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Snail Switches 5-FU-induced Apoptosis to Necrosis through Akt/PKB Activation and p53 Down-regulation
이수연, 전현민, 주민경, 김초희, 정의경, 박혜경, 강호성, Lee. Su-Yeon, Jeon. Hyun-Min, Ju. Min-Kyung, Kim. Cho-Hee, Jeong. Eui-Kyong, Park. Hye-Gyeong, Kang. Ho-Su 한국생명과학회 생명과학회지 6 Pages
한국생명과학회 생명과학회지 2012, Vol.22 No.8 1018-1023 (6 pages)
세포사멸이 억제되고 세포괴사가 일어남을 확인하였다. DOX 처리 및 Snail expression vectors인 pCR3.1-Snail-Flg와 phosphorylation-resistant mutant Snail vector인 pCR3.1-S104, 107A Snail-Flg을 이용하여 Snail을 과발현 시킨 경우 ERK1/2의 활성에는 영향을 주지 않는 반면 PTEN 발현억제 및 불활성화, 그리고 Akt/PKB 활성화가 유도됨을 관찰하였다. 또한, Snail은 5-FU에 의한 p53의 발현을 억제한다는 사실을 확인하였다. 따라서 Snail은 prosurvival kinase인 Akt/PKB의 활성화와 p53 억제를 통해 5-FU에 의한 세포사멸을... -
Direct tyrosine phosphorylation of Akt/PKB by epidermal growth factor receptor
배순식, 최장현, 윤성지, 김은경, 오용석, 김치대, 서판길, Bae. Sun-Sik, Choi. Jang-Hyun, Yun. Sung-Ji, Kim. Eun-Kyung, Oh. Yong-Suk, Kim. Chi-Dae, Suh. Pann-Ghill 한국생명과학회 생명과학회지 7 Pages
한국생명과학회 생명과학회지 2007, Vol.17 No.2 185-191 (7 pages)
Akt/PKB는 세포의 증식, 분화, 사멸, 혈관신생 등 매우 많은 생리활성 조절에 있어 매우 중요한 역할을 수행한다. 우리는 Akt/PKB의 tyrosine잔기의 인산화가 $Thr^{308}$ 인산화에 필수적임을 밝혔다. COS-7 세포주에 EGF를 처 리하면 Akt/PKB의 tyrosine 잔기에 인산화가 촉진되었으며 이러한 인산화 촉진은 Akt/PKB에 myristoylation site를 이용해 세포막으로 이동시키면 더욱 더 증가하였다. 특히, 분리된 Akt/PKB와 EGF 수용체를 이용해 인산화 반응을 실시하면 tyrosine잔기의 인산화뿐만 아니라 $Ser^{473}$에 대한 인산화도... -
대장균을 이용한 Akt/PKB Protein Kinase의 발현 및 활성화
이재학, Lee. Jae-Hag 한국미생물생명공학회 한국미생물·생명공학회지 5 Pages
한국미생물생명공학회 한국미생물·생명공학회지 2009, Vol.37 No.2 105-109 (5 pages)
중 serine/threonine kinase에 속하는 Akt/PKB는 세포 생존과 사멸, 당대사 등을 조절하는 것으로 알려져 있다. 이러한 이유로, Akt/PKB 단백질은 천연물질들로부터 항암제를 탐색하기 위한 한 가지 target으로 사용되어 왔다. 본 연구에서는 Akt/PKB 단백질을 대량으로 생산하기 위하여 대장균의 단백질 발현 시스템을 이용하여 human Akt/PKB 단백질을 발현시켰다. 대장균에서 대량 발현된 Akt는 일반적인 조건에서는 inclusion body를 형성하였다. 배양온도 $27^{circ}C$에서 0.01-0.09 mM IPTG로 발현 유도 시 발현된 human Akt/PKB... -
Activation of Akt/PKB at Serine 473 by N-acetylphytosphingosine (NAPS) and $C_{2}-ceramide$ Reduces Melanin Synthesis in B16F10 Mouse Melanoma Cells
Yi. Seh-Yoon, Han. Seon-Kyu, Park. Mee-Kyung, Yoo. Young-Sook 대한독성유전단백체학회 Molecular & cellular toxicology 8 Pages
대한독성유전단백체학회 Molecular & cellular toxicology 2006, Vol.2 No.2 81-88 (8 pages)
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Insulin-like growth factor-1 improves diabetic cardiomyopathy through antioxidative and anti-inflammatory processes along with modulation of Akt/GSK-3β signaling in rats
ChengYuWang, XiangDanLiZhiHongHao, DongyuanXu 대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 7 Pages
대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 2016, Vol.20 No.6 7 613-619 (7 pages)
kinase (GSK-3β). IGF-1 treatment, however, attenuated the metabolic abnormalities and myocardial apoptosis, interstitial fibrosis, oxidative stress and inflammation seen in diabetic rats, while also increasing the phosphorylation levels of Akt and GSK-3β. These findings suggest that IGF-1 ameliorates the pathophysiological progress of DCM along with an activation of the Akt/GSK-3β signaling pathway. Our findings suggest that IGF-1 could be a potential therapeutic choice for controlling DCM. -
Lnk is an important modulator of insulin-like growth factor-1/Akt/peroxisome proliferator-activated receptor-gamma axis during adipogenesis of mesenchymal stem cells
