References
- Broker LE, Huisman C, Span SW, et al (2004). Cathepsin B mediates caspase-independent cell death induced by microtubule stabilizing agents in non-small cell lung cancer cells. Cancer Res, 64, 27-30. https://doi.org/10.1158/0008-5472.CAN-03-3060
- Chiang KC, Tsui KH, Chung LC, et al (2014). Cisplatin modulates B-cell translocation gene 2 to attenuate cell proliferation of prostate carcinoma cells in both p53-dependent and p53-independent pathways. Sci Rep, 4, 5511.
- Chipuk JE, Green DR (2008). How do Bcl-2 proteins induce mitochondrial outer membrane permeabilization? Trends Cell Biol, 18, 157-64. https://doi.org/10.1016/j.tcb.2008.01.007
- Darzynkiewicz Z, Halicka HD, Zhao H (2010). Analysis of cellular DNA content by flow and laser scanning cytometry. Adv Exp Med Biol, 676, 137-47. https://doi.org/10.1007/978-1-4419-6199-0_9
- Douarre C, Gomez D, Morjani H, et al (2005). Overexpression of Bcl-2 is associated with apoptotic resistance to the G-quadruplex ligand 12459 but is not sufficient to confer resistance to long-term senescence. Nucleic Acids Res, 33, 2192-203. https://doi.org/10.1093/nar/gki514
- Foghsgaard L, Wissing D, Mauch D, et al (2001). Cathepsin B acts as a dominant execution protease in tumor cell apoptosis induced by tumor necrosis factor. J Cell Biol, 153, 999-1010. https://doi.org/10.1083/jcb.153.5.999
- Gondi CS, Rao JS (2013). Cathepsin B as a cancer target. Expert Opin Ther Targets, 17, 281-91. https://doi.org/10.1517/14728222.2013.740461
- Green DR, Kroemer G (2009). Cytoplasmic functions of the tumour suppressor p53. Nature, 458, 1127-30. https://doi.org/10.1038/nature07986
- Guicciardi ME, Deussing J, Miyoshi H, et al (2000). Cathepsin B contributes to TNF-alpha-mediated hepatocyte apoptosis by promoting mitochondrial release of cytochrome c. J Clin Invest, 106, 1127-37. https://doi.org/10.1172/JCI9914
- Joy B, Sivadasan R, Abraham TE, et al (2010). Lysosomal destabilization and Cathepsin B contributes for cytochrome c release and caspase activation in embelin-induced apoptosis. Mol Carcinog, 49, 324-36.
- Kagedal K, Johansson AC, Johansson U, et al (2005). Lysosomal membrane permeabilization during apoptosis--involvement of Bax? Int J Exp Pathol, 86, 309-21. https://doi.org/10.1111/j.0959-9673.2005.00442.x
- Laohathai K, Bhamarapravati N (1985). Culturing of human hepatocellular carcinoma. A simple and reproducible method. Am J Pathol, 118, 203-8.
- Leist M, Jaattela M (2001). Four deaths and a funeral: from caspases to alternative mechanisms. Nat Rev Mol Cell Biol, 2, 589-98.
- Lin CH, Lu WC, Wang CW, et al (2013). Capsaicin induces cell cycle arrest and apoptosis in human KB cancer cells. BMC Complement Altern Med, 13, 46. https://doi.org/10.1186/1472-6882-13-46
- Malla R, Gopinath S, Alapati K, et al (2010). Downregulation of uPAR and Cathepsin B induces apoptosis via regulation of Bcl-2 and Bax and inhibition of the PI3K/Akt pathway in gliomas. PLoS One, 5, 13731. https://doi.org/10.1371/journal.pone.0013731
- Manochantr S, Puthong S, Gamnarai P, et al (2011). Hep 88mAB induced ultrastructural alteration through apoptosis like program cell death in hepatocellular carcinoma. J Med Assoc Thai, 94, 109-16.
- Marchenko ND, Zaika A, Moll UM (2000). Death signal-induced localization of p53 protein to mitochondria. A potential role in apoptotic signaling. J Biol Chem, 275, 16202-12. https://doi.org/10.1074/jbc.275.21.16202
- Mitupatum T, Aree K, Kittisenachai S, et al (2015). Hep88mAb-Mediated Paraptosis-Like Apoptosis in HepG2 Cells via Downstream Upregulation and Activation of Caspase-3, Caspase-8 and Caspase-9. Asian Pac J Cancer Prev, 16, 1771-9. https://doi.org/10.7314/APJCP.2015.16.5.1771
- Nylandsted J, Gyrd-Hansen M, Danielewicz A, et al (2004). Heat shock protein 70 promotes cell survival by inhibiting lysosomal membrane permeabilization. J Exp Med, 200, 425-35. https://doi.org/10.1084/jem.20040531
- Puthong S, Rojpibulstit P, Buakeaw A ( 2009). Cytotoxic effect of Hep88 mAb: a novel monoclonal antibody against hepatocellular carcinoma. Thammasat Int J Sc Tech, 14, 95-104.
