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Jeong, K J,Park, S Y,Cho, K H,Sohn, J S,Lee, J,Kim, Y K,Kang, J,Park, C G,Han, J W,Lee, H Y Macmillan Publishers Limited 2012 Oncogene Vol.31 No.39
Lysophosphatidic acid (LPA) is a biolipid that has diverse biological activities implicated in ovarian cancer initiation and progression. Previous studies have shown the critical role of the Rho/Rho-associated kinase (ROCK) pathway in LPA-induced ovarian cancer progression. However, detailed underlying mechanism by which the Rho/ROCK pathway induces ovarian cancer cell invasion is still incompletely understood. In the present study, we observed that the Rho/ROCK pathway is implicated in the production of proteolytic enzymes, leading to LPA-induced ovarian cancer cell invasion. LPA induced matrix metalloproteinase (MMP)-9 expression in CAOV-3 and PA-1 cells and urokinase-type plasminogen activator (uPA) expression in SKOV-3 cells. LPA-induced proteolytic enzyme expression was required for the invasion of ovarian cancer cells expressing corresponding enzymes. Pretreatment of cells with a pharmacological inhibitor of Rho/ROCK (Y-27632) or overexpression of a dominant-negative mutant of Rho (Rho N19) profoundly inhibited LPA-induced proteolytic enzyme expression as well as the invasive potential of ovarian cancer cells. In addition, transfection with dominant-negative Ras (Ras N17) significantly inhibited LPA-induced Rho activation as well as MMP-9 and uPA expression. Consistently, Y-27632 reduced LPA-induced nuclear factor (NF)-κB activation that is critical for proteolytic enzyme expression and cellular invasion. Collectively, we demonstrate a mechanism by which LPA promotes ovarian cancer progression through coordinate activation of a Ras/Rho/ROCK/NF-κB signaling pathway and the proteolytic enzyme secretion, providing novel biomarkers and promising therapeutic targets for ovarian cancer cell progression.
손시환,고영두,김두환,박구부,이정규,이철영,신철교,정희식,곽석준,박명구,천민성,백철승 한국축산학회 2000 한국축산학회지 Vol.42 No.1
The Korean Native Stripped Cattle known as Chickso have distinctive black hair belts all over the body to varying extents on a Hanwoo(Korean Cattle)-like yellowish brown background. These Battle are remaining only in a limited area of this country and are known to yield a flavorful meat somewhat distinct from that of Hanwoo, but their genetic lineage has not been identified. We have carried out karyotyping of these cattle firm the lymphocyte culture. Blood samples were collected from 20 of male and female cattle that had been bred at Poongjeon Farm located in Kosong, Kyongnam, and were subjected to chromosomal morphology and G- and C-banding analysis. Chickso, like Hanwoo, had 58 autosomes and X and Y sex chromosomes which were morphologically very similar to those of the latter. All the 58 autosomes revealed almost a zero value of centromeric index, suggesting that they are acrocentric; sex chromosomes X and Y were submetacentric and metacentric, respectively. Following G-banding, the light bands appeared near the centromeric site in all the autosomes whereas the specific dark bands were consistently visible in each homologous chromosome. Overall, the G-banding pattern was nearly identical between the Chickso and Hanwoo. C-bands representing the heterochromatin were present at or near the centromere in all the autosomes, whereas in sex chromosomes, they were found distributed on variable sites. The proportion of constitutive heterochromatin ranged 20∼30%. These patterns were not significantly different between the two subspecies. All of these cytogenetic results suggest that the distinctive traits of Chickso did not arise from a cytogenetic variation from Hanwoo, i. e. the former is simply a subpopulation of the latter. As such, we propose that selection and propagation of the Chickso based on economic traits may be advantageous to the domestic beef industry.
Park, S.Y.,Song, H.J.,Sohn, U.D. North-Holland ; Elsevier Science Ltd 2009 european journal of pharmacology Vol.607 No.1
The RhoA/Rho-associated kinase (ROCK) signaling pathway has been known to play a critical role in Ca<SUP>2+</SUP>-sensitization of smooth muscle contraction. In this study, we investigated the role of ROCK in feline esophageal body smooth muscle contraction induced by electrical field stimulation and exogenous acetylcholine in vitro. Y-27632 [(+)-(R)-trans-4-(1-aminoethyl)-(4-pyridyl) cyclohexanecarboxamide dihydrochloride], ROCK inhibitor, and specific antibodies to ROCK1 and ROCK2 proteins, which are two isoforms of ROCK, were used. Electrical field stimulation induced off-contraction and on-contraction in the presence of N<SUP>G</SUP>-nitro-L-arginine methylester, originating from the cholinergic nerve. Y-27632 inhibited both excitatory contractions in a concentration-dependent manner. Exogenous acetylcholine concentration-dependently induced two types of contractions: an initial contraction which occurred immediately after the addition of acetylcholine during short periods, and a sustained contraction which sluggishly continued after the initial contraction. Maximal initial and sustained contractions were reached at 10<SUP>-5</SUP> M acetylcholine. Y-27632 significantly inhibited both acetylcholine-induced contractions in a concentration-dependent manner. Western blot analysis revealed that acetylcholine maximally increased the level of phosphorylation in the 20 kDa regulatory light chain of myosin II (MLC<SUB>20</SUB>) at Ser<SUP>19</SUP> from 0.25 min to 1 min, and then declined after 2 min. The level changes of MLC<SUB>20</SUB> phosphorylation during the 5 min paralleled with those of acetylcholine-induced contractions. The expression of ROCK1 and ROCK2 in membrane fractions of muscle was increased by acetylcholine; more specifically, ROCK2 continually expressed up to 5 min. Taken together, ROCK may be involved in neural-evoked and acetylcholine-induced contraction via translocation to the membrane in feline esophageal smooth muscle.
