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Association between 14bp Insertion/Deletion Polymorphism in Exon 8 of HLA-G gene and Oral Squamous Cell Carcinoma in Korean Population.

Sang Wook KANG ; Ju Yeon BAN

International Journal of Oral Biology.2017;42(2):79-83. doi:10.11620/IJOB.2017.42.2.079

Abnormal HLA-G expression occurs in various diseases such as melanoma, renal cell carcinoma, asthma, and classic Hodgkin's lymphoma. The purpose of this study was to determine whether HLA-G gene is linked with oral squamous cell carcinoma (OSCC). To investigate the possible link with susceptibility to OSCC, 54 OSCC patients and 120 healthy controls were enrolled in this study. HLA-G 14bp insertion/deletion polymorphism is in 3′-untranslated region of HLA-G gene. HLA-G 14bp insertion/deletion polymorphism was analyzed using the polymerase chain reaction (PCR) method. For the analysis of genetic data, SPSS18.0 program was used. Logistic regression models were performed for odds ratio (OR), 95 percent confidence interval (CI), and P value. There was a significant difference in distribution allele between OSCC patients and control subjects (OR=0.018, 95% CI=0.002-0.131, p<0.001). Our results suggest that HLA-G 14bp insertion/deletion polymorphism may be linked with susceptibility to OSCC in the Korean population.
Alleles ; Asthma ; Carcinoma, Renal Cell ; Carcinoma, Squamous Cell* ; Epithelial Cells* ; Exons* ; HLA-G Antigens* ; Hodgkin Disease ; Humans ; Logistic Models ; Melanoma ; Methods ; Odds Ratio ; Polymerase Chain Reaction

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Development of Refolding Process to Obtain Active Recombinant Human Bone Morphogenetic Protein-2 and its Osteogenic Efficacy on Oral Stem Cells.

Ji Hye LEE ; Young Joo JANG

International Journal of Oral Biology.2017;42(2):71-78. doi:10.11620/IJOB.2017.42.2.071

BMP-2 is a well-known TGF-beta related growth factor, having a significant role in bone and cartilage formation. It has been employed to promote bone formation in some clinical trials, and to differentiate mesenchymal stem cells into osteoblasts. However, it is difficult to obtain this protein in its soluble and active form. hBMP-2 is expressed as an inclusion body in the bacterial system. To continuously supply hBMP-2 for research, we optimized the refolding of recombinant hBMP-2 expressed in E. coli, and established an efficient method by using detergent and alkali. Using a heparin column, the recombinant hBMP-2 was purified with the correct refolding. Although combinatorial refolding remarkably enhanced the solubility of the inclusion body, a higher yield of active dimer form of hBMP-2 was obtained from one-step refolding with detergent. The refolded recombinant hBMP-2 induced alkaline phosphatase activity in mouse myoblasts, at ED₅₀ of 300-480ng/ml. Furthermore, the expressions of osteogenic markers were upregulated in hPDLSCs and hDPSCs. Therefore, using the process described in this study, the refolded hBMP-2 might be cost-effectively useful for various differentiation experiments in a laboratory.
Alkalies ; Alkaline Phosphatase ; Animals ; Cartilage ; Detergents ; Heparin ; Humans* ; Inclusion Bodies ; Mesenchymal Stromal Cells ; Methods ; Mice ; Myoblasts ; Osteoblasts ; Osteogenesis ; Solubility ; Stem Cells* ; Transforming Growth Factor beta

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Development of a Novel Subunit Vaccine Targeting Fusobacterium nucleatum FomA Porin Based on In Silico Analysis.

