• Molecules and Cells
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• v.40 no.5
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• pp.371-377
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• 2017

Despite the importance of the receptor activator of nuclear factor (NF)-kappaB ligand (RANKL)-RANK signaling mechanisms on osteoclast differentiation, little has been studied on how RANK expression is regulated or what regulates its expression during osteoclastogenesis. We show here that insulin signaling increases RANK expression, thus enhancing osteoclast differentiation by RANKL. Insulin stimulation induced RANK gene expression in time- and dose-dependent manners and insulin receptor shRNA completely abolished RANK expression induced by insulin in bone marrow-derived monocyte/macrophage cells (BMMs). Moreover, the addition of insulin in the presence of RANKL promoted RANK expression. The ability of insulin to regulate RANK expression depends on extracellular signal-regulated kinase 1/2 (ERK1/2) since only PD98059, an ERK1/2 inhibitor, specifically inhibited its expression by insulin. However, the RANK expression by RANKL was blocked by all three mitogen-activated protein (MAP) kinases inhibitors. The activation of RANK increased differentiation of BMMs into tartrate-resistant acid phosphatase-positive ($TRAP^+$) osteoclasts as well as the expression of dendritic cell-specific transmembrane protein (DC-STAMP) and d2 isoform of vacuolar ($H^+$) ATPase (v-ATPase) Vo domain (Atp6v0d2), genes critical for osteoclastic cell-cell fusion. Collectively, these results suggest that insulin induces RANK expression via ERK1/2, which contributes to the enhancement of osteoclast differentiation.

• Proceedings of the Korean Society of Precision Engineering Conference
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• 2003.06a
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• pp.1-4
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• 2003

Knowledge classification and expression of constructed knowledge have been main research issues in the field of knowledge representation. Constructed design knowledge of the former product loses its utility when new products with different structures are introduced to the market. In order to construct the design knowledge for a new product. designers need to reconstruct the design knowledge with new relationships. The design knowledge has been constructed with level trees, but it is difficult to rearrange the relations. Design DNA is proposed in this work in order to facilitate the rearrangement of design knowledge and give flexibility to knowledge structure. Design DNA is based on Layout-oriented domain knowledge and Function-oriented domain knowledge, which enables to generate new design knowledge that will result in new part geometries for given constraints on the part functions. Design DNA is applied to the design knowledge of lever system of the automatic transmission of passenger cars as an example.

• Journal of the Optical Society of Korea
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• v.20 no.5
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• pp.628-632
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• 2016

We studied experimentally and theoretically the vertical range of the confined electric field in the gap area of metamaterials, which was analyzed for various gap widths using terahertz time-domain spectroscopy. We measured the resonant frequency as a function of the thickness of poly(methyl methacrylate) in the range 0 to 3.2 μm to quantify the effective detection volumes. We found that the effective vertical range of the metamaterial is determined by the size of the gap width. The vertical range was found to decrease as the gap width of the metamaterial decreases, whereas the sensitivity is enhanced as the gap width decreases due to the highly concentrated electric field. Our experimental findings are in good agreement with the finite-difference time-domain simulation results. Finally, a numerical expression was obtained for the vertical range as a function of the gap width. This expression is expected to be very useful for optimizing the sensing efficiency.

• BMB Reports
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• v.48 no.12
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• pp.696-701
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• 2015

Toll-like receptor 3 (TLR3) recognizes viral double-stranded RNA. It stimulates pro-inflammatory cytokine and interferon production. Here we reported the expression of a novel isoform of TLR3 in human astrocyte cell lines whose message is generated by alternative splicing. The isoform represents the N-terminus of the protein. It lacks many of the leucine-rich repeat domains, the transmembrane domain, and the intracellular Toll/interleukin-1 receptor domain of TLR3. Type I interferons (interferon-α and interferon-β) induced the expression of this isoform. Exogenous overexpression of this isoform inhibited interferon regulatory factor 3, signal transducers and activators of transcription 1, and Inhibitor of kappa B α signaling following stimulation. This isoform of TLR3 also inhibited the production of chemokine interferon-γ-inducible protein 10. Our study clearly demonstrated that the expression of this isoform of TLR3 was a negative regulator of signaling pathways and that it was inducible by type I interferons. We also found that this isoform could modulate inflammation in the brain.

• Korean Institute of Interior Design Journal
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• v.13 no.2
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• pp.64-71
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• 2004

This study attempts to clarify inter-relationship between design expression in the surface of contemporary multi-family housing and physical trends in this digital age. The study examines characteristics of housing design influenced from new digital technology in the forms of metaphor such as dematerialization, fluidity and mobility. Currently constructed multi-family housing in Europe after 1990 has been analyzed to find digital reflections in the surfaces. As a conclusion, findings are as follows; In this digital age, a house is considered as a base in the forms of boxes and containers to network to outer worlds. In a complex of multi-family housing, public spaces move to the inside and become parts of private domain. Therefore, a house directly faces a street/outer world without transitional areas and devices. The facades of housing become delicate skins to control private domain in the inside and the world in the outside. In this digital age, the surfaces of housing are designed by ways of wrapping and screening. Printing and mapping methods are used to surface design because they are manipulative and flexible methods in design like graphic design. Screening devices using louvers and shutters are powerful tools to make random and unpredictable images. If units of a louver and a shutter were pixels, a whole surface would be a digital screen. In such assumption, the facade of buildings reflects digital screen to interface while the louvers in operation reflect clicking to network. As a conclusion, design expression in surfaces in-between of multi-family housing is a metaphor of digital mechanism.

