Nrf2 Nuclear(Nrf2 핵)란 무엇입니까?
Nrf2 Nuclear Nrf2 핵 - followed by quantification of Nrf2 nuclear using a luciferase reporter assay. [1]루시퍼라제 리포터 분석을 사용한 Nrf2 핵의 정량화. [1]
dose dependent manner 용량 의존적 방식
Further mechanistic studies confirmed that Pts increased antioxidant enzyme expression in a dose-dependent manner, which was related to Nrf2 nuclear translocation. [1] Nrf2 nuclear localization and autophagy, also increased in a dose dependent manner. [2] Our results demonstrate that Daph dramatically upregulated the antioxidant enzyme in a dose dependent manner, in association with induction of Nrf2 nuclear translocation and decreased Keap1 protein expression. [3]추가 기계 연구에서 Pts가 Nrf2 핵 전위와 관련된 항산화 효소 발현을 용량 의존적으로 증가시키는 것으로 확인되었습니다. [1] Nrf2 핵 국소화 및 자가포식 또한 용량 의존적 방식으로 증가했습니다. [2] nan [3]
Induced Nrf2 Nuclear 유도된 Nrf2 핵
Pretreatment with wortmannin, PI3K/AKT inhibitor, abolished BP induced Nrf2 nuclear translocation and HO-1 level. [1] Additionally, LY294002, a specific PI3K/Akt inhibitor, significantly suppressed FA-induced Nrf2 nuclear translocation and HO-1 protein expression and inhibited FA-induced occludin and ZO-1 protein expression. [2] Treatment with DEX and the GSK‐3β inhibitor SB216367 promoted phosphorylation of GSK‐3β, induced Nrf2 nuclear translocation, and increased transcription of the Nrf2 target genes heme oxygenase‐1 and NAD(P)H quinone oxidoreductase‐1, primarily in renal tubules. [3] In in vitro study, ACSO induced Nrf2 nuclear translocation in HepG2 cells, which is recognized as an initial trigger to induce antioxidative and detoxifying enzymes. [4] F508del CFTR correctors induced Nrf2 nuclear translocation, Nrf2-dependent luciferase activity, and transcriptional activation of target genes. [5]wortmannin, PI3K/AKT 억제제로 전처리하면 BP가 Nrf2 핵 전위 및 HO-1 수준을 유도했습니다. [1] 또한, 특정 PI3K/Akt 억제제인 LY294002는 FA 유도 Nrf2 핵 전위 및 HO-1 단백질 발현을 유의하게 억제하고 FA 유도 occludin 및 ZO-1 단백질 발현을 억제했습니다. [2] nan [3] nan [4] nan [5]
Promoted Nrf2 Nuclear Nrf2 원자력 추진
BRD4 inhibition promoted Nrf2 nuclear translocation and upregulated the transcriptional activity of Nrf2/antioxidant response element (ARE). [1] Additionally, biochanin A promoted Nrf2 nuclear translocation, promoted the expression of HO-1, and inhibited NF-κB activation in ischemic brain injury. [2] TSA markedly promoted Nrf2 nuclear translocation and its acetylation. [3] Berberine promoted Nrf2 nuclear translocation and phosphorylation in vitro. [4] Western blot analyses and immunofluorescence staining demonstrated that Swe pretreatment promoted Nrf2 nuclear translocation from Keap1-Nrf2 complex and enhanced the expressions of NAD(P)H: quinone oxidoreductase-1 (NQO1) and heme oxygenase-1 (HO-1) both in vivo and in vitro, while the expressions could be reversed by a Nrf2 inhibitor. [5]BRD4 억제는 Nrf2 핵 전위를 촉진하고 Nrf2/항산화 반응 요소(ARE)의 전사 활성을 상향 조절했습니다. [1] 또한, 바이오카닌 A는 Nrf2 핵 전위를 촉진하고, HO-1의 발현을 촉진하고, 허혈성 뇌 손상에서 NF-κB 활성화를 억제했습니다. [2] nan [3] nan [4] nan [5]