Kwangjoon JEONG ; Puth SAO ; Mi Jin PARK ; Hansol LEE ; Shi Ho KIM ; Joon Haeng RHEE ; Shee Eun LEE

International Journal of Oral Biology.2017;42(2):63-70. doi:10.11620/IJOB.2017.42.2.063

Selecting an appropriate antigen with optimal immunogenicity and physicochemical properties is a pivotal factor to develop a protein based subunit vaccine. Despite rapid progress in modern molecular cloning and recombinant protein technology, there remains a huge challenge for purifying and using protein antigens rich in hydrophobic domains, such as membrane associated proteins. To overcome current limitations using hydrophobic proteins as vaccine antigens, we adopted in silico analyses which included bioinformatic prediction and sequence-based protein 3D structure modeling, to develop a novel periodontitis subunit vaccine against the outer membrane protein FomA of Fusobacterium nucleatum. To generate an optimal antigen candidate, we predicted hydrophilicity and B cell epitope parameter by querying to web-based databases, and designed a truncated FomA (tFomA) candidate with better solubility and preserved B cell epitopes. The truncated recombinant protein was engineered to expose epitopes on the surface through simulating amino acid sequence-based 3D folding in aqueous environment. The recombinant tFomA was further expressed and purified, and its immunological properties were evaluated. In the mice intranasal vaccination study, tFomA significantly induced antigen-specific IgG and sIgA responses in both systemic and oral-mucosal compartments, respectively. Our results testify that intelligent in silico designing of antigens provide amenable vaccine epitopes from hard-to-manufacture hydrophobic domain rich microbial antigens.
Animals ; Cloning, Molecular ; Computational Biology ; Computer Simulation* ; Epitopes ; Epitopes, B-Lymphocyte ; Fusobacterium nucleatum* ; Fusobacterium* ; Hydrophobic and Hydrophilic Interactions ; Immunoglobulin A, Secretory ; Immunoglobulin G ; Membrane Proteins ; Mice ; Periodontitis ; Solubility ; Vaccination

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Action of Mitochondrial Substrates on Neuronal Excitability in Rat Substantia Gelatinosa Neurons.

Hae In LEE ; Sang Woo CHUN

International Journal of Oral Biology.2017;42(2):55-61. doi:10.11620/IJOB.2017.42.2.055

Recent studies indicate that mitochondria are an important source of reactive oxygen species (ROS) in the spinal dorsal horn. In our previous study, application of malate, a mitochondrial electron transport complex I substrate, induced a membrane depolarization, which was inhibited by pretreatment with ROS scavengers. In the present study, we used patch clamp recording in the substantia geletinosa (SG) neurons of spinal slices, to investigate the cellular mechanism of mitochondrial ROS on neuronal excitability. DNQX (an AMPA receptor antagonist) and AP5 (an NMDA receptor antagonist) decreased the malate-induced depolarization. In an external calcium free solution and addition of tetrodotoxin (TTX) for blockade of synaptic transmission, the malateinduced depolarization remained unchanged. In the presence of DNQX, AP5 and AP3 (a group I metabotropic glutamate receptor (mGluR) antagonist), glutamate depolarized the membrane potential, which was suppressed by PBN. However, oligomycin (a mitochondrial ATP synthase inhibitor) or PPADS (a P2 receptor inhibitor) did not affect the substrates-induced depolarization. These results suggest that mitochondrial substrate-induced ROS in SG neuron directly acts on the postsynaptic neuron, therefore increasing the ion influx via glutamate receptors.
Animals ; Calcium ; Electron Transport Complex I ; Glutamic Acid ; Membrane Potentials ; Membranes ; Mitochondria ; Mitochondrial Proton-Translocating ATPases ; N-Methylaspartate ; Neurons* ; Oligomycins ; Rats* ; Reactive Oxygen Species ; Receptors, AMPA ; Receptors, Glutamate ; Receptors, Metabotropic Glutamate ; Spinal Cord Dorsal Horn ; Substantia Gelatinosa* ; Synaptic Transmission ; Tetrodotoxin

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Water Extracts of Anthriscus sylvestris Leaf induces Apoptosis in FaDu Human Hypopharynx Squamous Carcinoma Cells.

