참고문헌
- Fan G, Jiang X, Wu X et al (2016) Anti-inflammatory activity of Tanshinone IIA in LPS-stimulated RAW264.7 macrophages via miRNAs and TLR4-NF-kappaB pathway. Inflammation 39, 375-384 https://doi.org/10.1007/s10753-015-0259-1
- Duffield JS (2003) The inflammatory macrophage: a story of Jekyll and Hyde. Clin Sci 104, 27-38 https://doi.org/10.1042/CS20020240
- Fujihara M, Muroi M, Tanamoto K, Suzuki T, Azuma H and Ikeda H (2003) Molecular mechanisms of macrophage activation and deactivation by lipopolysaccharide: roles of the receptor complex. Pharmacol Ther 100, 171-194 https://doi.org/10.1016/j.pharmthera.2003.08.003
- Chung HY, Cesari M, Anton S et al (2009) Molecular inflammation as an underlying mechanism of aging: the anti-inflammatory action of calorie restriction. Ageing Res Rev 8, 18-30 https://doi.org/10.1016/j.arr.2008.07.002
- Korhonen R, Lahti A, Kankaanranta H and Moilanen E (2005) Nitric oxide production and signaling in inflammation. Curr Drug Targets Inflamm Allergy 4, 471-479 https://doi.org/10.2174/1568010054526359
- Grilli M and Memo M (1999) Possible role of NF-kappaB and p53 in the glutamate-induced pro-apoptotic neuronal pathway. Cell Death Differ 6, 22-27 https://doi.org/10.1038/sj.cdd.4400463
- Lawrence T, Gilroy DW, Colville-Nash PR and Willoughby DA (2001) Possible new role for NF-kB in the resolution of inflammation. Nat Med 7, 1291-1297 https://doi.org/10.1038/nm1201-1291
- Riehemann K, Behnke B and Schulze-Osthoff K (1999) Plant extracts from stinging nettle (Urtica dioica), an antirheumatic remedy, inhibit the proinflammatory transcription factor NF-kB. FEBS Lett 442, 89-94 https://doi.org/10.1016/S0014-5793(98)01622-6
- Ivashkiv LB (2011) Inflammatory signaling in macrophages: transitions from acute to tolerant and alternative activation states. Eur J Immunol 41, 2477-2481 https://doi.org/10.1002/eji.201141783
- Sica A and Mantovani A (2012) Macrophage plasticity and polarization: in vivo veritas. J Clin Invest 122, 787-795 https://doi.org/10.1172/JCI59643
- Shibayama H, Takai E, Matsumura I et al (2004) Identification of a cytokine-induced antiapoptotic molecule anamorsin essential for definitive hematopoiesis. J Exp Med 199, 581-592 https://doi.org/10.1084/jem.20031858
- Li X, Wu K and Fan D (2010) CIAPIN1 as a therapeutic target in cancer. Expert Opin Ther Targets 14, 603-610 https://doi.org/10.1517/14728221003774127
- Hao Z, Li X, Qiao T, Du R, Hong L and Fan D (2006) CIAPIN1 confers multidrug resistance by upregulating the expression of MDR-1 and MRP-1 in gastric cancer cells. Cancer Biol Ther 5, 261-266 https://doi.org/10.4161/cbt.5.3.2381
- Li X, Fan R, Zou X et al (2008) Reversal of multidrug resistance of gastric cancer cells by down-regulation of CIAPIN1 with CIAPIN1 siRNA. Mol Biol 42, 102-109
- Park KA, Yun N, Shin DI et al (2011) Nuclear translocation of anamorsin during drug-induced dopaminergic neurodegeneration in culture and in rat brain. J Neural Transm 118, 433-444 https://doi.org/10.1007/s00702-010-0490-8
- Wang X, Pan J and Li J (2015) Cytokine-induced apoptosis inhibitor 1 inhibits the growth and proliferation of multiple myeloma. Mol Med Res 12, 2056-2062 https://doi.org/10.3892/mmr.2015.3656
- Sethi G, Shanmugam MK, Ramachandran L, Kumar AP and Tergaonkar V (2012) Multifaceted link between cancer and inflammation. Biosci Rep 32, 1-15 https://doi.org/10.1042/BSR20100136
- Sethi G and Tergaonkar V (2009) Potential pharmacological control of the NF-kappaB pathway. Trends Pharmacol Sci 30, 313-321 https://doi.org/10.1016/j.tips.2009.03.004
