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BioMed Research International
Volume 2014 (2014), Article ID 690103, 10 pages
http://dx.doi.org/10.1155/2014/690103
Review Article

Current and Emerging Biomarkers of Cell Death in Human Disease

1College of Bioinformatics Science and Technology, Harbin Medical University, Harbin 150081, China
2College of Bioengineering, Henan University of Technology, Zhengzhou 450001, China

Received 28 March 2014; Accepted 17 April 2014; Published 18 May 2014

Academic Editor: Wencai Ma

Copyright © 2014 Kongning Li et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. Y. Fuchs and H. Steller, “Programmed cell death in animal development and disease,” Cell, vol. 147, no. 4, pp. 742–758, 2011. View at Publisher · View at Google Scholar · View at Scopus
  2. H. Engelberg-Kulka, S. Amitai, I. Kolodkin-Gal, and R. Hazan, “Bacterial programmed cell death and multicellular behavior in bacteria,” PLoS Genetics, vol. 2, no. 10, p. e135, 2006. View at Publisher · View at Google Scholar · View at Scopus
  3. M. O. Hengartner, “The biochemistry of apoptosis,” Nature, vol. 407, no. 6805, pp. 770–776, 2000. View at Publisher · View at Google Scholar · View at Scopus
  4. G. Kroemer, L. Galluzzi, P. Vandenabeele et al., “Classification of cell death: recommendations of the Nomenclature Committee on Cell Death 2009,” Cell Death and Differentiation, vol. 16, no. 1, pp. 3–11, 2009. View at Publisher · View at Google Scholar · View at Scopus
  5. L. Galluzzi, I. Vitale, J. M. Abrams et al., “Molecular definitions of cell death subroutines: recommendations of the Nomenclature Committee on Cell Death 2012,” Cell Death and Differentiation, vol. 19, no. 1, pp. 107–120, 2012. View at Publisher · View at Google Scholar · View at Scopus
  6. V. Zuzarte-Luís and J. M. Hurlé, “Programmed cell death in the developing limb,” International Journal of Developmental Biology, vol. 46, no. 7, pp. 871–876, 2002. View at Google Scholar · View at Scopus
  7. M. Su, Y. Mei, and S. Sinha, “Role of the crosstalk between autophagy and apoptosis in Cancer,” Journal of Oncology, vol. 2013, Article ID 102735, 14 pages, 2013. View at Publisher · View at Google Scholar
  8. L. E. Mũoz, K. Lauber, M. Schiller, A. A. Manfredi, and M. Herrmann, “The role of defective clearance of apoptotic cells in systemic autoimmunity,” Nature Reviews Rheumatology, vol. 6, no. 5, pp. 280–289, 2010. View at Publisher · View at Google Scholar · View at Scopus
  9. S. W. Lowe and A. W. Lin, “Apoptosis in cancer,” Carcinogenesis, vol. 21, no. 3, pp. 485–495, 2000. View at Google Scholar · View at Scopus
  10. J. A. Marchal, G. J. Lopez, M. Peran et al., “The impact of PKR activation: from neurodegeneration to cancer,” The FASEB Journal, 2014. View at Publisher · View at Google Scholar
  11. P. Bonaldo and M. Sandri, “Cellular and molecular mechanisms of muscle atrophy,” Disease Models & Mechanisms, vol. 6, pp. 25–39, 2013. View at Google Scholar
  12. S. Elmore, “Apoptosis: a review of programmed cell death,” Toxicologic Pathology, vol. 35, no. 4, pp. 495–516, 2007. View at Publisher · View at Google Scholar · View at Scopus
  13. S. Gupta, A. Agrawal, S. Agrawal, H. Su, and S. Gollapudi, “A paradox of immunodeficiency and inflammation in human aging: lessons learned from apoptosis,” Immunity and Ageing, vol. 3, article 5, 2006. View at Publisher · View at Google Scholar · View at Scopus
  14. A. A. Neves and K. M. Brindle, “Imaging cell death,” Journal of Nuclear Medicine, vol. 55, pp. 1–4, 2014. View at Google Scholar
