• 제목/요약/키워드: College1

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Phosphorylation by $Ca^{+2}$/calmodulin-dependent Kinase II Regulates Binding of Capsaicin to VR1

  • Koo, Jae-Yeon;Kim, Sang-Sung;Kim, Man-Soo;Park, Seung-Pyo;Shim, Won-Sik;Yang, Young-Duk;Cho, Hwa-Won;Kim, Mi-Sook;Kim, Byung-Moon;Oh, Uh-Taek
    • 대한약학회:학술대회논문집
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    • 대한약학회 2003년도 Proceedings of the Convention of the Pharmaceutical Society of Korea Vol.2-2
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    • pp.128.1-128.1
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    • 2003
  • VR1, a capsaicin receptor, is now known to playa major role in mediating inflammatory thermal nociception. Although the physiological role or biophysical properties of VR1 are known, its activation mechanisms by ligands are poorly understood. Here, we show that VR1 requires phosphorylation by $Ca^{2+}$-calmodulin-dependent kinase II (CaMKII) for its activation by capsaicin. In contrast, dephosphorylation by calcineurin, leads to desensitization of the receptor. Point mutation of VR1 at two putative consensus sites for CaMKII fails to elicit capsaicin-sensitive currents with concomitant reduction in phosphorylation of VR1 in vivo. (omitted)

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Endothelial Aquaporin-1 (AQP1) Expression Is Regulated by Transcription Factor Mef2c

  • Jiang, Yong;Liu, He;Liu, Wen-jing;Tong, Hai-bin;Chen, Chang-jun;Lin, Fu-gui;Zhuo, Yan-hang;Qian, Xiao-zhen;Wang, Zeng-bin;Wang, Yu;Zhang, Peng;Jia, Hong-liang
    • Molecules and Cells
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    • 제39권4호
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    • pp.292-298
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    • 2016
  • Aquaporin 1 (AQP1) is expressed in most microvasculature endothelial cells and forms water channels that play major roles in a variety of physiologic processes. This study aimed to delineate the transcriptional regulation of AQP1 by Mef2c in endothelial cells. Mef2c cooperated with Sp1 to activate human AQP1 transcription by binding to its proximal promoter in human umbilical cord vein endothelial cells (HUVEC). Over-expression of Mef2c, Sp1, or Mef2c/Sp1 increased HUVEC migration and tube-forming ability, which can be abolished AQP1 knockdown. These data indicate that AQP1 is a direct target of Mef2c in regulating angiogenesis and vasculogenesis of endothelial cells.

Glutamic-oxaloacetic transaminase 1 regulates adipocyte differentiation by altering nicotinamide adenine dinucleotide phosphate content

  • Yang, Yang;Cheng, Zhimin;Zhang, Wanfeng;Hei, Wei;Lu, Chang;Cai, Chunbo;Zhao, Yan;Gao, Pengfei;Guo, Xiaohong;Cao, Guoqing;Li, Bugao
    • Animal Bioscience
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    • 제35권2호
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    • pp.155-165
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    • 2022
  • Objective: This study was performed to examine whether the porcine glutamic-oxaloacetic transaminase 1 (GOT1) gene has important functions in regulating adipocyte differentiation. Methods: Porcine GOT1 knockout and overexpression vectors were constructed and transfected into the mouse adipogenic 3T3-L1 cells. Lipid droplets levels were measured after 8 days of differentiation. The mechanisms through which GOT1 participated in lipid deposition were examined by measuring the expression of malate dehydrogenase 1 (MDH1) and malic enzyme (ME1) and the cellular nicotinamide adenine dinucleotide phosphate (NADPH) content. Results: GOT1 knockout significantly decreased lipid deposition in the 3T3-L1 cells (p<0.01), whereas GOT1 overexpression significantly increased lipid accumulation (p<0.01). At the same time, GOT1 knockout significantly decreased the NADPH content and the expression of MDH1 and ME1 in the 3T3-L1 cells. Overexpression of GOT1 significantly increased the NADPH content and the expression of MDH1 and ME1, suggesting that GOT1 regulated adipocyte differentiation by altering the NADPH content. Conclusion: The results preliminarily revealed the effector mechanisms of GOT1 in regulating adipose differentiation. Thus, a theoretical basis is provided for improving the quality of pork and studies on diseases associated with lipid metabolism.

Role of hydrogen peroxide in Rac1 mediated activation of p70s6k signaling pathway

  • Bae, Gyu-Un;Kwon, Hyoung-Keun;Kim, Gwan-Tae;Kim, Yong-Kee;Yoon, Jong-Woo;Cho, Eun-Jung;Lee, Hyang-Woo;Han, Jeung-Whan
    • 대한약학회:학술대회논문집
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    • 대한약학회 2003년도 Proceedings of the Convention of the Pharmaceutical Society of Korea Vol.1
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    • pp.222.1-222.1
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    • 2003
  • The signal transduction pathway leading to the activation of the p70s6k plays an important role in the progression of cells from G0/G1 to S phase of the cell cycle but remains incompletely characterized. We investigated the role of the Rho family G protein Rac1 in H2O2-mediated p70s6k activation. Transient expression of a dominant negative mutants of the small GTP-binding proteins Rac1 (Rac1N17) and Cdc42(Cdc42N17) showed reduced levels of slower migration on Western blots of one-dimensional SDS-PAGE in p70s6k and ERK1/2 by PDFG stimulation. (omitted)

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NMDA Receptor and NO Mediate ET-1-Induced Behavioral and Cardiovascular Effects in Periaqueductal Gray Matter of Rats

  • Ryu, Jung-Su;Shin, Chang-Yell;Yang, Sung-Jun;Lee, Tai-Sang;La, Hyun-O;Song, Hyun-Ju;Yom, Yoon-Ki;Huh, In-Hoi;Sohn, Uy-Dong
    • Archives of Pharmacal Research
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    • 제24권1호
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    • pp.64-68
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    • 2001
  • Endothelin-1 (ET-1 ), a novel and potent vasoconstrictor in blood vessel, is known to have some functions in the rat central nervous system (CNS), In order to investigate the central functions of ET-1 , ET-1 was administered to the periaqueductal gray area (PAC) of anesthetized rats to induce barrel rolling and increase the arterial blood pressure (ABP). ET-1 had a modulatory effect on central cardiovascular and behavioral control. The selective N-methyl-D-aspartate (NMDA) receptor antagonist MK-801 (3${u}m/ol/kg$, i.p.) blocked the ET-1 induced responses, and both the nitric oxide synthase (NOS) inhibitor L-NAME (N-nitro-L-arginine mIThyl-ester 1 nmol/rat) and the nitric oxide (NO) scavenger hemoglobin (15 nmol/rat) had similar effects in redtAcing the IT-1 (10 pmol/rat)-induced behavioral changes and ABP elevation. However, NO donor sodium nitroprusside (SNP 10${u}g$, 1${u}g/rat$) decreased the ET-1 induced ABP elevation, and recovered the ET-1 -induced barrel rolling effect that was reduced by MK-801. These results suggest that ET-1 might have neuromodulatory functions such as ABP elevation and barrel rolling induction in the PAG of the rats via the NMDA receptor and NO.

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