• The Journal of Korean Medicine
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• v.24 no.3
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• pp.35-44
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• 2003

Objective : This study was performed to evaluate the effects of Palmijihwang-hwan (Baweidehuang-wan) and Obaeja (Galla Rhois) on the regeneration of periodontal tissue. Methods : In this study, we used MC3T3-El cells, such as osteoblast-like cell lines and human periodontal ligament fibroblasts, for experimental material. We separated each type of cells into a control group and an experimental group. In the control group, the cells were cultivated for 48 hours with distilled water and media which contained 10% fetal bovine serum (FBS) and penicillin (l00unit/ml)-streptomycin ($l00{\mu\textrm{g}}/ml$) at $37^{\circ}$ in 5% $CO_2$ gas. In the experimental group, the cells were cultivated for 48 hours with Palmijihwang-hwan extract and Obaeja extract (concentrations $1{\mu\textrm{g}}/ml,{\;}25{\mu\textrm{g}}/ml,{\;}50{\mu\textrm{g}}/ml$) under the same conditions as the control group. Investigating the regeneration of periodontal tissue was performed by evaluating proliferation, the activity of alkaline phosphatase and the synthetic ability of proteins using those cultivated cells by means of microculture tetrazolium (MTT) assay, alkaline phosphatase substrate kit and protein assay kit. Results : 1. In vitro, Palmijihwang-hwan extract increased the proliferation of MC3T3-El cells. 2. In vitro, Obaeja extract increased the activity of alkaline phosphatase and the synthetic ability of protein in MC3T3-El cells and human periodontal ligament fibroblasts depending on Obaeja extract's concentration. Conclusion : Obaeja extract can be developed as a subsidiary medicine for the regeneration of periodontal tissue. Further studies to evaluate the different concentrations the Obaeja extract and clinical trials in vivo are suggested.

• Korean Journal of Clinical Laboratory Science
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• v.43 no.1
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• pp.6-11
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• 2011

In clinical chemistry tests, the interfering substances such as hemoglobin, lipid, bilirubin, and drugs, etc. can cause the changes of test results performed by spectrophotometrical methods. We evaluated the effects of interfering substances on the test results by adding interfering substances on the samples in the 19 kinds of clinical chemistry tests such as aspartate aminotransferase, alanine aminotransferase, alkaline phosphatase, lactate dehydrogenase, gamma-glutamyltransferase, total protein, albumin, glucose, total cholesterol, total bilirubin, triglyceride, uric acid, calcium, inorganic phosphours, high density lipoprotein cholesterol, low density lipoprotein cholesterol, creatinine, blood urea nitrogen, and C-reactive protein using newly implemented automatic chemical analyzer Toshiba TBA-C8000 under the direction of CLSI EP07-A guideline. Hemolytic samples show increased concentration of total protein, aspartate aminotransferase, alanine aminotransferase, and lactate dehydrogenase and reduced concentration of total bilirubin, alkaline phosphatase by interfering effect. Hyperlipemic samples show increased concentration of total protein and alkaline phosphatase and reduced concentration of low density lipoprotein cholesterol. The samples with conjugated bilirubinemia show increased concentration of inorganic phosphours, otherwise the samples with unconjugated bilirubinemia show no interference or allowable range in the test result.

• BMB Reports
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• v.35 no.3
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• pp.283-290
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• 2002

The glycogen-associated protein phosphatase (PP1G/$R_{GL}$) may play a central role in the hormonal control of glycogen metabolism in the skeletal muscle. Here, we investigated the in vivo epinephrine effect of glycogen metabolism in the skeletal muscle of the wild-type and $R_{GL}$ knockout mice. The administration of epinephrine increased blood glucose levels from 200±20 to 325±20 mg/dl in both wild-type and knockout mice. Epinephrine decreased the glycogen synthase -/+ G6P ratio from 0.24±0.04 to 0.10±0.02 in the wild-type, and from 0.17±0.02 to 0.06±0.01 in the knockout mice. Conversely, the glycogen phosphorylase activity ratio increased from 0.21±0.04 to 0.65±0.07 and from 0.30±0.04 to 0.81±0.06 in the epinephrine trated wild-type and knockout mice respectively. The glycogen content of the knockout mice was substantially lower (27%) than that of both wild-type mice; and epinephrine decreased glycogen content in the wild-type and knockout mice. Also, in Western blot analysis there was no compensation of the other glycogen targeting components PTG/R5 and R6 in the knockout mice compared with the wild-type. Therefore, $R_{GL}$ is not required for the epinephrine stimulation of glycogen metabolism, and rather another phosphatase and/or regulatory subunit appears to be involved.