  15. K. Nishida, O. Yamaguchi, and K. Otsu, “Crosstalk between autophagy and apoptosis in heart disease,” Circulation Research, vol. 103, no. 4, pp. 343–351, 2008. View at Publisher · View at Google Scholar · View at Scopus
  16. G. Marino, M. Niso-Santano, E. H. Baehrecke, and G. Kroemer, “Self-consumption: the interplay of autophagy and apoptosis,” Nature Reviews Molecular Cell Biology, vol. 15, pp. 81–94, 2014. View at Google Scholar
  17. S. A. Susin, H. K. Lorenzo, N. Zamzami et al., “Molecular characterization of mitochodrial apoptosis-inducing factor,” Nature, vol. 397, no. 6718, pp. 441–446, 1999. View at Publisher · View at Google Scholar · View at Scopus
  18. F. H. Igney and P. H. Krammer, “Death and anti-death: tumour resistance to apoptosis,” Nature Reviews Cancer, vol. 2, no. 4, pp. 277–288, 2002. View at Google Scholar · View at Scopus
  19. M. V. Jain, A. M. Paczulla, T. Klonisch et al., “Interconnections between apoptotic, autophagic and necrotic pathways: implications for cancer therapy development,” Journal of Cellular and Molecular Medicine, vol. 17, pp. 12–29, 2013. View at Google Scholar
  20. J.-O. Pyo, J. Nah, and Y.-K. Jung, “Molecules and their functions in autophagy,” Experimental and Molecular Medicine, vol. 44, no. 2, pp. 73–80, 2012. View at Publisher · View at Google Scholar · View at Scopus
  21. A. M. Choi, S. W. Ryter, and B. Levine, “Autophagy in human health and disease,” The New England Journal of Medicine, vol. 368, pp. 1845–1846, 2013. View at Google Scholar
  22. Y. Wang and Z. H. Qin, “Coordination of autophagy with other cellular activities,” Acta Pharmacologica Sinica, vol. 34, pp. 585–594, 2013. View at Google Scholar
  23. K. S. Choi, “Autophagy and cancer,” Experimental and Molecular Medicine, vol. 44, no. 2, pp. 109–120, 2012. View at Publisher · View at Google Scholar · View at Scopus
  24. S. Miller, B. Tavshanjian, A. Oleksy et al., “Shaping development of autophagy inhibitors with the structure of the lipid kinase Vps34,” Science, vol. 327, no. 5973, pp. 1638–1642, 2010. View at Publisher · View at Google Scholar · View at Scopus
  25. D. Denton, S. Nicolson, and S. Kumar, “Cell death by autophagy: facts and apparent artefacts,” Cell Death and Differentiation, vol. 19, no. 1, pp. 87–95, 2012. View at Publisher · View at Google Scholar · View at Scopus
  26. T. Vanden Berghe, A. Linkermann, S. Jouan-Lanhouet, H. Walczak, and P. Vandenabeele, “Regulated necrosis: the expanding network of non-apoptotic cell death pathways,” Nature Reviews Molecular Cell Biology, vol. 15, pp. 135–147, 2014. View at Google Scholar
  27. S. J. Kim and J. Li, “Caspase blockade induces RIP3-mediated programmed necrosis in Toll-like receptor-activated microglia,” Cell Death & Disease, vol. 4, article e716, 2013. View at Google Scholar
  28. Q. Remijsen, T. W. Kuijpers, E. Wirawan, S. Lippens, P. Vandenabeele, and T. Vanden Berghe, “Dying for a cause: NETosis, mechanisms behind an antimicrobial cell death modality,” Cell Death and Differentiation, vol. 18, no. 4, pp. 581–588, 2011. View at Publisher · View at Google Scholar · View at Scopus
  29. L. Galluzzi, O. Kepp, S. Krautwald, G. Kroemer, and A. Linkermann, “Molecular mechanisms of regulated necrosis,” Seminars in Cell & Developmental Biology, 2014. View at Publisher · View at Google Scholar
  30. I. Vitale, L. Galluzzi, M. Castedo, and G. Kroemer, “Mitotic catastrophe: a mechanism for avoiding genomic instability,” Nature Reviews. Molecular Cell Biology, vol. 12, no. 6, pp. 385–392, 2011. View at Publisher · View at Google Scholar · View at Scopus
  31. G. Imreh, H. V. Norberg, S. Imreh, and B. Zhivotovsky, “Chromosomal breaks during mitotic catastrophe trigger γH2AX-ATM-p53-mediated apoptosis,” Journal of Cell Science, vol. 124, no. 17, pp. 2951–2963, 2011. View at Publisher · View at Google Scholar · View at Scopus
