참고문헌
- Kastelein JJ, van der Steeg WA, Holme I et al (2008) Lipids, apolipoproteins, and their ratios in relation to cardiovascular events with statin treatment. Circulation 117, 3002-3009 https://doi.org/10.1161/CIRCULATIONAHA.107.713438
- Sofer O, Fainaru M, Schafer Z and Goldman R (1992) Regulation of lipoprotein lipase secretion in murine macrophages during foam cell formation in vitro. Effect of triglyceride-rich lipoproteins. Arterioscler Thromb 12, 1458-1466 https://doi.org/10.1161/01.ATV.12.12.1458
- Aronis A, Aharoni-Simon M, Madar Z and Tirosh O (2009) Triacylglycerol-induced impairment in mitochondrial biogenesis and function in J774.2 and mouse peritoneal macrophage foam cells. Arch Biochem Biophys 492, 74-81 https://doi.org/10.1016/j.abb.2009.09.011
- Gotto AM, Jr. (1998) Triglyceride: the forgotten risk factor. Circulation 97, 1027-1028 https://doi.org/10.1161/01.CIR.97.11.1027
- Elmore S (2007) Apoptosis: a review of programmed cell death. Toxicol Pathol 35, 495-516 https://doi.org/10.1080/01926230701320337
- Bronner DN, O'Riordan MX and He Y (2013) Caspase-2 mediates a Brucella abortus RB51-induced hybrid cell death having features of apoptosis and pyroptosis. Front Cell Infect Microbiol 3, 83
- Albert ML (2004) Death-defying immunity: do apoptotic cells influence antigen processing and presentation? Nat Rev Immunol 4, 223-231 https://doi.org/10.1038/nri11308
- Brennan MA and Cookson BT (2000) Salmonella induces macrophage death by caspase-1-dependent necrosis. Mol Microbiol 38, 31-40 https://doi.org/10.1046/j.1365-2958.2000.02103.x
- Jesenberger V, Procyk KJ, Yuan J, Reipert S and Baccarini M (2000) Salmonella-induced caspase-2 activation in macrophages: a novel mechanism in pathogen-mediated apoptosis. J Exp Med 192, 1035-1046 https://doi.org/10.1084/jem.192.7.1035
- Thornberry NA, Rano TA, Peterson EP et al (1997) A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis. J Biol Chem 272, 17907-17911 https://doi.org/10.1074/jbc.272.29.17907
- Cohen GM (1997) Caspases: the executioners of apoptosis. Biochem J 326 (Pt 1), 1-16 https://doi.org/10.1042/bj3260001
- Tewari M, Quan LT, O'Rourke K et al (1995) Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmAinhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell 81, 801-809 https://doi.org/10.1016/0092-8674(95)90541-3
- Aflaki E, Radovic B, Chandak PG et al (2011) Triacylglycerol accumulation activates the mitochondrial apoptosis pathway in macrophages. J Biol Chem 286, 7418-7428 https://doi.org/10.1074/jbc.M110.175703
- Son SJ, Rhee KJ, Lim J, Kim TU, Kim TJ and Kim YS (2013) Triglyceride-induced macrophage cell death is triggered by caspase-1. Biol Pharm Bull 36, 108-113
- Zhang WH, Wang X, Narayanan M et al (2003) Fundamental role of the Rip2/caspase-1 pathway in hypoxia and ischemia-induced neuronal cell death. Proc Natl Acad Sci U S A 100, 16012-16017 https://doi.org/10.1073/pnas.2534856100
- Lamkanfi M, Kanneganti TD, Van Damme P et al (2008) Targeted peptidecentric proteomics reveals caspase-7 as a substrate of the caspase-1 inflammasomes. Mol Cell Proteomics 7, 2350-2363 https://doi.org/10.1074/mcp.M800132-MCP200
- Puccini J, Dorstyn L and Kumar S (2013) Caspase-2 as a tumour suppressor. Cell Death Differ 20, 1133-1139 https://doi.org/10.1038/cdd.2013.87
- Fava LL, Bock FJ, Geley S and Villunger A (2012) Caspase-2 at a glance. J Cell Sci 125, 5911-5915 https://doi.org/10.1242/jcs.115105
- Bouchier-Hayes L and Green DR (2012) Caspase-2: the orphan caspase. Cell Death Differ 19, 51-57 https://doi.org/10.1038/cdd.2011.157
- Aronis A, Madar Z and Tirosh O (2008) Lipotoxic effects of triacylglycerols in J774.2 macrophages. Nutrition 24, 167-176 https://doi.org/10.1016/j.nut.2007.10.017
-
Lim J, Kim YS, Kim SH et al (2013) Triglyceride enhances susceptibility to TNF-
${\alpha}$ -induced cell death in THP-1 cells. Genes & Genomics 36, 87-93 - Kolodgie FD, Narula J, Burke AP et al (2000) Localization of apoptotic macrophages at the site of plaque rupture in sudden coronary death. Am J Pathol 157, 1259-1268 https://doi.org/10.1016/S0002-9440(10)64641-X
- Plesnila N, Zinkel S, Le DA et al (2001) BID mediates neuronal cell death after oxygen/ glucose deprivation and focal cerebral ischemia. Proc Natl Acad Sci U S A 98, 15318-15323 https://doi.org/10.1073/pnas.261323298
- Yeretssian G, Labbe K and Saleh M (2008) Molecular regulation of inflammation and cell death. Cytokine 43, 380-390 https://doi.org/10.1016/j.cyto.2008.07.015
- Huang YT, Huang YH, Hour TC, Pan BS, Liu YC and Pan MH (2006) Apoptosis-inducing active components from Corbicula fluminea through activation of caspase-2 and production of reactive oxygen species in human leukemia HL-60 cells. Food Chem Toxicol 44, 1261-1272 https://doi.org/10.1016/j.fct.2006.02.001
- Stefanis L, Troy CM, Qi H, Shelanski ML and Greene LA (1998) Caspase-2 (Nedd-2) processing and death of trophic factor-deprived PC12 cells and sympathetic neurons occur independently of caspase-3 (CPP32)-like activity. J Neurosci 18, 9204-9215 https://doi.org/10.1523/JNEUROSCI.18-22-09204.1998
- Lim J, Kim SH, Kang YW et al (2014) Triglyceride up-regulates expression of ABCG1 in PMA-induced THP-1 macrophages through activation of JNK and p38 MAPK pathways. Biomed Sci Lett 20, 237-243 https://doi.org/10.15616/BSL.2014.20.4.237
- Joo D, Woo JS, Cho KH et al (2016) Biphasic activation of extracellular signal-regulated kinase (ERK) 1/2 in epidermal growth factor (EGF)-stimulated SW480 colorectal cancer cells. BMB Rep 49, 220-225 https://doi.org/10.5483/BMBRep.2016.49.4.004
- Imre G, Heering J, Takeda AN et al (2012) Caspase-2 is an initiator caspase responsible for pore-forming toxinmediated apoptosis. EMBO J 31, 2615-2628 https://doi.org/10.1038/emboj.2012.93
- Jo HS, Kim DS, Ahn EH et al (2016) Protective effects of Tat-NQO1 against oxidative stress-induced HT-22 cell damage, and ischemic injury in animals. BMB Rep 49, 617-622 https://doi.org/10.5483/BMBRep.2016.49.11.117