Increased Nrf2 Nuclear Nrf2 핵 증가
Additionally, we demonstrated that NGF impaired the activation of the JNK/c‐Jun signaling pathway and significantly increased Nrf2 nuclear translocation and HO‐1 expression. [1] These effects were likely due to the amplification of the antioxidant defenses through increased Nrf2 nuclear translocation stimulated by the antioxidants and by the prevention of polyol fructokinase pathway overactivation. [2] Finally, MT increased Nrf2 nuclear translocation, and Nrf2 target genes (HO-1, NQO1, SOD1 and CAT) mRNA expressions in the spleen of AlCl3-exposed rat. [3] Moreover, curcumin pretreatment increased Nrf2 nuclear translocation and downstream enzyme expression, heme oxygenase-1 (HO-1) and NADPH quinone reductase-1 (NQO1). [4]또한, 우리는 NGF가 JNK/c-Jun 신호 전달 경로의 활성화를 손상시키고 Nrf2 핵 전위 및 HO-1 발현을 유의하게 증가시킨다는 것을 입증했습니다. [1] 이러한 효과는 항산화제에 의해 자극된 증가된 Nrf2 핵 전위를 통한 항산화제 방어의 증폭과 폴리올 프럭토키나제 경로 과활성화의 방지로 인한 것 같습니다. [2] nan [3] nan [4]
Induce Nrf2 Nuclear Nrf2 핵 유도
In primary CF cells, F508del-CFTR correctors induce Nrf2 nuclear localization, Nrf2-dependent luciferase activity, and transcriptional activation of target genes. [1] Cells sense ER oxidative protein folding through H2O2, which induces Nrf2 nuclear translocation. [2] Furthermore, We found that BBR can dramatically induce Nrf2 nuclear translocation, increase total Nrf2 levels and enhance ARE activity. [3]1차 CF 세포에서 F508del-CFTR 교정자는 Nrf2 핵 국소화, Nrf2 의존성 루시퍼라제 활성 및 표적 유전자의 전사 활성화를 유도합니다. [1] 세포는 Nrf2 핵 전위를 유도하는 H2O2를 통해 접히는 ER 산화 단백질을 감지합니다. [2] nan [3]
Activated Nrf2 Nuclear 활성화된 Nrf2 핵
Cell-based studies showed that RUT significantly increased the LD50 for hydrogen peroxide (H2O2)-induced cell damage, activated NRF2 nuclear translocation, and suppressed the production of reactive oxygen species (ROS) in H2O2-treated HCT116 cells, activated NRF2 luciferase reporter activities in HCT116 cells and HepG2 cells, and induced the expression of NRF2 target genes in primary intestinal epithelial cells. [1] Additionally, leonurine treatment activated Nrf2 nuclear translocation in both aging mice and normal young mice, and the expression levels of Nrf2 in normal young mice was higher than those in naturally aging mice. [2]세포 기반 연구에 따르면 RUT는 과산화수소(H2O2)로 유도된 세포 손상에 대한 LD50을 유의하게 증가시키고 NRF2 핵 전위를 활성화하고 H2O2 처리된 HCT116 세포에서 활성 산소종(ROS) 생성을 억제하고 NRF2 루시페라제 리포터 활성을 활성화함을 보여주었습니다. HCT116 세포 및 HepG2 세포에서, 그리고 일차 장 상피 세포에서 NRF2 표적 유전자의 발현을 유도하였다. [1] 또한, 레오누린 처리는 노화된 마우스와 정상적인 어린 마우스 모두에서 Nrf2 핵 전위를 활성화시켰고, 정상적인 어린 마우스에서 Nrf2의 발현 수준은 자연적으로 노화된 마우스보다 더 높았다. [2]
nrf2 nuclear translocation Nrf2 핵 이식