  32. H. Vakifahmetoglu, M. Olsson, C. Tamm, N. Heidari, S. Orrenius, and B. Zhivotovsky, “DNA damage induces two distinct modes of cell death in ovarian carcinomas,” Cell Death and Differentiation, vol. 15, no. 3, pp. 555–566, 2008. View at Publisher · View at Google Scholar · View at Scopus
  33. M. Castedo, J.-L. Perfettini, T. Roumier, and G. Kroemer, “Cyclin-dependent kinase-1: linking apoptosis to cell cycle and mitotic catastrophe,” Cell Death and Differentiation, vol. 9, no. 12, pp. 1287–1293, 2002. View at Publisher · View at Google Scholar · View at Scopus
  34. M. Kimura, T. Yoshioka, M. Saio, Y. Banno, H. Nagaoka, and Y. Okano, “Mitotic catastrophe and cell death induced by depletion of centrosomal proteins,” Cell Death & Disease, vol. 4, article e603, 2013. View at Google Scholar
  35. J. Portugal, S. Mansilla, and M. Bataller, “Mechanisms of drug-induced mitotic catastrophe in cancer cells,” Current Pharmaceutical Design, vol. 16, no. 1, pp. 69–78, 2010. View at Publisher · View at Google Scholar · View at Scopus
  36. A. Eguchi, A. Wree, and A. E. Feldstein, “Biomarkers of liver cell death,” Journal of Hepatology, vol. 60, no. 5, pp. 1063–1074, 2014. View at Publisher · View at Google Scholar
  37. F. Crea, P. L. Clermont, A. Parolia, Y. Wang, and C. D. Helgason, “The non-coding transcriptome as a dynamic regulator of cancer metastasis,” Cancer and Metastasis Reviews, 2013. View at Publisher · View at Google Scholar
  38. X. X. Guo, Y. Li, C. Sun et al., “p53-dependent Fas expression is critical for Ginsenoside Rh2 triggered caspase-8 activation in HeLa cells,” Protein Cell, vol. 5, no. 3, pp. 224–234, 2014. View at Google Scholar
  39. S. Seirafian, V. Prod'homme, D. Sugrue et al., “Human cytomegalovirus suppresses fas expression and function,” Journal of General Virology, vol. 95, pp. 933–939, 2014. View at Google Scholar
  40. M. E. Guicciardi and G. J. Gores, “Life and death by death receptors,” The FASEB Journal, vol. 23, no. 6, pp. 1625–1637, 2009. View at Publisher · View at Google Scholar · View at Scopus
  41. K. Reimers, C. Radtke, C. Y. Choi et al., “Expression of TNF-related apoptosis-inducing ligand (TRAIL) in keratinocytes mediates apoptotic cell death in allogenic T cells,” Annals of Surgical Innovation and Research, vol. 3, article 13, 2009. View at Publisher · View at Google Scholar · View at Scopus
  42. S. Maher, D. Toomey, C. Condron, and D. Bouchier-Hayes, “Activation-induced cell death: the controversial role of Fas and Fas ligand in immune privilege and tumour counterattack,” Immunology and Cell Biology, vol. 80, no. 2, pp. 131–137, 2002. View at Publisher · View at Google Scholar · View at Scopus
  43. Y. Q. Zhang, C. X. Xiao, B. Y. Lin et al., “Silencing of Pokemon enhances caspase-dependent apoptosis via fas- and mitochondria-mediated pathways in hepatocellular carcinoma cells,” PLoS ONE, vol. 8, Article ID e68981, 2013. View at Google Scholar
  44. M. P. Messer, P. Kellermann, S. J. Weber et al., “Silencing of fas, fas-associated via death domain, or caspase 3 differentially affects lung inflammation, apoptosis, and development of trauma-induced septic acute lung injury,” Shock, vol. 39, pp. 19–27, 2013. View at Google Scholar
  45. H.-Q. Wang, X.-D. Yu, Z.-H. Liu et al., “Deregulated miR-155 promotes Fas-mediated apoptosis in human intervertebral disc degeneration by targeting FADD and caspase-3,” Journal of Pathology, vol. 225, no. 2, pp. 232–242, 2011. View at Publisher · View at Google Scholar · View at Scopus
