$ bronchodilator, was prepared and its feasibility as a novel transdermal drug delivery system was examined. Proliposomal granules containing clenbuterol was prepared by a standard method using sorbitol and lecithin with (Rx 2) or without cholesterol (Rx 1). The porous structure of sorbitol in the proliposomes was maintained allowing tree flowability of the granules. Following contact with water, the granules were converted probably to liposomes almost completely within several minutes. It indicates that proliposomes may be hydrated, when they are applied on the skin under occlusive condition in vivo, by the sweat to form liposomes. Clenbuterol release from Rx 1 and Rx 2 proliposomes to pH 7.4 isotonic phospate buffer (PBS) across cellulose membrane (mol. wt. cut-off of 12000-14000) was retarded significantly compared with that from the mixture of clenbuterol powder and blank proliposomes. Interestingly, proliposomes prepared with lecithin and cholesterol (i.e., Rx 2 proliposomes) showed much more retarded release of clenbuterol than proliposomes prepared only with lecithin (i.e.. Rx 1 proliposomes), indicating that clenbuterol release from proliposomes can be controlled by the addition of cholesterol to the proliposomes. Proliposomal patches were prepared using PVC film as an occlusive backing sheet, two sides adhesive tape (urethane, 1.45 mm thickness) as a reservoir for proliposome granules and Millipore MF-membrane (0.45 mm pore size) as a drug release-controlling membrane. Rx 1 or Rx 2 proliposomes containing 4.6 mg of clenbuterol were loaded into the reservoir of the patch. Clenbuterol release from the patches to pH 7.4 PBS was determined using USP paddle (50 rpm)-over-disc release method. Clenbuterol release from the proliposomal patches was much more retarded even than from a matrix type clenbuterol patch (Boehringer Ingelheim ltd). Being consistent with clenbuterol release from the proliposomal granules, the release from the patches was highly dependent on the presence of cholesterol in the proliposomes : Patches containing Rx 2 proliposomes showed several fold slower drug release than patches containing Rx 1 proliposomes. When the patch containing Rx 1 proliposomes was applied on to the back of a hair-removed rat, clenbuterol concentration in the rat blood was maintained during 6-72 hrs. Transdermal absorption of clenbuterol from the patch was accelerated when the patch was prehydrated with 50 ml of pH 7.4 PBS before topical application. Above results indicate that sustained transdermal delivery of clenbuterol is feasible using proliposomal patches if the cholesterol content and pore size of the release rate-controlling membrane of patches, for example, are appropriately controlled.
Human embryonic stem (ES) cells are derived from the inner cell mass of the preimplantation embryo and have the capacity to differentiate into various types of cells in the body. Hence, these cells may potentially be an indefinite source of cells for cell therapy in various degenerative diseases including neuronal disorders. For clinical applications of human ES cells, directed differentiation of these cells would be necessary. The objective of this study is to develop the culture condition for the expansion of neural precursor cells derived from human ES cells. Human ES cells were able to differentiate into neural precursor cells upon a stepwise culture condition. Neural precursor cells were propagated up to 5000-fold in cell numbers over 12-week period of culture and evaluated for their characteristics. Expressions of sox1 and pax6 transcripts were dramatically up-regulated along the differentiation stages by RT-PCR analysis. In contrast, expressions of oct4 and nanog transcripts were completely disappeared in neural precursor cells. Expressions of nestin, pax6 and sox1 were also confirmed in neural precursor cells by immunocytochemical analysis. Upon differentiation, the expanded neural precursor cells differentiated into neurons, astrocytes, and oligodendrocytes. In immunocytochemical analysis, expressions of type III ${\beta}$-tubulin and MAP2ab were observed Presence of astrocytes and oligodendrocytes were also confirmed by expressions of GFAP and O4, respectively. Results of this study demonstrate the feasibility of long-term expansion of human ES cell-derived neural precursor cells in vitro, which can be a potential source of the cells for the treatment of neurodegenerative disorders.