Cell-based studies showed that RUT significantly increased the LD50 for hydrogen peroxide (H2O2)-induced cell damage, activated NRF2 nuclear translocation, and suppressed the production of reactive oxygen species (ROS) in H2O2-treated HCT116 cells, activated NRF2 luciferase reporter activities in HCT116 cells and HepG2 cells, and induced the expression of NRF2 target genes in primary intestinal epithelial cells. [1] Furthermore, ILQ treatment to MGN rats showed anti-oxidative effects through the prominent stimulation of Nrf2 signaling pathway and inhibition of Keap1, which consequently increases the Nrf2 nuclear translocation and thereby induces expression of NQO1 and HO-1. [2] Western blot densitometry was used to measure Nrf2 nuclear translocation in Caco2 cells after exposure to RRx-001. [3] Pretreatment with wortmannin, PI3K/AKT inhibitor, abolished BP induced Nrf2 nuclear translocation and HO-1 level. [4] Further studies showed CTE treatment significantly enhanced Sirt1 expression and activated the Nrf2 signaling pathway by the increase of Nrf2 nuclear translocation, NQO-1 and HO-1 expression. [5] BRD4 inhibition promoted Nrf2 nuclear translocation and upregulated the transcriptional activity of Nrf2/antioxidant response element (ARE). [6] Cd‐stimulated Nrf2 nuclear translocation and subsequent elevated expression of Nrf2‐downstream targets were significantly inhibited by PU treatment. [7] LY294002 (PI3K inhibitor) dramatically blocked piceatannol-mediated increasing of Nrf2 nuclear translocation, HO-1 expression, and cytoprotective activity, indicating the involvement of PI3K/Akt pathway in the cytoprotective effect of piceatannol. [8] Additionally, LY294002, a specific PI3K/Akt inhibitor, significantly suppressed FA-induced Nrf2 nuclear translocation and HO-1 protein expression and inhibited FA-induced occludin and ZO-1 protein expression. [9] Additionally, biochanin A promoted Nrf2 nuclear translocation, promoted the expression of HO-1, and inhibited NF-κB activation in ischemic brain injury. [10] Additionally, we demonstrated that NGF impaired the activation of the JNK/c‐Jun signaling pathway and significantly increased Nrf2 nuclear translocation and HO‐1 expression. [11] Our data showed that TP induced oxidative stress and cell damage in the rat renal tubular epithelial cell line NRK-52E cells by activation of GSK-3β and nuclear translocation of Fyn, which resulted in decreased Nrf2 nuclear translocation. [12] Further mechanistic studies confirmed that Pts increased antioxidant enzyme expression in a dose-dependent manner, which was related to Nrf2 nuclear translocation. [13] Treatment with DEX and the GSK‐3β inhibitor SB216367 promoted phosphorylation of GSK‐3β, induced Nrf2 nuclear translocation, and increased transcription of the Nrf2 target genes heme oxygenase‐1 and NAD(P)H quinone oxidoreductase‐1, primarily in renal tubules. [14] TSA markedly promoted Nrf2 nuclear translocation and its acetylation. [15] In addition to its local effects, the