참고문헌
- Arlt A, Grobe O, Sieke A, Kruse ML, Folsch UR, Schmidt WE, Schafer H (2001). Expression of the NF-kappa B target gene IEX-1 (p22/PRG1) does not prevent cell death but instead triggers apoptosis in Hela cells. Oncogene 20:69-76. https://doi.org/10.1038/sj.onc.1204061
- Arlt A, Kruse ML, Breitenbroich M, Gehrz A, Koc B, Minkenberg J, Folsch UR, Schafer H. (2003). The early response gene IEX-1 attenuates NF-kappaB activation in 293 cells, a possible counter-regulatory process leading to enhanced cell death. Oncogene 22: 3343-3351. https://doi.org/10.1038/sj.onc.1206524
- Arlt A, Rosenstiel P, Kruse ML, Grohmann F, Minkenberg J, Perkins ND, Folsch UR, Schreiber S, Schafer H (2008). IEX-1 directly interferes with RelA/p65 dependent transactivation and regulation of apoptosis. Biochim Biophys Acta 1783:941-952. https://doi.org/10.1016/j.bbamcr.2007.12.010
- Barrett AJ (1994). The possible role of neutrophil proteinases in damage to articular cartilage. 1978. Agents Actions 43:194-200; discussion 200-1. https://doi.org/10.1007/BF01986688
- Charles CH, Yoon JK, Simske JS, Lau LF (1993). Genomic structure, cDNA sequence, and expression of gly96, a growth factor-inducible immediate-early gene encoding a short-lived glycosylated protein. Oncogene 8:797-801.
- Felbor U, Dreier L, Bryant RA, Ploegh HL, Olsen BR, Mothes W (2000). Secreted cathepsin L generates endostatin from collagen XVIII. Embo J 19:1187-1194. https://doi.org/10.1093/emboj/19.6.1187
- Garcia J, Ye Y, Arranz V, Letourneux C, Pezeron G, Porteu F (2002). IEX-1: a new ERK substrate involved in both ERK survival activity and ERK activation. Embo J 21:5151-5163. https://doi.org/10.1093/emboj/cdf488
- Green DR, Reed JC (1998). Mitochondria and apoptosis. Science 281:1309-1312. https://doi.org/10.1126/science.281.5381.1309
- Im HJ, Craig TA, Pittelkow MR, Kumar R (2002). Characterization of a novel hexameric repeat DNA sequence in the promoter of the immediate early gene, IEX-1, that mediates 1alpha,25-dihydroxyvitamin D(3)- associated IEX-1 gene repression. Oncogene 21:3706-3714. https://doi.org/10.1038/sj.onc.1205450
- Kim JH, Lee KA, Bae J (2011) BCL2L10 protein induces apoptosis in KGN-human granulosa cells. Develpoment and Reproduction 15:113-120.
