한국인 턱끝구멍의 형태

김희진,이승일,정인혁 대한해부학회 1995 Anatomy & Cell Biology Vol.28 No.1

기계적 자극이 치주인대 세포의 osteoprotegerin과 receptor activator of nuclear factor κB ligand mRNA 발현에 미치는 영향

이기주,이승일,황충주,,옥승호,전옥순 대한치과교정학회 2005 대한치과교정학회지 Vol.35 No.4

본 연구는 치주인대 세포에 지속적이고 점진적 인장력을 가하여 치아 이동 시 형성되는 인장부위의 기계적 자극에 대한 생화학적 전달과 치조골 흡수와 생성 조절 기전을 이해하고자 하였다. 치주인대 세포가 배양된 유연한 성장 표면을 가진 배지에 지속적이고 점진적인 인장력을 가하고 골흡수 인자인 PGE_(2)와 골형성 인자인 ALP의 생성량을 1, 3, 6, 12시간 후에 측정하여 정량비교하였고 파골세포 분화기전을 조절하는 OPG, RANKL의 인자들과 matrix metalloproteinase (MMP)-1, -8, -9, -13, tissue inhlbitor of matrix metalloproteinase (TIMP)-1의 인자들을 역전사 중합효소 연쇄반응 검사하여 m-RNA 발현을 비교한 결과, 치주인대 세포에 인장력을 가한 경우 대조군보다 PGE_(2)의 농도가 적었고 (p<0.05) ALP의 농도 변화는 없었으며 OPG의 mRNA 발현이 증가하였으나, RANKL의 mRNA 발현은 감소하였다. 그리고 TIMP-1과 MMP-1, -8, -9, -13의 mRNA 발현이 대조군과 차이가 없었다. 이상의 연구에서 사람의 치주인대 세포는 점진적이고 지속적인 인장력에 대한 반응으로 PGE_(2)의 생성과 RANKL의 mRNA 발현은 감소하고 OPG의 mRNA 발현은 증가하여 골흡수를 억제하는 효과를 보이는 것으로 나타났다. Tooth movement is a result of mutual physiologic responses between the periodontal ligament and alveolar bone stimulated by mechanical strain. The PDL cell and osteoblast are known to have an influence on bone formation by controlling collagen synthesis and alkaline phosphatase activation. Moreover, recent studies have shown that the PDL cell and osteoblast release osteoprotegerin(OPG) and the receptor activator of nuclear factor κB ligand (RANKL) to control the level of osteoclast differentiation and activation which in turn influences bone resorption. In this study, progressively increased, continuous tenslonal force was applied to PDL cells. The objective was to progressively increased. continuous tensional force was applied to PDL cells. The objective was to find out which kind of biochemical reactions occur after tensional force application and to illuminate the alveolar bone resorption and apposition mechanism. Continuous and progressively increased tensile force was applied to PDL cells cultured on a petriperm dish wlth a flexible membrane. The amount of PGE_(2) and ALP synthesis were measured after 1, 3, 6 and 12 hours of force application. Secondly, RT-PCR analysis was carried out for OPG and RANKL whlch control osteoclast differentiation and MMP-1, -8, -9, -13 and TIMP-1 which regulate the resolution of collagen and resorption of the osteoid layer. According to the results, we concluded that progressively increased, continuous force application to human PDL cells reduces PGE_(2) synthesls, and increases OPG mRNA expression.

Solubilization of Na/K/Cl Cotransporter in Rabbit Parotid Acini and Its Purification-Separation of Bumetanide Binding Protein by ¹⁴C-NEM Labeling

Syng-Ill Lee,Yun-Jung Yu,R. James Turner 대한구강생물학회 1994 International Journal of Oral Biology Vol.18 No.2

교정력에 의한 치아이동과 Biomechanical adaptation

이승일(Syng-Ill Lee) 대한치과의사협회 2013 대한치과의사협회지 Vol.51 No.3

Orthodontic tooth movement is a unique process which tooth, solid material is moving into hard tissue, bone. Orthodontic force in general provides the strain to the PDL and alveolar bone, which in turn generates the interstitial fluid flow(in detail, fluid flow in PDL and canaliculi). As a results of matrix strain, periodontal ligament cells and bone cells are deformed, releasing variety of cytokines, chemokines, and growth factors. These molecules lead to the orthodontic tooth movement(OTM). In these inflammation and tissue remodeling sites, all of the cells could closely communicate with one another, flowing the information for tissue remodeling. To accelerate the rate of OTM in future, local injection of single growth factor(GF) or a combination of multiple GF’s in the periodontal tissues might intervene to stimulate the rate of OTM. Corticotomy is effective and safe to accelerate OTM.