BRP2 administration on mouse mesenteric arteries was able to reduce the angiotensin II-induced vasoconstriction by the Nrf2 nuclear translocation, the reduction of the active form of Ras-related C3 botulinum toxin substrate 1 (Rac1), and the NADPH oxidase activity. [16] In in vitro study, ACSO induced Nrf2 nuclear translocation in HepG2 cells, which is recognized as an initial trigger to induce antioxidative and detoxifying enzymes. [17] Hyperglycemia modulates Nrf2 nuclear translocation, IL‐6 secretion and NO levels. [18] Meanwhile, BD was able to upregulate protein levels of Nrf2 and its downstream genes NQO1 and γ-GCS through inducing Nrf2 nuclear translocation, enhancing protein stability, and inhibiting ubiquitination. [19] Berberine promoted Nrf2 nuclear translocation and phosphorylation in vitro. [20] Ginsenoside C‐Y has exhibited photoaging effects by increasing TGF‐β1 level, fortifying Nrf2 nuclear translocation and restricting AP‐1 and MAPK phosphorylation. [21] Cells sense ER oxidative protein folding through H2O2, which induces Nrf2 nuclear translocation. [22] Western blot analyses and immunofluorescence staining demonstrated that Swe pretreatment promoted Nrf2 nuclear translocation from Keap1-Nrf2 complex and enhanced the expressions of NAD(P)H: quinone oxidoreductase-1 (NQO1) and heme oxygenase-1 (HO-1) both in vivo and in vitro, while the expressions could be reversed by a Nrf2 inhibitor. [23] Similarly, XJEK treatment for 2 wk potentiated Nrf2 nuclear translocation and HO-1 expression and inhibited the deficiency of nuclear Nrf2 and HO-1 at 6 wk post-MI compared with that of the MI groups, indicating the attenuation of the renal oxidative stress condition. [24] Western blot analysis showed that the Nrf2 nuclear translocation and MAPK pathway were involved in the potential mechanisms of IRN on cardiac hypertrophy inhibition. [25] Further studies showed that LY294002, aPI3K inhibitor, abolished the effects of SMSO on GSK-3β phosphorylation and Nrf2 nuclear translocation as well as the protective effects on pancreatic β cells. [26] HO-1, NQO1 mRNA/protein expressions and Nrf2 nuclear translocation significantly triggered by tideglusib. [27] These effects were likely due to the amplification of the antioxidant defenses through increased Nrf2 nuclear translocation stimulated by the antioxidants and by the prevention of polyol fructokinase pathway overactivation. [28] Our results demonstrate that Daph dramatically upregulated the antioxidant enzyme in a dose dependent manner, in association with induction of Nrf2 nuclear translocation and decreased Keap1 protein expression. [29] FL prevented t-BHP-induced cytotoxicity and intracellular accumulation of reactive oxygen species through activation of catalase expression via SAPK/JNK phosphorylation and Nrf2 nuclear translocation. [30] Under