• Reproductive and Developmental Biology
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• v.36 no.3
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• pp.193-198
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• 2012

This study was to examine expression of the recombinant full-length adiponectin (recombinant adiponectin) in insect ovarian cell culture system and to characterize structural properties of the recombinant adiponectin secreted in medium. Gene construct encoding the recombinant adiponectin contained N-terminal collagen-like domain (110 Amino Acids, AAs), C-terminal globular domain (137 AAs) and C-terminal peptides for detection with V5 antibody (26 AAs included adaptor peptide) and purification using the 6xHis tag (6 AAs). The approximate molecular weight of the product (monomer) was 35 kDa. Molecular mass species of the expressed recombinant adiponectin were monomer (~35 kDa), dimer (~70 kDa), trimer (~105 kDa) and hexamer (~210 kDa). The major secreted species were the LMW forms, such as monomer, dimer, and trimer. There was MMW of hexamer as minor form. HMW multimers (~300 kDa) were shown as a tracer or not detected on the SDS-PAGE in several experiments (data not shown). The multimer forms in this study were not compatible to those in animal or human serum and adipose tissue by other researcher's study in which the major multimer forms were HMW. By protein denaturing experiments with reducing reagent (${\beta}$-MeOH), anionic detergent (SDS) and heat ($95^{\circ}C$) on the SDS-PAGE, not all adiponectin multimers seemed to have disulfide bond linked structure to form multimers. The recombinant adiponectin which expressed in insect ovarian cell culture system seemed to have the limitation as full physiological regulator for the application to animal and human study.

• Korean Journal of Plant Tissue Culture
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• v.27 no.5
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• pp.379-385
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• 2000

tRNA and 7SL RNA based antisense vehicles were prepared by inserting conserved anti-viral and anti-viroid domains. Anti-PVS coat protein leader sequence (ACPL) and antistructural antihairpin domain of PSTVd (AHII) were inserted in tRNA cassette; anti- zing finger domain of PVS, AHII and anti hop latent viroid ribozyme were inserted in 7SL RNA gene isolated from A. thaliana. These constructs were shown to be transcribed both, in in vitro and in in vivo conditions. However, it followed from our work that closely linked position of PoIII reference genes and PoIIII antisense genes within T-DNA lead to the impairment of RNA expression in transgenic plants. To assay in vivo transcription of antisense genes, hairy root potato cultures were established using h. tumefaciens A4-24 bearing both, Ri plasmid and PoIII-promoterless plant expression vectors with antisense RNA genes. Expression of antisense RNA in transgenic potato tissues was proven by specific RT-PCR reactions.

• Asian-Australasian Journal of Animal Sciences
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• v.29 no.7
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• pp.944-951
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• 2016

Tdrd12 is one of tudor domain containing (Tdrd) family members. However, the expression pattern of Tdrd12 has not been well studied. To compare the expression levels of Tdrd12 in various tissues, real time-polymerase chain reaction was performed using total RNAs from liver, small intestine, heart, brain, kidney, lung, spleen, stomach, uterus, ovary, and testis. Tdrd12 mRNA was highly expressed in testis. Antibody against mouse TDRD12 were generated using amino acid residues SQRPNEKPLRLTEKKDC of TDRD12 to investigate TDRD12 localization in testis. Immunostaining assay shows that TDRD12 is mainly localized at the spermatid in the seminiferous tubules of adult testes. During postnatal development, TDRD12 is differentially expressed. TDRD12 was detected in early spermatocytes at 2 weeks and TDRD12 was localized at acrosome of the round spermatids. TDRD12 expression was not co-localized with TDRD1 which is an important component of piRNA pathway in germ cells. Our results indicate that TDRD12 may play an important role in spermatids and function as a regulator of spermatogenesis in dependent of TDRD1.

• BMB Reports
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• v.43 no.3
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• pp.199-204
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• 2010

The protein p104 was first isolated as a binding partner of the Src homology domain of phospholipase C$\gamma$1, and has been shown to associate with p85$\alpha$, Grb2. The ectopic expression of p104 reduced cellular growth rate, which was also achieved with the overexpression of only the proline-rich region of p104. The proline-rich region of p104 has been found to inhibit the colony formation of platelet-derived growth factor BB-stimulated NIH3T3 cells and MCF7 cancer cells on soft agar. Mutagenesis analysis showed that the second and third proline-rich regions are essential for growth control, as well as for interaction with p85$\alpha$. Overexpression of p104 increased the level of the cyclin-dependent kinase inhibitor, $p27^{Kip1}$, and inhibited the activity of phosphoinositide 3-kinase (PI3K). In summary, p104 interacts with p85$\alpha$ and is involved in the regulation of $p27^{Kip1}$ expression for the reduction of cellular proliferation.

• The Journal of Natural Sciences
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• v.8 no.2
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• pp.35-41
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• 1996

To find the substrate interacting site of the MCAT1, charged amino acid residues in the transmembrane domain were changed to opposite charged amino acids and studied the arginine uptake, gp70 binding, efflux and protein expression using the Xenopus oocyte expression method. Among the five mutants of MCAT1, the D403K showed the most interesting characteristics, which had normal gp70 binding but low arginine uptake function, that means the normal expression on the membrane but decreased transport function. All mutants except K211E showed decreased arginine efflux, and kinetic study showed decreased Vmax. Together, Clu(403) residue of MCAT1 may show the possible substrate interacting site in the transmembrane domain of MCAT1.