Solubilization of Na/K/Cl Cotransporter in Rabbit Parotid Acini and Its Purification-Separation of Bunetanide Binding Protein by ^14C-NEM Labeling

Lee, Syng-Ill,Yu, Yun-Jung,Turner, R. James The Official Publication of Korean Academy of Oral 1994 International Journal of Oral Biology Vol.18 No.2

In rat parotid basolateral membranes the presence of a 160 kD protein can be labeled with the irreversible sulfhydryl reagent [^14C]-N-ethyl maleimide in a bumetanide-protectable fasion. The previous results suggest that the existence of an esential sulfhydryl group is closely associated with the bumetanide-binding site on the parotid Na/K/Cl cotransporter, provide strong evidence that this protein is a part or all of the parotid bumetanide-binding site. When this protein is treated with endoglycosidase F/N-glycosidase F to remove N-linked oligosaccharides, its apparent molecular weight decreases to 135 kD. The bumetanide-binding protein was purified using two preparative electrophoresis steps. First, a Triton X-100 extract enriched in this protein was run on preparative electophoresis to obtain fractions containing proteins in the 160 kD range. These were then deglycosylated with endoglycosidase F/N-glycosidase F and selected fractions were pooled and rerun on preparative electrophoresis to obtain a final 135 kD fraction. The enrichment of the bumetanide-binding protein on this final 135kD fraction estimated from [^14C]-N-ethylmaleimide labeling was approximately 48 times relative to the starting membrane extract. Since the bumetanide-binding site represents approximately 2% of the total protein this starting extract, this enrichment indicates a high degree of purity of this protein in the 135 kD fraction.

Role of Regulators of G-Protein Signaling 4 in Ca<SUP>2+</SUP> Signaling in Mouse Pancreatic Acinar Cells

Soonhong Park,Syng-Ill Lee,Dong Min Shin 대한생리학회-대한약리학회 2011 The Korean Journal of Physiology & Pharmacology Vol.15 No.6

Regulators of G-protein signaling (RGS) proteins are regulators of Ca²⁺ signaling that accelerate the GTPase activity of the G-protein Ձ-subunit. RGS1, RGS2, RGS4, and RGS16 are expressed in the pancreas, and RGS2 regulates G-protein coupled receptor (GPCR)-induced Ca²⁺ oscillations. However, the role of RGS4 in Ca²⁺ signaling in pancreatic acinar cells is unknown. In this study, we investigated the mechanism of GPCR-induced Ca²⁺ signaling in pancreatic acinar cells derived from RGS4^−/− mice. RGS4^−/− acinar cells showed an enhanced stimulus intensity response to a muscarinic receptor agonist in pancreatic acinar cells. Moreover, deletion of RGS4 increased the frequency of Ca²⁺ oscillations. RGS4^−/− cells also showed increased expression of sarco/endoplasmic reticulum Ca²⁺ ATPase type 2. However, there were no significant alterations, such as Ca²⁺ signaling in treated high dose of agonist and its related amylase secretion activity, in acinar cells from RGS4^−/− mice. These results indicate that RGS4 protein regulates Ca²⁺ signaling in mouse pancreatic acinar cells.

Real-time Imaging of Inositol 1,4,5-trisphosphate Movement in Mouse Salivary Gland Cells

Jeong Hee Hong,Syng-Ill Lee,Dong Min Shin KOREAN ACADAMY OF ORAL BIOLOGY 2008 International Journal of Oral Biology Vol.33 No.4

Inositol 1,4,5-trisphosphate (IP3) plays an important role in the release of Ca2+ from intracellular stores into the cytoplasm in a variety of cell types. IP3 translocation dynamics have been studied in response to many types of cell signals. However, the dynamics of cytosolic IP3 in salivary acinar cells are unclear. A green fluorescent protein (GFP)-tagged pleckstrin homology domain (PHD) was constructed and introduced into a phospholipase C δ1 (PLC δ1) transgenic mouse, and then the salivary acinar cells were isolated. GFP-PHD was heterogeneously localized at the plasma membrane and intracellular organelles in submandibular gland and parotid gland cells. Application of trypsin, a G protein-coupled receptor activator, to the two types of cells caused an increase in GFP fluorescence in the cell cytoplasm. The observed time course of trypsin-evoked IP3 movement in acinar cells was independent of cell polarity, and the fluorescent label showed an immediate increase throughout the cells. These results suggest that GFP-PHD in many tissues of transgenic mice, including non-cultured primary cells, can be used as a model for examination of IP3 intracellular dynamics.