- Rojpibulstit P, Kittisenachai S, Puthong S, et al (2014). Hep88 mAb-initiated paraptosis-like PCD pathway in hepatocellular carcinoma cell line through the binding of mortalin (HSPA9) and alpha-enolase. Cancer Cell International, 14.
- Sartorius UA, Krammer PH (2002). Upregulation of Bcl-2 is involved in the mediation of chemotherapy resistance in human small cell lung cancer cell lines. Int J Cancer, 97, 584-92. https://doi.org/10.1002/ijc.10096
- Sperandio S, de Belle I, Bredesen DE (2000). An alternative, nonapoptotic form of programmed cell death. Proc Natl Acad Sci U S A, 97, 14376-81. https://doi.org/10.1073/pnas.97.26.14376
- Sperandio S, Poksay K, de Belle I, et al (2004). Paraptosis:mediation by MAP kinases and inhibition by AIP-1/Alix. Cell Death Differ, 11, 1066-75. https://doi.org/10.1038/sj.cdd.4401465
- Stankiewicz AR, Lachapelle G, Foo CP, et al (2005). Hsp70 inhibits heat-induced apoptosis upstream of mitochondria by preventing Bax translocation. J Biol Chem, 280, 38729-39. https://doi.org/10.1074/jbc.M509497200
- Starenki D, Hong SK, Lloyd RV, et al (2014). Mortalin (GRP75/HSPA9) upregulation promotes survival and proliferation of medullary thyroid carcinoma cells. Oncogene.
- Taghiyev A, Sun D, Gao ZM, et al (2012). Embelin-induced apoptosis of HepG2 human hepatocellular carcinoma cells and blockade of HepG2 cells in the G2/M phase via the mitochondrial pathway. Exp Ther Med, 4, 649-54. https://doi.org/10.3892/etm.2012.637
- Taurin S, Seyrantepe V, Orlov SN, et al (2002). Proteome analysis and functional expression identify mortalin as an antiapoptotic gene induced by elevation of [Na+]i/[K+]i ratio in cultured vascular smooth muscle cells. Circ Res, 91, 915-22. https://doi.org/10.1161/01.RES.0000043020.45534.3E
- Wadhwa R, Takano S, Kaur K, et al (2006). Upregulation of mortalin/mthsp70/Grp75 contributes to human carcinogenesis. Int J Cancer, 118, 2973-80. https://doi.org/10.1002/ijc.21773
- Walker C, Bottger S, Low B (2006). Mortalin-based cytoplasmic sequestration of p53 in a nonmammalian cancer model. Am J Pathol, 168, 1526-30. https://doi.org/10.2353/ajpath.2006.050603
- Walter RB, Raden BW, Kamikura DM, et al (2005). Influence of CD33 expression levels and ITIM-dependent internalization on gemtuzumab ozogamicin-induced cytotoxicity. Blood, 105, 1295-302.
- Wang H, Zhang J, Sit WH, et al (2014a). Cordyceps cicadae induces G2/M cell cycle arrest in MHCC97H human hepatocellular carcinoma cells: a proteomic study. Chin Med, 9, 15. https://doi.org/10.1186/1749-8546-9-15
- Wang Y, Ji P, Liu J, et al (2009). Centrosome-associated regulators of the G(2)/M checkpoint as targets for cancer therapy. Mol Cancer, 8, 8. https://doi.org/10.1186/1476-4598-8-8
- Wang YX, Cai H, Jiang G, et al (2014b). Silibinin inhibits proliferation, induces apoptosis and causes cell cycle arrest in human gastric cancer MGC803 cells via STAT3 pathway inhibition. Asian Pac J Cancer Prev, 15, 6791-8. https://doi.org/10.7314/APJCP.2014.15.16.6791
- Whelan JA, Russell NB, Whelan MA (2003). A method for the absolute quantification of cDNA using real-time PCR. Journal of Immunological Methods, 278, 261-9. https://doi.org/10.1016/S0022-1759(03)00223-0
- Wyllie AH, Golstein P (2001). More than one way to go. Proc Natl Acad Sci U S A, 98, 11-3. https://doi.org/10.1073/pnas.98.1.11
Cited by
- Long non-coding RNA Gas5 regulates proliferation and apoptosis in HCS-2/8 cells and growth plate chondrocytes by controlling FGF1 expression via miR-21 regulation vol.25, pp.1, 2018, https://doi.org/10.1186/s12929-018-0424-6
- Furosine Induced Apoptosis by the Regulation of STAT1/STAT2 and UBA7/UBE2L6 Genes in HepG2 Cells vol.19, pp.6, 2018, https://doi.org/10.3390/ijms19061629
- BYD Ameliorates Oxidative Stress-Induced Myocardial Apoptosis in Heart Failure Post-Acute Myocardial Infarction via the P38 MAPK-CRYAB Signaling Pathway vol.9, pp.1664-042X, 2018, https://doi.org/10.3389/fphys.2018.00505
- Insights into stress responses in mandarins triggered by Bacillus subtilis cyclic lipopeptides and exogenous plant hormones upon Penicillium digitatum infection pp.1432-203X, 2019, https://doi.org/10.1007/s00299-019-02386-1