the effect of SFN, up-regulation of nuclear Nrf2 expression and down-regulation of cytosolic Nrf2 expression were observed, which led to Nrf2 nuclear translocation and enhanced the expression of HO-1. [31] Finally, MT increased Nrf2 nuclear translocation, and Nrf2 target genes (HO-1, NQO1, SOD1 and CAT) mRNA expressions in the spleen of AlCl3-exposed rat. [32] F508del CFTR correctors induced Nrf2 nuclear translocation, Nrf2-dependent luciferase activity, and transcriptional activation of target genes. [33] COS facilitated the Nrf2 nuclear translocation, and knockdown of Nrf2 almost abrogated the cytoprotection of COS, demonstrating that activation of Nrf2 acted as an essential step in this cytoprotective process. [34] In contrast, pretreating adult mice with the selective IGF‐1R inhibitor picropodophyllin diminished exercise‐induced neurogenesis, concurrent with reduced Nrf2 nuclear translocation and proteasome activity. [35] Furthermore, We found that BBR can dramatically induce Nrf2 nuclear translocation, increase total Nrf2 levels and enhance ARE activity. [36] Additionally, leonurine treatment activated Nrf2 nuclear translocation in both aging mice and normal young mice, and the expression levels of Nrf2 in normal young mice was higher than those in naturally aging mice. [37] Moreover, curcumin pretreatment increased Nrf2 nuclear translocation and downstream enzyme expression, heme oxygenase-1 (HO-1) and NADPH quinone reductase-1 (NQO1). [38] In human proximal tubular epithelial HK-2 cells, CPUY192018 treatment significantly increased Nrf2 protein level and Nrf2 nuclear translocation, which enhanced Nrf2-ARE transcription capacity and the downstream protein content in a Nrf2 dependent manner. [39] KEY FINDING TG or TM induced H9c2 cell injury and ER-phagy and upregulated CRT expression, PERK phosphorylation, Nrf2 nuclear translocation, and expression of ATF4, Beclin 1, and LC3B-II compared with control cells. [40] Molecular data revealed that PB1, a major component in PMR, stabilized Nrf2 by inhibiting the ubiquitination of Nrf2, which led to subsequent activation of the Nrf2-ARE pathway, including the enhancements of Nrf2 nuclear translocation, Nrf2-ARE binding and ARE transcriptional activity. [41]세포 기반 연구에 따르면 RUT는 과산화수소(H2O2)로 유도된 세포 손상에 대한 LD50을 유의하게 증가시키고 NRF2 핵 전위를 활성화하고 H2O2 처리된 HCT116 세포에서 활성 산소종(ROS) 생성을 억제하고 NRF2 루시페라제 리포터 활성을 활성화함을 보여주었습니다. HCT116 세포 및 HepG2 세포에서, 그리고 일차 장 상피 세포에서 NRF2 표적 유전자의 발현을 유도하였다. [1] 또한, MGN 쥐에 대한 ILQ 처리는 Nrf2 신호전달 경로의 현저한 자극과 Keap1의 억제를 통해 항산화 효과를 나타내어 결과적으로 Nrf2 핵 전위를 증가시켜 NQO1 및 HO-1의 발현을 유도하였다. [2] nan [3] wortmannin, PI3K/AKT 억제제로 전처리하면 BP가 Nrf2 핵 전위 및 HO-1 수준을 유도했습니다. [4] 추가 연구는 CTE 처리가 Sirt1 발현을 유의하게 향상시키고 Nrf2 핵 전위, NQO-1 및 HO-1 발현의 증가에 의해 Nrf2 신호 전달 경로를 활성화함을 보여주었습니다. [5] BRD4 억제는 Nrf2 핵 전위를 촉진하고 Nrf2/항산화 반응 요소(ARE)의 전사 활성을 상향 조절했습니다. [6] nan [7] LY294002(PI3K 억제제)는 Nrf2 핵 전위, HO-1 발현 및 세포 보호 활성의 piceatannol 매개 증가를 극적으로 차단하여 piceatannol의 세포 보호 효과에서 PI3K/Akt 경로의 관련성을 나타냅니다. [8] 또한, 특정 PI3K/Akt 억제제인 LY294002는 FA 유도 Nrf2 핵 전위 및 HO-1 단백질 발현을 유의하게 억제하고 FA 유도 occludin 및 ZO-1 단백질 발현을 억제했습니다. [9] 또한, 바이오카닌 A는 Nrf2 핵 전위를 촉진하고, HO-1의 발현을 촉진하고, 허혈성 뇌 손상에서 NF-κB 활성화를 억제했습니다. [10] 또한, 우리는 NGF가 JNK/c-Jun 신호 전달 경로의 활성화를 손상시키고 Nrf2 핵 전위 및 HO-1 발현을 유의하게 증가시킨다는 것을 입증했습니다. [11] nan [12] 추가 기계 연구에서 Pts가 Nrf2 핵 전위와 관련된 항산화 효소 발현을 용량 의존적으로 증가시키는 것으로 확인되었습니다. [13] nan [14] nan [15] 국소 효과 외에도 마우스 장간막 동맥에 대한 BRP2 투여는 Nrf2 핵 전위에 의한 안지오텐신 II 유도 혈관 수축, Ras 관련 C3 보툴리눔 독소 기질 1(Rac1)의 활성 형태 감소 및 NADPH 산화효소 활성 [16] nan [17] nan [18] nan [19] nan [20] nan [21] 세포는 Nrf2 핵 전위를 유도하는 H2O2를 통해 접히는 ER 산화 단백질을 감지합니다. [22] nan [23] nan [24] Western blot 분석은 Nrf2 핵 전위와 MAPK 경로가 심장 비대 억제에 대한 IRN의 잠재적 기전에 관여한다는 것을 보여주었습니다. [25] 추가 연구에 따르면 aPI3K 억제제인 LY294002는 GSK-3β 인산화 및 Nrf2 핵 전위에 대한 SMSO의 효과와 췌장 β 세포에 대한 보호 효과를 제거했습니다. [26] HO-1, NQO1 mRNA/단백질 발현 및 Nrf2 핵 전위는 tideglusib에 의해 크게 촉발되었습니다. [27] 이러한 효과는 항산화제에 의해 자극된 증가된 Nrf2 핵 전위를 통한 항산화제 방어의 증폭과 폴리올 프럭토키나제 경로 과활성화의 방지로 인한 것 같습니다. [28] nan [29] FL은 SAPK/JNK 인산화 및 Nrf2 핵 전위를 통한 카탈라아제 발현의 활성화를 통해 t-BHP에 의한 세포 독성 및 활성 산소 종의 세포 내 축적을 방지했습니다. [30] SFN의 효과 하에 핵 Nrf2 발현의 상향 조절 및 세포질 Nrf2 발현의 하향 조절이 관찰되었으며, 이는 Nrf2 핵 전위를 유도하고 HO-1의 발현을 향상시켰다. [31] nan [32] nan [33] COS는 Nrf2 핵 전위를 촉진하고 Nrf2의 녹다운은 COS의 세포 보호를 거의 폐지하여 Nrf2의 활성화가 이 세포 보호 과정에서 필수적인 단계로 작용함을 보여줍니다. [34] nan [35] nan [36] 또한, 레오누린 처리는 노화된 마우스와 정상적인 어린 마우스 모두에서 Nrf2 핵 전위를 활성화시켰고, 정상적인 어린 마우스에서 Nrf2의 발현 수준은 자연적으로 노화된 마우스보다 더 높았다. [37] nan [38] 인간 근위 세뇨관 상피 HK-2 세포에서 CPUY192018 처리는 Nrf2 단백질 수준과 Nrf2 핵 전위를 유의하게 증가시켜 Nrf2-ARE 전사 능력과 Nrf2 의존적 방식으로 다운스트림 단백질 함량을 향상시켰습니다. [39] 핵심 발견 TG 또는 TM은 대조군 세포와 비교하여 H9c2 세포 손상 및 ER-파지를 유도하고 CRT 발현, PERK 인산화, Nrf2 핵 전위 및 ATF4, Beclin 1 및 LC3B-II의 발현을 상향 조절하였다. [40] 분자 데이터는 PMR의 주요 구성요소인 PB1이 Nrf2의 유비퀴틴화를 억제하여 Nrf2를 안정화시켰으며, 이는 Nrf2 핵 전위, Nrf2-ARE 결합 및 ARE 전사 활성의 향상을 포함하여 Nrf2-ARE 경로의 후속 활성화를 유도함을 보여주었습니다. [41]
nrf2 nuclear accumulation Nrf2 핵 축적
This lingering injury of renal tubules was associated with sustained oxidative stress that was concomitant with an impaired Nrf2 antioxidant defense, marked by mitigated Nrf2 nuclear accumulation and blunted induction of its target antioxidant enzymes, like heme oxygenase (HO)-1. [1] Nrf2 nuclear accumulation was increased and was accompanied by decreased Keap1 expression. [2] APAP subsided Nrf2 nuclear accumulation by inhibition of keap1 degradation, thereby reducing the binding of Nrf2 to ARE, leading to the loss of expression of antioxidant proteins such as HO-1, inducing a series of oxidative stress and apoptosis events. [3] In conclusion, a physiological concentration of luteolin induces the expression of phase II drug-metabolizing enzymes by enhancement of Nrf2 nuclear accumulation through MEK1/2-ERK1/2-mediated phosphorylation of Nrf2, increasing Nrf2 stability and inducing a conformational change of Keap1. [4]신장 세뇨관의 이 지속적인 손상은 Nrf2 핵 축적이 완화되고 헴 옥시게나제(H2O)-1과 같은 표적 항산화 효소의 유도 둔화로 표시되는 손상된 Nrf2 항산화 방어와 수반되는 지속적인 산화 스트레스와 관련이 있습니다. [1] Nrf2 핵 축적이 증가하고 Keap1 발현이 감소했습니다. [2] nan [3] 결론적으로, 생리학적 농도의 루테올린은 MEK1/2-ERK1/2가 매개하는 Nrf2 인산화를 통해 Nrf2 핵 축적을 증가시켜 Nrf2 안정성을 증가시키고 Keap1의 구조적 변화를 유도하여 2상 약물 대사 효소의 발현을 유도한다. [4]