Caffeine Inhibits Acetylcholine- and Noradrenaline-Evoked but not Substance P-Evoked Intracellular Ca^2+ increases in Rat Mandibular Salivary Acini

Seo, Jeong Taeg,Lee, Syng Ill,Steward, Martin C.,Elliott, Austin C. The Official Publication of Korean Academy of Oral 1995 International Journal of Oral Biology Vol.19 No.2

The inhibitory effects of caffeine on the increases in intracellular Ca^2+ concentration ([Ca^2+]_i) induced by muscarinic, α-adrenergic and substance-P (SP) receptor stimulations were investigated in mandibular salivary acini isoloted from the rats. The acini loaded with fura-2 were exposed to excitation wavelength at 340 and 380 nm. The emitted fluorescence was measured at 510 nm with a photomultiplier tube attached to the spectrofluorometer system. The acini were first stimulated with 1 μM acetylcholine (ACh) followed by the second stimulation with ACh, noradrenaline or SP and the data were normalized by setting the first peak values of [Ca^2+]_i increases to 100%. The peak value of [Ca^2+]_i increase caused by the second stimulation with 1 μM ACh was reduced to 79.4±3.4% (n=7) compared with the first. In the presence of 20 mM caffeine, the second peak value of [Ca^2+]_i increase was reduced to 23.4±3.0% (n=7, p<0.001). The increase in [Ca^2+]_i caused by 3 μM noradrenaline stimulation was also greatly inhibited by the pretreatment with caffeine. In contrast. 5 nM SP-induced [Ca^2+]_i increase was reduced from 103.8±7.2%(n=8) to 87.2±4.6%(n=10) by the pretreatment with 20 mM caffeine but this difference was not significant. When the acini were subsequently stimulated with ACh and SP in the absence of perfusate Ca^2+,[Ca^2+]_i increase in response to SP was completely abolished(n=3). This result suggests that ACh and SP mobilize Ca^2+ from the same intracellular Ca^2+ pool. In conclusion, caffeine does not block the SP-induced [Ca^2+]_i increase while the ACh- and noradrenaline-induced[Ca^2+]_i increases were inhibited by caffeine. Since these two receptors both activate the common signalling pathway leading from G-protein to [Ca^2+]_i increase, the most possible site of caffeine action is receptor-G protein interaction.

Effect of Insulin on the Regulation of Na/K/Cl Cotransporter (NKCC2) in HEK293 Cells

Chang, Heesoon,Lee, Jin-Ill,Shin, Dong-Min,Ohk, Seung-Ho,Lee, Syng-Ill Korean Academy of Oral Biology and the UCLA Dental 2002 International Journal of Oral Biology Vol.27 No.3

Insulin is one of the regulators involved in Na^+ reabsorption in kidney. The Na^+ channel and Na/K/2CI cotransporter (NKCC2) system are primarily considered as the possible routes for Na^+ movement into the cell. The purpose of this stud is to understand the regulation of NKCC2 as a candidate for Na^+ movement across the kidney cell in response to insulin. In order to clarify the role of the insulin in human embryonic kidney cell line, HEK293, the cells were exposed to the different circumstances (isotonic, hypertonic), and then cell volume, expression of NKCC2 mRNA, intracellular Ca^2+ and functional activity of the cotransporter using pH dye, and the intracellular Ca^2+ level were analyzed in each condition. The cell volume of HEK293 which was shrunken by hypertonic stress recovered to nearly original state by the addition of 1μM insulin. It is obvious that insulin prevented cell shrinkage by operating the regulatory volume increase (RVI) machinery of the cell. However, insulin-induced RVI was blocked by the treatment of 10μM bumetanide. Furthermore, NKCC2 mRNA was expressed remarkably in the presence of 1μM insulin. Such results might suggest that the presence of 1μM insulin. Such results might suggest that the volume regulation of HEK293 cell showed the typical change in intracellular Ca^2+ concentration in response to carbachol as seen in other normal cells. However, insulin did not induce the change of intracellular calcium level of the HEK293 cell. Taken all together, these findings suggest that the insulin stimulates the sodium transport of HEK293 cell through the upregulation of NKCC2 under the hypertonic condition.

The Transcription Factor Mist1 Regulates the Cellular Polarity in Mouse Pancreatic Acinar Cells

Yu-Mi Yang,Syng-Ill Lee,Dong Min Shin KOREAN ACADAMY OF ORAL BIOLOGY 2012 International Journal of Oral Biology Vol.37 No.1

Pancreatic acinar cells exhibit a polarity that is characterized by the localization of secretory granules at the apical membrane. However, the factors that regulate cellular polarity in these cells are not well understood. In this study, we investigated the effect of Mist1, a basic helix-loop-helix transcription factor, on the cellular architecture of pancreatic acinar cells. Mist1-null mice displayed secretory granules that were diffuse throughout the pancreatic acinar cells, from the apical to basolateral membranes, whereas Mist1 heterozygote mice showed apical localization of secretory granules. Deletion of the Mist1 gene decreased the expression of type 3 inositol 1,4,5-triphosphate receptors (IP3R) but did not affect apical localization and expression of IP3R2. Mist1- null mice also displayed an increase in luminal areas and an increase in the expression of zymogen granules in pancreatic acinar cells. These results suggest that Mist1 plays a critical role in polar localization of cellular organelles and in maintaining cellular architecture in mouse pancreatic acinar cells.