Jung Eun YANG ; Seul Ah LEE ; Sung Min MOON ; Seul Hee HAN ; Yun Hee CHOI ; Su Gwan KIM ; Do Kyung KIM ; Bo Ram PARK ; Chun Sung KIM

International Journal of Oral Biology.2017;42(2):47-54. doi:10.11620/IJOB.2017.42.2.047

Anthriscus sylvestris (L.) Hoffm. is a perennial herb found widely distributed in various regions of Korea, Europe, and New Zealand. The root of A. sylvestris have been extensively used in the treatment for antitussive, antipyretic, cough remedy in Oriental medicine, but the physiologically active function of the leaf of A. sylvestris is as yet unknown. In this study, we investigated the anti-cancer activity and the mechanism of cell death of water extracts of leaf of Anthriscus sylvestris (WELAS), on human FaDu hypopharyngeal squamous carcinoma cells. Our data showed that WELAS treatment inhibited cell viability in a concentration- and time-dependent manner. In addition, the treatment of WELAS markedly induced apoptosis in FaDu cells, as determined by the viability assay, DAPI stain and FACS analysis. WELAS also increased the proteolytic cleavage of procaspase-3, -9 and PARP (poly(ADP-ribose) polymerase). In addition, exposure to WELAS decreased the expression of Bcl-2 (an anti-apoptotic factor), but increased the expression of Bax (a pro-apoptotic factor), suggesting that mitochondria-dependent apoptotic pathways are mediated in WELAS-induced apoptosis. Taken together, these results indicate that water extracts of leaf of A. sylvestris inhibits cell growth and induces apoptosis via the mitochondrial-dependent apoptotic pathway in FaDu human hypopharyngeal squamous carcinoma cells. Therefore, we propose that the water extracts of leaf of A. sylvestris is a novel chemotherapeutic drug, having growth inhibitory properties and induction of apoptosis in human oral cancer cells.
Apoptosis* ; Carcinoma, Squamous Cell* ; Caspase 3 ; Cell Death ; Cell Survival ; Cough ; Europe ; Humans* ; Hypopharynx* ; Korea ; Medicine, East Asian Traditional ; Mouth Neoplasms ; New Zealand ; Water*

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Effect of Metformin on Cell Growth and Differentiation in Cultured Odontoblasts.

Chang Young OH ; Su Gwan KIM ; Dae San GO ; Sun Kyoung YU ; Tae Hoon KIM ; Chun Sung KIM ; Joo Cheol PARK ; Do Kyung KIM

International Journal of Oral Biology.2017;42(2):39-45. doi:10.11620/IJOB.2017.42.2.039

Metformin (1,1-dimethylbiguanide hydrochloride), derived from French lilac (Galega officinalis), is a first-line anti-diabetic drug prescribed for patients with type 2 diabetes. However, the role of metformin in odontoblastic cell differentiation is still unclear. This study therefore undertook to examine the effect of metformin on regulating odontoblast differentiation in MDPC-23 mouse odontoblastic cells derived from mouse dental papilla cells. As compared to controls, metformin significantly accelerated the mineralization, significantly increased and accelerated the expressions of ALP and Col I mRNAs, and significantly increased the accelerated expressions of DSPP and DMP-1 mRNAs, during differentiation of MDPC-23 cells. There was no alteration in cell proliferation of MDPC-23 cells, on exposure to metformin. These results suggest that the effect of metformin on MDPC-23 mouse odontoblastic cells derived from mouse dental papilla cells, facilitates the odontoblast differentiation and mineralization, without altering the cell proliferation.
Animals ; Cell Differentiation ; Cell Proliferation ; Dental Papilla ; Humans ; Metformin* ; Mice ; Miners ; Odontoblasts* ; RNA, Messenger

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Xylitol Down-Regulates 1alpha,25-Dihydroxy Vitamin D3-induced Osteoclastogenesis via in Part the Inhibition of RANKL Expression in Osteoblasts.