- Kobayashi T, Pittelkow MR, Warner GM, Squillace KA, Kumar R (1998). Regulation of a novel immediate early response gene, IEX-1, in keratinocytes by 1alpha, 25-dihydroxyvitamin D3. Biochem Biophys Res Commun 251:868-873. https://doi.org/10.1006/bbrc.1998.9556
- Koblinski JE, Ahram M, Sloane BF (2000). Unraveling the role of proteases in cancer. Clin Chim Acta 291:113-135. https://doi.org/10.1016/S0009-8981(99)00224-7
- Kruse ML, Arlt A, Sieke A, Grohmann F, Grossmann M, Minkenberg J, Folsch UR, Schafer H (2005). Immediate early gene X1 (IEX-1) is organized in subnuclear structures and partially co-localizes with promyelocytic leukemia protein in HeLa cells. J Biol Chem 280: 24849-24856. https://doi.org/10.1074/jbc.M501571200
- Kumar R, Lutz W, Frank E, Im HJ (2004). Immediate early gene X-1 interacts with proteins that modulate apoptosis. Biochem Biophys Res Commun 323:1293-1298. https://doi.org/10.1016/j.bbrc.2004.09.006
- Li W, Yuan XM, Ivanova S, Tracey KJ, Eaton JW, Brunk UT (2003). 3-Aminopropanal, formed during cerebral ischaemia, is a potent lysosomotropic neurotoxin. Biochem J 371:429-436. https://doi.org/10.1042/BJ20021520
- Li W, Yuan X, Nordgren G, Dalen H, Dubowchik GM, Firestone RA, Brunk UT (2000). Induction of cell death by the lysosomotropic detergent MSDH. FEBS Lett 470:35-39. https://doi.org/10.1016/S0014-5793(00)01286-2
- Manna SK, Zhang HJ, Yan T, Oberley LW, Aggarwal BB (1998). Overexpression of manganese superoxide dismutase suppresses tumor necrosis factor-induced apoptosis and activation of nuclear transcription factorkappaB and activated protein-1. J Biol Chem 273:13245-13254. https://doi.org/10.1074/jbc.273.21.13245
- Osawa Y, Nagaki M, Banno Y, Brenner DA, Nozawa Y, Moriwaki H, Nakashima S (2003). Expression of the NF-kappa B target gene X-ray-inducible immediate early response factor-1 short enhances TNF-alphainduced hepatocyte apoptosis by inhibiting Akt activation. J Immunol 170:4053-4060. https://doi.org/10.4049/jimmunol.170.8.4053
- Schilling D, Pittelkow MR, Kumar R (2001). IEX-1, an immediate early gene, increases the rate of apoptosis in keratinocytes. Oncogene 20:7992-7997. https://doi.org/10.1038/sj.onc.1204965
- Shen L, Guo J, Santos-Berrios C, Wu MX (2006). Distinct domains for anti- and pro-apoptotic activities of IEX-1. J Biol Chem 281:15304-15311. https://doi.org/10.1074/jbc.M600054200
- Stoka V, Turk B, Schendel SL, Kim TH, Cirman T, Snipas SJ, Ellerby LM, Bredesen D, Freeze H, Abrahamson M, Bromme D, Krajewski S, Reed JC, Yin XM, Turk V, Salvesen GS (2001). Lysosomal protease pathways to apoptosis. Cleavage of bid, not pro-caspases, is the most likely route. J Biol Chem 276:3149-3157. https://doi.org/10.1074/jbc.M008944200
- Tait DL, Obermiller PS, Hatmaker AR, Redlin-Frazier S, Holt JT (1999). Ovarian cancer BRCA1 gene therapy: Phase I and II trial differences in immune response and vector stability. Clin Cancer Res 5:1708-1714.
- Turk B, Stoka V, Rozman-Pungercar J, Cirman T, Droga- Mazovec G, Oresic K, Turk V (2002). Apoptotic pathways: involvement of lysosomal proteases. Biol Chem 383:1035-1044.
- Vancompernolle K, Van Herreweghe F, Pynaert G, Van de Craen M, De Vos K, Totty N, Sterling A, Fiers W, Vandenabeele P, Grooten J (1998). Atractyloside-induced release of cathepsin B, a protease with caspase-processing activity. FEBS Lett 438:150-158. https://doi.org/10.1016/S0014-5793(98)01275-7
- Yoon S, Ha HJ, Kim YH, Won M, Park M, Ko JJ, Lee K, Bae J (2009). IEX-1-induced cell death requires BIM and is modulated by MCL-1. Biochem Biophys Res Commun 382:400-404. https://doi.org/10.1016/j.bbrc.2009.03.037
- Yoon S, Na SY, Kim HM, Lee K, Bae J (2010) Mutural activities of IEX-1 and MCL-1 on the apoptosis of ovarian cancer cells. Develpoment and Reproduction 14:83-89.
- Zhang Y, Finegold MJ, Porteu F, Kanteti P, Wu MX (2003). Development of T-cell lymphomas in Emu-IEX-1 mice. Oncogene 22:6845-6851. https://doi.org/10.1038/sj.onc.1206707