- Lemmon MA and Schlessinger J (2010) Cell signaling by receptor tyrosine kinases. Cell 141, 1117-1134 https://doi.org/10.1016/j.cell.2010.06.011
- El-Andaloussi S, Holm T and Langel U (2005) Cell-penetrating peptides: mechanisms and applications. Curr Pharm Des 11, 3597-3611 https://doi.org/10.2174/138161205774580796
- Wadia JS and Dowdy SF (2002) Protein transduction technology. Curr Opin Biotechnol 13, 52-56 https://doi.org/10.1016/S0958-1669(02)00284-7
- Ramsey JD and Flynn NH (2015) Cell-penetrating peptides transport therapeutics into cells. Pharmacol Ther 54, 78-86 https://doi.org/10.1016/j.pharmthera.2015.07.003
- Zhang X, Li Y, Cheng Y et al (2015) Tat PTD-endostatin: A novel anti-angiogenesis protein with ocular barrier permeability via eye-drops. Biochim Biophys Acta 1850, 1140-1149 https://doi.org/10.1016/j.bbagen.2015.01.019
- Sakurazawa M, Katsura K, Saito M, Asoh S, Ohta S and Katayama Y (2012) Mild hypothermia enhanced the protective effect of protein therapy with transductive anti-death FNK protein using a rat focal transient cerebral ischemia model. Brain Res 1430, 86-92 https://doi.org/10.1016/j.brainres.2011.10.041
- Kim MJ, Park M, Kim DW et al (2015) Transduced PEP-1-PON1 proteins regulate microglial activation and dopaminergic neuronal death in a Parkinson's disease model. Biomaterials 64, 45-56 https://doi.org/10.1016/j.biomaterials.2015.06.015
- Kim MJ, Kim DW, Park JH et al (2013) PEP-1-SIRT2 inhibits inflammatory response and oxidative stress-induced cell death via expression of antioxidant enzymes in murine macrophages. Free Radic Biol Med 63, 432-445 https://doi.org/10.1016/j.freeradbiomed.2013.06.005
- Shin MJ, Kim DW, Lee YP et al (2014) Tat-glyoxalase protein inhibits against ischemic neuronal cell damage and ameliorates ischemic injury. Free Radic Biol Med 67, 195-210 https://doi.org/10.1016/j.freeradbiomed.2013.10.815
- Yeo HJ, Shin MJ, Yeo EJ et al (2019) Tat-CIAPIN1 inhibits hippocampal neuronal cell damage through the MAPK and apoptotic signaling pathways. Free Radic Biol Med 135, 68-78 https://doi.org/10.1016/j.freeradbiomed.2019.02.028
- Moon JI, Han MJ, Yu SH et al (2019) Enhanced delivery of protein fused to cell penetrating peptides to mammalian cells. BMB Rep 52, 324-329 https://doi.org/10.5483/BMBRep.2019.52.5.195
- Yeo HJ, Yeo EJ, Shin MJ et al (2018) Protective effects of Tat-DJ-1 protein against streptozotocin-induced diabetes in a mice model. BMB Rep 51, 362-367 https://doi.org/10.5483/BMBRep.2018.51.7.101
- Jaiswal YK, Jaiswal MK, Agrawal V and Chaturvedi MM (2009) Bacterial endotoxin (LPS)-induced DNA damage in preimplanting embryonic and uterine cells inhibits implantation. Fertil Steril 91, 2095-2103 https://doi.org/10.1016/j.fertnstert.2008.04.050
- Uto T, Suangkaew N, Morinaga O, Kariyazono H, Oiso S and Shoyama Y (2010) Eriobotryae folium extract suppresses LPS-induced iNOS and COX-2 expression by inhibition of NF-kappaB and MAPK activation in murine macrophages. Am J Chin Med 38, 985-994 https://doi.org/10.1142/S0192415X10008408
-
Gao Y, Jiang W, Dong C et al (2012) Anti-inflammatory effects of sophocarpine in LPS-induced RAW 264.7 cells via NF-
${\kappa}B$ and MAPKs signaling pathways. Toxicol In Vitro 26, 1-6 https://doi.org/10.1016/j.tiv.2011.09.019 -
Cao F, Liu T, Xu Y, Xu D and Feng S (2015) Curcumin inhibits cell proliferation and promotes apoptosis in human osteoclastoma cell through MMP-9, NF-
${\kappa}B$ and JNK signaling pathways. Int J Clin Exp Pathol 8, 6037-6045 -