Seung Ho OHK ; Hyunjoo JEONG ; Jong Pill KIM ; Yun Jung YOO ; Jeong Taeg SEO ; Dong Min SHIN ; Syng Ill LEE

International Journal of Oral Biology.2013;38(3):127-134.

Xylitol is a sugar alcohol with a variety of functions including bactericidal and anticariogenic effects. However, the cellular mechanisms underlying the role of xylitol in bone metabolism are not yet clarified. In our present study, we exploited the physiological role of xylitol on osteoclast differentiation in a co-culture system of osteoblastic and RAW 264.7 cells. Xylitol treatment of these co-cultures reduced the number of tartrate-resistant acid phosphatase (TRAP)-positive multinucleated cells induced by 10 nM 1alpha,25(OH)2D3 in a dose-dependent manner. A cell viability test revealed no marked cellular damage by up to 100 mM of xylitol. Exposure of osteoblastic cells to xylitol decreased RANKL, but not OPG, mRNA expression in the presence of 10(-8) M 1alpha,25(OH)2D3 in a dose-dependent manner. Furthermore, bone resorption activity, assessed on bone slices in the co-culture system, was found to be dramatically decreased with increasing xylitol concentrations. RANKL and OPG proteins were assayed by ELISA and the soluble RANKL (sRANKL) concentration was decreased with an increased xylitol concentration. In contrast, OPG was unaltered by any xylitol concentration in this assay. These results indicate that xylitol inhibits 1alpha,25(OH)2D3-induced osteoclastogenesis by reducing the sRANKL/OPG expression ratio in osteoblastic cells.
Acid Phosphatase ; Bone Resorption ; Cell Survival ; Coculture Techniques ; Enzyme-Linked Immunosorbent Assay ; Isoenzymes ; Osteoblasts ; Osteoclasts ; Proteins ; RNA, Messenger ; Vitamins ; Xylitol

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Tumor Necrosis Factor alpha up-regulates the Expression of beta2 Adrenergic Receptor via NF-kappaB-dependent Pathway in Osteoblasts.

Kyunghwa BAEK ; Jiho KANG ; Hyo Rin HWANG ; Jeong Hwa BAEK

International Journal of Oral Biology.2013;38(3):121-126.

Tumor necrosis factor alpha (TNFalpha) is a multifunctional inflammatory cytokine that regulates various cellular and biological processes. Increased levels of TNFalpha have been implicated in a number of human diseases including diabetes and arthritis. Sympathetic nervous system stimulation via the beta2-adrenergic receptor (beta2AR) in osteoblasts suppresses osteogenic activity. We previously reported that TNFalpha up-regulates beta2AR expression in murine osteoblastic cells and that this modulation is associated with TNFalpha inhibition of osteoblast differentiation. In our present study, we explored whether TNFalpha induces beta2AR expression in human osteoblasts and then identified the downstream signaling pathway. Our results indicated that beta2AR expression was increased in Saos-2 and C2C12 cells by TNFalpha treatment, and that this increase was blocked by the inhibition of NF-kappaB activation. Chromatin immunoprecipitation and luciferase reporter assay results indicated that NF-kappaB directly binds to its cognate elements on the beta2AR promoter and thereby stimulates beta2AR expression. These findings suggest that the activation of TNFalpha signaling in osteoblastic cells leads to an upregulation of beta2AR and also that TNFalpha induces beta2AR expression in an NF-kappaB-dependent manner.
Arthritis ; Biological Processes ; Chromatin Immunoprecipitation ; Durapatite ; Humans ; Luciferases ; NF-kappa B ; Osteoblasts ; Receptors, Adrenergic ; Sympathetic Nervous System ; Tumor Necrosis Factor-alpha ; Up-Regulation

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Effects of CoCl2 on Osteogenic Differentiation of Human Mesenchymal Stem Cells.

Yeon Hee MOON ; Jung Wan SON ; Jung Sun MOON ; Jee Hae KANG ; Sun Hun KIM ; Min Seok KIM

International Journal of Oral Biology.2013;38(3):111-119.