• Molecules and Cells
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• v.42 no.8
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• pp.604-616
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• 2019

Phosphoserine phosphatase (PSPH) is one of the key enzymes of the L-serine synthesis pathway. PSPH is reported to affect the progression and survival of several cancers in an L-serine synthesis-independent manner, but the mechanism remains elusive. We demonstrate that PSPH promotes lung cancer progression through a noncanonical L-serine-independent pathway. PSPH was significantly associated with the prognosis of lung cancer patients and regulated the invasion and colony formation of lung cancer cells. Interestingly, L-serine had no effect on the altered invasion and colony formation by PSPH. Upon measuring the phosphatase activity of PSPH on a serine-phosphorylated peptide, we found that PSPH dephosphorylated phospho-serine in peptide sequences. To identify the target proteins of PSPH, we analyzed the protein phosphorylation profile and the PSPH-interacting protein profile using proteomic analyses and found one putative target protein, IRS-1. Immunoprecipitation and immunoblot assays validated a specific interaction between PSPH and IRS-1 and the dephosphorylation of phospho-IRS-1 by PSPH in lung cancer cells. We suggest that the specific interaction and dephosphorylation activity of PSPH have novel therapeutic potential for lung cancer treatment, while the metabolic activity of PSPH, as a therapeutic target, is controversial.

• Journal of Plant Biotechnology
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• v.7 no.1
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• pp.27-35
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• 2005

Eighty-five different cultivars of Brassica rapa, B. juncea, B. nap us, B. carinata, B. oleracea and hexaploid Brassica collected from Bangladesh, Japan, China and Denmark were analyzed by SDS-PAGE for seed and leaf protein variations, using esterase, acid phosphatase and peroxidase isozyme analysis. Ten polymorphic bands were identified from seed protein however no identifiable polymorphic band was found in the leaf protein. Polymorphic markers clearly distinguished the different Brassica species as well as yellow sarson (YS) and brown seeded (BS) cultivars of B. rapa. The $F_1$ cross between YS and brown seeded cultivars showed the existance of all poly-morphic bands of the respective parents. The Bangla-deshi and Japanese cultivars of B. rapa differed in the amount of seed protein. In the case of isozyme analysis, esterase showed the highest number of polymorphic bands (13) followed by acid phosphatase (9) and peroxidase (5). These polymorphic markers were very effec-tive for classification of all the species studied in this experiment. In parentage tests using isozymes, the hybridity of intra-and-interspecific crosses of almost all the seedlings could be identified from their respective cross combinations. Esterase polymorphism showed a clear differentiation between YS and BS types of B. rapa. In addition, two esterase polymorphic markers were iden ified to differentiate some cultivars of B. juncea. Segregation patterns in these two esterase bands showed a simple Mendelian monohybrid ratio of 3:1 in $F_2$, 1:1 in test cross and 1:0 in back cross progenies. No polymorphic band was identified to distinguish different cultivars of the same species by acid phosphatase or peroxidase. Polymerase Chain Reaction (PCR) was carried out with seed coat color specific marker of B. juncea. The yellow seeded cultivars produced a strong band at 0.5 kb and weak band 1.2 kb. In the addition of these two specific bands, Japanese yellow-seeded cultivars expressed two more weak bands at 1.0 kb and 1.1 kb. Where the brown seeded cultivars generated a single strong band at 1.1 kb. In segregating population, the yellow seed coat color marker segregated at a ratio 15 (brown) : 1 (yellow), indicating the digenic inheritance pattern of the trait.

• Korean Journal of Community Nutrition
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• v.4 no.2
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• pp.239-247
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• 1999

Six-week-old Sprague Dawley rats were fed the diets of 20% casein or soy protein. Two weeks after the feeding, hepatocellular chemical carcinogenesis was initiated by diethylnitrosamine(DEN), and promoted by the diet containing 0.01% 2-acetylamino-fluorene(AAF) and two-thirds partial hepatectomy(PH). The animals were sacrificed at 8 weeks after the DEN injection. The area of placetal glutathione S-trnasferase(GST-P) positive foci, the activities of several enzymes in cellualr antioxidant enzyme systems and glucose 6-phosphatase were determined to investigate the mechanism of the anticarcinogenic effect by the dietary proteins. In another set of experiments, the drinking water of rats fed casein was supplemented with 1.5% inositol hexaphosphate(InsP6) to elucidate whether it has the comparable anticancer action of soy protein. The area and number of GST-P positive foci in the soy protein group were significantly(p<0.05) lower than those inthe casein group. The livers of rats fed casein showed moderate fattydegeneration and larger hyperplastic nodules than those of rats fed soy protein. In another set of experiments, the area and number of GST-P positive foci in the rats fed casein supplemented with InsP6 were not significantly different from those in the rats fed casein or soy protein. The lipid peroxidation of rats fed different protein sources showed no significant difference. Glutathione S-transferase(GST) activities were increased significantly(p<0.05) by carcinogen treatment in all dietary groups. Glucose 6-phosphatase(G6Pase) activities were decreased by carcinogen treatment, and hence showed a reverse relationship(r=-0.695, p<0.01) to the GST-P positive foci. Therefore, the activities in the rats fed casein were lower than those in the rats fed soy protein. These results suggest that the soy protein seems to be more anti-carcinogenic than casein by decreasing the preneoplastic lesion and by increasing the membrane stability but inositol hexaphosphate, a component of soy protein, may not be protective against hepatocarcinogenesis.