Kim KN, Heo SJ, Yoon WJ et al (2010) Fucoxanthin inhibits the inflammatory response by suppressing the activation of NF-
${\kappa}B$ and MAPKs in lipopolysaccharideinduced RAW 264.7 macrophages. Eur J Pharmacol 649, 369-375 https://doi.org/10.1016/j.ejphar.2010.09.032 - Ki YW, Park JH, Lee JE, Shin IC and Koh HC (2013) JNK and p38 MAPK regulate oxidative stress and the inflammatory response in chlorpyrifos-induced apoptosis. Toxicol Lett 218, 235-245 https://doi.org/10.1016/j.toxlet.2013.02.003
- Barton GM and Medzhitov R (2003) Toll-like receptor signaling pathways. Science 300, 1524-1525 https://doi.org/10.1126/science.1085536
- Langford MP, McGee DJ, Ta KH, Redens TB and Texada DE (2011) Multiple caspases mediate acute renal cell apoptosis induced by bacterial cell wall components. Ren Fail 33, 192-206 https://doi.org/10.3109/0886022X.2011.553304
- Yun N, Lee YM, Kim C et al (2014) Anamorsin, a novel caspase-3 substrate in neurodegeneration. J Biol Chem 289, 22183-22195 https://doi.org/10.1074/jbc.M114.552679
- Wang J, Li Q, Wang C et al (2016) Knock-down of CIAPIN1 sensitizes K562 chronic myeloid leukemia cells to Imatinib by regulation of cell cycle and apoptosisassociated members via NF-kB and ERK5 signaling pathways. Biochem Pharmacol 99, 132-145 https://doi.org/10.1016/j.bcp.2015.12.002
- Fujihara M, Muroi M, Tanamoto K, Suzuki T, Azuma H and Ikeda H (2003) Molecular mechanisms of macrophage activation and deactivation by lipopolysaccharide: roles of the receptor complex. Pharmacol Ther 100, 171-194 https://doi.org/10.1016/j.pharmthera.2003.08.003
-
Khan S, Shin EM, Choi RJ et al (2011) Suppression of LPS-induced inflammatory and NF-
${\kappa}B$ responses by anomalin in RAW 264.7 macrophages. J Cell Biochem 112, 2179-2188 https://doi.org/10.1002/jcb.23137 -
Su YW, Chiou WF, Chao SH, Lee MH, Chen CC and Tsai YC (2011) Ligustilide prevents LPS-induced iNOS expression in RAW 264.7 macrophages by preventing ROS production and down-regulating the MAPK, NF-
${\kappa}B$ and AP-1 signaling pathways. Int Immunopharmacol 11, 1166-1172 https://doi.org/10.1016/j.intimp.2011.03.014 - Stanley PL, Steiner S, Havens M and Tramposch KM (1991) Mouse skin inflammation induced by multiple topical applications of 12-O-tetradecanoylphorbol-13-acetate. Skin Pharmacol 4, 262-271 https://doi.org/10.1159/000210960
- Hoffmann A and Baltimore D (2006) Circuity of nuclear factor kappaB signaling. Immunol Rev 210, 171-186 https://doi.org/10.1111/j.0105-2896.2006.00375.x
- Baud V and Karin M (2009) Is NF-kappaB a good target for cancer therapy? Hopes and pitfalls. Nat Rev Drug Discovery 8, 33-40 https://doi.org/10.1038/nrd2781
- Kundu JK, Shin YK and Surh YJ (2006) Resveratrol modulates phorbol ester-induced pro-inflammatory signal transduction pathways in mouse skin in vivo: NF-kappaB and AP-1 as prime targets. Biochem Pharmacol 72, 1506-1515 https://doi.org/10.1016/j.bcp.2006.08.005
- Murakami A, Nakamura Y, Torikai K et al (2000) Inhibitory effect of citrus nobiletin on phorbol esterinduced skin inflammation, oxidative stress, and tumor promotion in mice. Cancer Res 60, 5059-5066
- Chung WY, Park JH, Kim MJ et al (2007) Xanthorrhizol inhibits 12-O-tetradecanoylphorbol-13-acetate-induced acute inflammation and two-stage mouse skincarcinogenesis by blocking the expression of ornithine decarboxylase, cyclooxygenase-2 and inducible nitric oxide synthase through mitogen-activated protein kinases and/or the nuclear factor-kappa B. Carcinogen 28, 1224-1231 https://doi.org/10.1093/carcin/bgm005