OBJECTIVE: To investigate the effects of the hypoxia inducible factor-1 (HIF-1) activation-mimicking agent cobalt chloride (CoCl2) on the osteogenic differentiation of human mesenchymal stem cells (hMSCs) and elucidate the underlying molecular mechanisms. STUDY DESIGN: The dose and exposure periods for CoCl2 in hMSCs were optimized by cell viability assays. After confirmation of CoCl2-induced HIF-1alpha and vascular endothelial growth factor expression in these cells by RT-PCR, the effects of temporary preconditioning with CoCl2 on hMSC osteogenic differentiation were evaluated by RT-PCR analysis of osteogenic gene expression, an alkaline phosphatase (ALP) activity assay and by alizarin red S staining. RESULTS: Variable CoCl2 dosages (up to 500 microM) and exposure times (up to 7 days) on hMSC had little effect on hMSC survival. After CoCl2 treatment of hMSCs at 100 microM for 24 or 48 hours, followed by culture in osteogenic differentiating media, several osteogenic markers such as Runx-2, osteocalcin and osteopontin, bone sialoprotein mRNA expression level were found to be up-regulated. Moreover, ALP activity was increased in these treated cells in which an accelerated osteogenic capacity was also verified by alizarin red S staining. CONCLUSIONS: The osteogenic differentiation potential of hMSCs could be preserved and even enhanced by CoCl2 treatment.
Alkaline Phosphatase ; Anoxia ; Anthraquinones ; Cell Survival ; Cobalt ; Durapatite ; Gene Expression ; Humans ; Integrin-Binding Sialoprotein ; Mesenchymal Stromal Cells ; Osteocalcin ; Osteopontin ; RNA, Messenger ; Vascular Endothelial Growth Factor A

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Apoptotic Effects of Co-Treatment with a Chios Gum Mastic and Eugenol on G361 Human Melanoma Cells.

Jae Beom JO ; Sang Hun OH ; In Ryoung KIM ; Gyoo Cheon KIM ; Hyun Ho KWAK ; Bong Soo PARK

International Journal of Oral Biology.2013;38(3):101-110.

We investigated the synergistic apoptotic effects of co-treatments with Chios gum mastic (CGM) and eugenol on G361 human melanoma cells. An MTT assay was conducted to investigate whether this co-treatment efficiently reduces the viability of G361 cells compared with each single treatment. The induction and augmentation of apoptosis were confirmed by DNA electrophoresis, Hoechst staining, and analyses of DNA hypoploidy. Western blot analysis and immunofluorescent staining were also performed to evaluate expression and translocation of apoptosis-related proteins following CGM and eugenol co-treatment. Proteasome activity and mitochondrial membrane potential (MMP) changes were also assayed.The results indicated that the co-treatment of CGM and eugenol induces multiple pathways and processes associated with an apoptotic response in G361 cells. These include nuclear condensation, DNA fragmentation, a reduction in MMP and proteasome activity, an increase of Bax and decrease of Bcl-2, a decreased DNA content, cytochrome c release into the cytosol, the translocation of AIF and DFF40 (CAD) into the nucleus, and the activation of caspase-9, caspase-7, caspase-3, PARP and DFF45 (ICAD). In contrast, separate treatments of 40 microg/ml CGM or 300 microM eugenol for 24 hours did not induce apoptosis. Our present data thus suggest that a combination therapy of CGM and eugenol is a potential treatment strategy for human melanoma.
Apoptosis ; Blotting, Western ; Caspase 3 ; Caspase 7 ; Caspase 9 ; Cytochromes c ; Cytosol ; DNA ; DNA Fragmentation ; Electrophoresis ; Eugenol ; Gingiva ; Humans ; Melanoma ; Membrane Potential, Mitochondrial ; Proteasome Endopeptidase Complex ; Proteins ; Resins, Plant

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