• BMB Reports
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• v.36 no.3
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• pp.288-293
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• 2003

Low molecular weight phosphotyrosine protein phosphatase (LMW-PTP) has been implicated in modulating the EphB1-mediated signaling pathway. In this study, we demonstrated that the EphA8 receptor phosphorylates LMW-PTP in vitro. In addition, we discovered that mixing these two proteins leads to EphA8 dephosphorylation in the absence of phosphatase inhibitors. Finally, we demonstrated that LMW-PTP, modified by the EphA8 autokinase activity, possesses enhanced catalytic activity in vitro. These results suggest that LMW-PTP may also participate in a feedback-control mechanism of the EphA8 receptor autokinase activity in vivo.

• The Korean Journal of Zoology
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• v.33 no.1
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• pp.70-77
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• 1990

The change of phosphatase activities of the epididymal spermatozoa has been examined during epididymal maturation in mouse. The quantitative analysis of phQsphatase activities have been carried out using the method modified by Emst(1975). The results of experiment were summarized as the followings. Total protein of the caput epididyrnal spermatozoa(CPS) was measured as 59.1 $\pm$8.4(mg/10 9 spermatozoa), and that of the cauda epididymal spermatozoa(CDS) was 14.0$\pm$12.3(mg/10 9 spermatozoa). When phosphatase activities of the CDS in basic reaction medium were 29.2% in alkaline phosphatase, 44.9% in ATPse and 53.8% in acid phosphatase. The activities were eminently decreased in all CDS in contrast to those of CPS. The alkaline phosphatase and ATPase activities of K+ -dependent were decreased in CDS when compared with caput epididymal spermatozoa, and alkaline phosphatase, ATPase and acid phosphatase activities of $Ca^2$+ -dependent were increased in homogenized spermatozoa when compared with intact spermatozoa. From these results, it may be concluded that the decrease of phosphatases activities in spermatozoa during epididymal maturation may play some significant roles in acquiring fertilizing capability.

• Journal of Life Science
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• v.24 no.1
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• pp.14-19
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• 2014

Kinesin-1 consists of two heavy chains (KHCs), also called KIF5s, and two light chains (KLCs) that form a heterotetrameric complex. Here, we demonstrate the binding of a neuronal KHC, KIF5A, to the carboxyl (C)-terminal tail region of Fig4 (also known as Sac3), a phosphatase that removes the 5-phosphate from phosphatidylinositol-3,5-bisphosphate ($PtdIns(3,5)P_2$). Fig4 bound to the C-terminal region of KIF5A but not to other KHCs (KIF5B and KIF5C) and KLC1 in yeast two-hybrid assays. The interaction was further confirmed in a glutathione S-transferase pull-down assay and by co-immunoprecipitation. Anti-KIF5A antibody co-immunoprecipitated Fig4 with KIF5A from mouse brain extracts. These results suggest that kinesin-1 could transport the Fig4-associated protein complex or cargo in cells.

• Fisheries and Aquatic Sciences
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• v.13 no.1
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• pp.49-55
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• 2010

A bacterial strain with phytase and glucose-1-phosphatase activity was isolated from seawater. The colony was identified as an Enterobacter cloacae strain and named E. cloacae B11. A gene, agpEnB11, coding for an intracellular acid glucose phosphatase was cloned from the strain and sequenced. It comprised 1,242 nucleotides and encoded a polypeptide of 413 amino acids. Recombinant glucose-1-phosphatase (AgpEn) was overexpressed in Escherichia coli and purified using Ni-NTA column under native conditions. Purified protein displayed a single band of 47 kDa on SDS-PAGE. AgpEn hydrolyzed a wide variety of phosphorylated compounds, with high activity for glucose-1-phosphate and glucose-6-phosphate. Optimum pH and temperature for enzyme activity were pH 5.0 and $50^{\circ}C$, respectively. Enzyme activity was stimulated by $Ca^{2+}$ and $Co^{2+}$, and inhibited by $Cu^{2+}$.