Lee, S.,Jang, S.,Kang, J.G.,Sohn, Y. Elsevier 2015 Materials science and engineering B. Advanced Func Vol.201 No.-
Understanding the role of the host oxide material is very important for developing phosphor materials. Here, Eu(III)- and Tb(III)-doped La(OH)<SUB>3</SUB> nanowires were prepared by a facial hydrothermal method, and Eu(III)- and Tb(III)-doped La<SUB>2</SUB>O<SUB>3</SUB> nanostructures were obtained by a post-thermal treatment. Their physicochemical characteristics were examined by scanning electron microscopy (SEM), transmission electron microscopy (TEM), X-ray diffraction (XRD), Fourier transform infrared spectroscopy (FT-IR), and ultraviolet-visible absorption spectroscopy. The photoluminescence (PL) counter mapping profiles were obtained to understand the photoluminescence mechanism. All the emission profiles were assigned based on the <SUP>5</SUP>D<SUB>0</SUB>→<SUP>7</SUP>F<SUB>J</SUB> (J=0-4) transitions of Eu(III) and the <SUP>5</SUP>D<SUB>4</SUB>→<SUP>7</SUP>F<SUB>J</SUB> (J=6, 5, 4, 3) transitions of Tb(III) ions. The hygroscopic La<SUB>2</SUB>O<SUB>3</SUB> host is unstable under ambient conditions and changed slowly to more stable La(OH)<SUB>3</SUB>. PL decay lifetime was observed be longer for the annealed sample with lower doping concentration due to a higher crystallinity.
Ok, S.H.,Kwon, S.C.,Yeol Han, J.,Yu, J.,Shin, I.W.,Lee, H.K.,Chung, Y.K.,Choi, M.J.,Sohn, J.T. North-Holland ; Elsevier Science Ltd 2014 european journal of pharmacology Vol.723 No.-
Mepivacaine is an aminoamide local anesthetic that produces vasoconstriction in vivo and in vitro. The goals of this in vitro study were to determine whether mepivacaine-induced contraction involves calcium sensitization in isolated endothelium-denuded aortas, and to investigate the specific protein kinases involved. The effects of mepivacaine and potassium chloride on intracellular calcium concentrations ([Ca<SUP>2+</SUP>]<SUB>i</SUB>) and tension in the presence or absence of Y-27632 or GF 109203X were measured simultaneously using the acetoxymethyl ester of fura-2-loaded aortic strips. Cumulative mepivacaine concentration-response curves were generated in the presence or absence of the following inhibitors: Rho kinase inhibitor Y-27632, protein kinase C (PKC) inhibitor GF 109203X, extracellular signal-regulated kinase (ERK) inhibitor PD 98059, c-Jun NH<SUB>2</SUB>-terminal kinase (JNK) inhibitor SP600125, and p38 mitogen-activated protein kinase (MAPK) inhibitor SB 203580. Phosphorylation of PKC and MAPK, and membrane translocation of Rho kinase were detected in vascular smooth muscle cells by Western blotting. The slope of the mepivacaine-induced [Ca<SUP>2+</SUP>]<SUB>i</SUB>-tension curve was higher than that of the KCl-induced [Ca<SUP>2+</SUP>]<SUB>i</SUB>-tension curve. Pretreatment with Y-27632 or GF 109203X shifted the mepivacaine-induced [Ca<SUP>2+</SUP>]<SUB>i</SUB>-tension curve to the lower right. Pretreatment with Y-27632, GF 109203X, PD 98059, or SP600125 attenuated mepivacaine-induced contraction in a concentration-dependent manner. Y-27632 and GF 109203X attenuated mepivacaine-induced Rho kinase membrane translocation and PKC phosphorylation, respectively. PD 98059 and SP600125 attenuated mepivacaine-induced ERK and JNK phosphorylation, respectively. Taken together, these results indicate that mepivacaine-induced contraction involves increased calcium sensitization mediated by Rho kinase and PKC. Such contraction mainly involves activation of ERK- and JNK-mediated pathways.