nrf2 nuclear factor Nrf2 핵 인자
In vitro activity and gene expression of superoxide dismutase (SOD), catalase (Cat), and Nrf2 nuclear factor were measured. [1] Abbreviations: ACTB: actin beta; ATG5: autophagy related 5; BAF: bafilomycin A1; BECN1: beclin 1; CAT: catalase; CSF2: colony stimulating factor 2; CT: control; CYCS (cytochrome C: somatic); DCs: dendritic cells; EBV: Epstein-Barr virus; GSR: glutathione-disulfide reductase; KEAP1: kelch like ECH associated protein 1; IL4: interleukin 4; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; MET: metformin; NAC: N-acetylcysteine; NFE2L2/NRF2 nuclear factor: erythroid 2 like 2; NRF1 (nuclear respiratory factor 1); clPARP1: cleaved poly(ADP-ribose) polymerase; Rapa: Rapamycin; ROS: reactive oxygen species; SQSTM1/p62: sequestosome 1; TFAM: (transcription factor A: mitochondrial); TUBA1A: tubulin alpha 1a. [2]Superoxide dismutase(SOD), catalase(Cat), Nrf2 핵인자의 in vitro 활성과 유전자 발현을 측정하였다. [1] 약어: ACTB: 액틴 베타; ATG5: 자가포식 관련 5; BAF: 바필로마이신 A1; BECN1: 베클린 1; CAT: 카탈라제; CSF2: 집락 자극 인자 2; CT: 통제; CYCS(사이토크롬 C: 체세포); DC: 수지상 세포; EBV: 엡스타인-바 바이러스; GSR: 글루타티온-디설파이드 환원효소; KEAP1: 켈치 유사 ECH 관련 단백질 1; IL4: 인터루킨 4; MAP1LC3/LC3: 미세소관 관련 단백질 1 경쇄 3; MET: 메트포르민; NAC: N-아세틸시스테인; NFE2L2/NRF2 핵 인자: 적혈구 2 유사 2; NRF1(핵 호흡 인자 1); clPARP1: 절단된 폴리(ADP-리보스) 폴리머라제; 라파: 라파마이신; ROS: 활성산소종; SQSTM1/p62: sequestosome 1; TFAM: (전사 인자 A: 미토콘드리아); TUBA1A: 튜불린 알파 1a. [2]
nrf2 nuclear localization Nrf2 핵 현지화
In primary CF cells, F508del-CFTR correctors induce Nrf2 nuclear localization, Nrf2-dependent luciferase activity, and transcriptional activation of target genes. [1] Nrf2 nuclear localization and autophagy, also increased in a dose dependent manner. [2]1차 CF 세포에서 F508del-CFTR 교정자는 Nrf2 핵 국소화, Nrf2 의존성 루시퍼라제 활성 및 표적 유전자의 전사 활성화를 유도합니다. [1] Nrf2 핵 국소화 및 자가포식 또한 용량 의존적 방식으로 증가했습니다. [2]
nrf2 nuclear level Nrf2 핵 수준
Moreover, QUIN increased Keap1 and Nrf2 nuclear levels and increased the protein-protein interaction between Keap1 and DPP3 and Keap1 and p62 30 min after QUIN administration. [1] Although the inhibition of PI3K/Akt did not inhibit the Nrf2 nuclear level under 4 μM rhein, LY294002 inhibited the Nrf2 nuclear level under 2 μM rhein and blocked HO-1 expression. [2]더욱이, QUIN은 Keap1 및 Nrf2 핵 수준을 증가시켰고, QUIN 투여 30분 후 Keap1과 DPP3, Keap1 및 p62 사이의 단백질-단백질 상호작용을 증가시켰다. [1] PI3K/Akt의 억제는 4μM rhein에서 Nrf2 핵 수준을 억제하지 않았지만 LY294002는 2μM rhein에서 Nrf2 핵 수준을 억제하고 HO-1 발현을 차단했습니다. [2]