This study was aimed to design and formulate the moisture-activated patches containing ofloxacin and lidocaine for antibacterial and local anesthetic action. The solubility of lidocaine at $32^{\circ}C$ in various vehicles decreased in the rank order of PG $759.5{\pm}44.5\;mg/mL$ > PGL > IPM > PEG 300 > PEG 400 > Ethanol > PGMC > DGME > PGML > OA > $Captex^{\circledR}\;300$ > $Captex^{\circledR}\;200$ > water $(4.0{\pm}0.1\;mg/mL)$. Ofloxacin revealed very low solubility, which the highest solubility was obtained from PEG 400 $(18.7{\pm}6.3\;mg/mL)$ among the vehicles used. The addition of lactic acid increased the solubility of ofloxacin dramatically; the solubility at 5% lactic acid was $133.7{\pm}9.7\;mg/mL$. As $2-hydroxypropyl-{\beta}-cyclodextrin$ was added at the concentrations of 40, 80, 120, 160 and 200 mM, the solubilities of lidocaine and ofloxacin were enhanced up to three and two times, respectively, with concentration-dependent pattern. Gel intermediates for filmtype patches were prepared with mucoadhesive polymer, viscosity builders, lidocaine or ofloxacin at pH values from 5 to 7. Gels were cast onto a release liner and dried at room temperature. Dried patch was attached onto an adhesive backing layer, thus forming a patch system. Patches containing a single drug component were characterized by in vitro measurement of drug release rates through a cellulose barrier membrane. The release study was carried out at $37^{\circ}C$ using a Franz-type cell. Receptor solutions were isotonic phosphate buffers (pH 7.4). Samples $(100\;{\mu}L)$ were taken over 24 hours and quantitated by a verified HPLC method. The releases from all tested were proportional to the square root of time. The release rates were 0.9, 157.3 and $281.7\;{\mu}g/cm^{2}/min^{1/2}$ for the lidocaine patches and 19.8,37.2 and $50.7\;{\mu}g/cm^{2}/min^{1/2}$ for the ofloxacin patches at the concentrations of 0.3, 0.5 and 1 %, respectively. The release rates were dose dependent in both drug patches $(R^{2}\;=\;0.9077\;for\;lidocaine;\;R^{2}\;=\;0.9949\;for\;ofloxacin)$ and those were also thickness-dependent $(R^{2}\;=\;0.9246\;for\;lidocaine;\;R^{2}\;=\;0.9512\;for\;ofloxacin)$.
Glycoprotein hormones have a common $\alpha$-subunit that is involved in the signaling pathway together with G protein, adenylcyclase and cAMP induction; however, it is an unclear how this common structure is related to hormonal action. To determine the biological functions of the COOH-terminal amino acids in the $\alpha$-subunit of these glycoprotein hormones, a tethered-molecule was constructed by fusing the $NH_2$-terminus of the $\alpha$-subunit to the COOH-terminus of the $\beta$-subunit of equine chorionic gonadotropin (eCG). The following deletion mutants were created by PCR; Ile was inserted at position 96 to form ${\Delta}96$, Lys was substituted at position 95 to form ${\Delta}95$, His was inserted at position 93 to form ${\Delta}93$ and Tyr was substituted at position 87 to form ${\Delta}87$. Each mutant was transfected into CHO-K1 cells. Tethered-wt eCG, and ${\Delta}96$, ${\Delta}95$, and ${\Delta}93$ mutants were efficiently secreted into the medium but the ${\Delta}87$ mutant was not secreted. Interestingly, the RT-PCR, real-time PCR, and northern blot analyses confirmed that the RNA was transcribed in the ${\Delta}87$ mutant. However, the ${\Delta}87$ mutant protein was not detected in the medium or the intracellular fraction of the cell lysates. The LH- and FSH-like activities of the recombinant proteins were assayed in terms of cAMP production using rat LH/CG and rat FSH receptors. The metabolic clearance rate (MCR) was determined by injecting rec-eCG (2 IU) into the tail vein. The ${\Delta}95$ and ${\Delta}93$ mutants were completely inactive in both the LH- and FSH-like activity assays. The ${\Delta}96$ mutant showed slight activity in the LH-like activity assay. In comparison to the wild type, the activity of the ${\Delta}96$ mutant in the FSH-like activity assay was the highest among all the mutants. The MCR assay in which rec-eCG was injected showed a peak at 10 min in all the treatment groups, which disappeared 4 h after injection. These results imply a direct interaction between the receptor and the COOH-terminal region of the a-subunit. The data also reveal a significant difference in the mechanism by which the eCG hormone interacts with the rLH and rFSH receptors. The COOH-terminal region of the $\alpha$-subunit is very important for the secretion and functioning of this hormone.