JunHeeLee, SangHunLee, HyangSeonLee, SeungTaekJi, SeokYunJung, JaeHoKim, 6, SunSikBae, Sang-MoKwon 대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 8 Pages
대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 2016, Vol.20 No.5 3 459-466 (8 pages)
that IGF-1-induced increase in the phosphorylation of Akt and mammalian target of rapamycin was triggered by the dissociation of the IGF-1R–Lnk complex. Expression levels of a pivotal transcription factor peroxisome proliferatoractivated receptor gamma (PPAR-γ) and its adipogenic target genes (LPL and FABP4) significantly decreased in Lnk –/– MSCs. These results suggested that Lnk adaptor protein regulated the adipogenesis of MSCs through the IGF-1/Akt/PPAR-γ pathway. -
Activation of Akt/protein kinase B mediates the protective effects of mechanical stretching against myocardial ischemia-reperfusion injury
Chan-Hyung Kim*, Jia Hao, Hee-Yul Ahn, Si Wook Kim* 대한수의학회 Journal of Veterinary Science 10 Pages
대한수의학회 Journal of Veterinary Science 2012, 제 13권 제 3호 4 235-244 (10 pages)
Akt/protein kinase B is a well-known cell survival factor and activated by many stimuli including mechanical stretching. Therefore, we evaluated the cardioprotective effect of a brief mechanical stretching of rat hearts and determined whether activation of Akt through phosphatidylinositol 3-kinase (PI3K) is involved in stretch-induced cardioprotection (SIC). Stretch preconditioning reduced infarct size and improved post- ischemic cardiac function compared to the control group. Phosphorylation of... -
Inhibition of eNOS/sGC/PKG Pathway Decreases Akt Phosphorylation Induced by Kainic Acid in Mouse Hippocampus
SangHyunLee, JongSeonByun, PilJaeKong, HeeJaeLee, DukKyungKim, HaeSungKim, Jong-HeeSohn, JaeJunLee, , SoYoungLim, WanjooChun, SungSooKim 대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 7 Pages
대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 2010, Vol.14 No.1 6 37-43 (7 pages)
The serine/threonine kinase Akt has been shown to play a role of multiple cellular signaling pathways and act as a transducer of many functions initiated by growth factor receptors that activate phosphatidylinositol 3-kinase (PI3K). It has been reported that phosphorylated Akt activates eNOS resulting in the production of NO and that NO stimulates soluble guanylate cyclase (sGC), which results in accumulation of cGMP and subsequent activation of the protein kinase G (PKG). It has been also... -
Comparative Effects of PKB-α and PKC-ζ on the Phosphorylation of GLUT4-Containing Vesicles in Rat Adipocytes
Jong-SikHah 대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 8 Pages
대한생리학회-대한약리학회 The Korean Journal of Physiology & Pharmacology 2000, Vol.4 No.6 7 479-486 (8 pages)
B (PKB)/Akt and PKC-ζ, those are known as the downstream target of PI3-kinase in regulation of GLUT4 translocation, is not known yet. An interesting possibility is that these protein kinases phosphorylate GLUT4 directly in this process. In the present study, PKB-α and PKC-ζ were added exogenously to GLUT4-containing vesicles purified from low density microsome (LDM) of the rat adipocytes by immunoadsorption and immunoprecipitation for direct phosphorylation of GLUT4. Interestingly GLUT4 was...