Our previous study showed that transgenic (TG) pigs harboring human EPO (hEPO) gene have been shown to have reproductive disorders, including low pregnancy rates, irregular estrus cycle and low little size. To investigate these reasons, we assessed estrus behavior (standing response) and plasma $17{\beta}$-estradiol ($E_2$) level, which partly reflect reproductive function, during the estrus cycles after synchronization and superovulation by hormone treatments. Then, we analysed blood composition and expression of hEPO gene in TG pigs. Pigs were injected with PG600. After 10 days, pigs were fed with Regumate porcine for 6 days. Blood samples were collected from jugular vein. Analysis of blood composition and $E_2$ level were measured by Hemavet 950 and $E_2$ ELISA kit, respectively. And, the expression of hEPO gene in reproductive organs was quantitated by real-time RT-PCR. The percentage of estrus behavior in TG was significantly decreased. Hematocrit (HCT), hemoglobin (Hb) concentration and red blood cell (RBC) number were significantly higher in TG than wild type (WT). On the other hand, high expression of hEPO gene in TG was observed in the mammary gland as well as in the uterus. Moreover, plasma $E_2$ level was significantly higher in TG than WT. These results suggest that nonspecific expression of hEPO gene in the other organs of TG may affect blood composition and plasma $E_2$ level, thereby causing reproductive disorders.
The enzyme xylose isomerase (E.C. 5.3.1.5, XI) is responsible for the conversion of an aldose to ketose, especially xylose to xylulose. Owing to the ability of XI to isomerize glucose to fructose, this enzyme is used in the food industry to prepare high-fructose corn syrup. Therefore, we studied the characteristics of XI from Anoxybacillus kamchatkensis G10, a thermophilic bacterium. First, the gene coding for XI (xylA) was inserted into the pET-21a(+) expression vector and the construct was transformed into the Escherichia coli competent cell BL21 (DE3). The expression of recombinant XI was induced in the absence of isopropyl-thio-${\beta}$-galactopyranoside and purified using Ni-NTA affinity chromatography. The optimum temperature of recombinant XI was $80^{\circ}C$ and measurement of the heat stability indicated that 55% of residual activity was maintained after 2 h incubation at $60^{\circ}C$. The optimum pH was found to be 7.5 in sodium phosphate buffer. Magnesium, manganese, and cobalt ions were found to increase the enzyme activity; manganese was the most effective. Additionally, recombinant XI was resistant to the presence of $Ca^{2+}$ and $Zn^{2+}$ ions. The kinetic properties, $K_m$ and $V_{max}$, were calculated as 81.44 mM and $2.237{\mu}mol/min/mg$, respectively. Through redundancy analysis, XI of A. kamchatkensis G10 was classified into a family containing type II XIs produced by the genera Geobacillus, Bacillus, and Thermotoga. These results suggested that the thermostable nature of XI of A. kamchatkensis G10 may be advantageous in industrial applications and food processing.
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