  46. Z. G. Mao, C. C. Jiang, F. Yang, R. F. T. Rick F. Thorne, P. Hersey, and X. D. Zhang, “TRAIL-induced apoptosis of human melanoma cells involves activation of caspase-4,” Apoptosis, vol. 15, no. 10, pp. 1211–1222, 2010. View at Publisher · View at Google Scholar · View at Scopus
  47. H. E. Saqr, O. M. Omran, J. L. Oblinger, and A. J. Yates, “TRAIL-induced apoptosis in U-1242 MG glioma cells,” Journal of Neuropathology and Experimental Neurology, vol. 65, no. 2, pp. 152–161, 2006. View at Publisher · View at Google Scholar · View at Scopus
  48. C. A. Hetz, M. Hunn, P. Rojas, V. Torres, L. Leyton, and A. F. G. Quest, “Caspase-dependent initiation of apoptosis and necrosis by the Fas receptor in lymphoid cells: onset of necrosis is associated with delayed ceramide increase,” Journal of Cell Science, vol. 115, no. 23, pp. 4671–4863, 2002. View at Publisher · View at Google Scholar · View at Scopus
  49. T. K. Owonikoko, M. S. Hossain, C. Bhimani et al., “Soluble FAS ligand as a biomarker of disease recurrence in differentiated thyroid cancer,” Cancer, vol. 119, pp. 1503–1511, 2013. View at Google Scholar
  50. C. Costagliola, V. Romano, M. De Tollis et al., “TNF-alpha levels in tears: a novel biomarker to assess the degree of diabetic retinopathy,” Mediators of Inflammation, vol. 2013, Article ID 629529, 6 pages, 2013. View at Publisher · View at Google Scholar
  51. D. R. McIlwain, T. Berger, and T. W. Mak, “Caspase functions in cell death and disease,” Cold Spring Harbor Perspectives in Biology, vol. 5, Article ID a008656, 2013. View at Google Scholar
  52. C. Pop and G. S. Salvesen, “Human caspases: activation, specificity, and regulation,” Journal of Biological Chemistry, vol. 284, no. 33, pp. 21777–21781, 2009. View at Publisher · View at Google Scholar · View at Scopus
  53. S. Ghavami, M. Hashemi, S. R. Ande et al., “Apoptosis and cancer: mutations within caspase genes,” Journal of Medical Genetics, vol. 46, no. 8, pp. 497–510, 2009. View at Publisher · View at Google Scholar · View at Scopus
  54. K. Sakamaki and Y. Satou, “Caspases: evolutionary aspects of their functions in vertebrates,” Journal of Fish Biology, vol. 74, no. 4, pp. 727–753, 2009. View at Publisher · View at Google Scholar · View at Scopus
  55. A. Alcivar, S. Hu, J. Tang, and X. Yang, “DEDD and DEDD2 associate with caspase-8/10 and signal cell death,” Oncogene, vol. 22, no. 2, pp. 291–297, 2003. View at Publisher · View at Google Scholar · View at Scopus
  56. J. Huai, L. Jöckel, K. Schrader, and C. Borner, “Role of caspases and non-caspase proteases in cell death,” F1000 Biology Reports, vol. 2, no. 1, article 48, 2010. View at Publisher · View at Google Scholar · View at Scopus
  57. S. P. Cullen and S. J. Martin, “Caspase activation pathways: some recent progress,” Cell Death and Differentiation, vol. 16, no. 7, pp. 935–938, 2009. View at Publisher · View at Google Scholar · View at Scopus
  58. C. Adrain, B. M. Murphy, and S. J. Martin, “Molecular ordering of the caspase activation cascade initiated by the cytotoxic T lymphocyte/natural killer (CTL/NK) protease granzyme B,” Journal of Biological Chemistry, vol. 280, no. 6, pp. 4663–4673, 2005. View at Publisher · View at Google Scholar · View at Scopus
  59. I. H. Engels, G. Totzke, U. Fischer, K. Schulze-Osthoff, and R. U. Jänicke, “Caspase-10 sensitizes breast carcinoma cells to TRAIL-induced but not tumor necrosis factor-induced apoptosis in a caspase-3-dependent manner,” Molecular and Cellular Biology, vol. 25, no. 7, pp. 2808–2818, 2005. View at Publisher · View at Google Scholar · View at Scopus
  60. E. R. McDonald III and W. S. El-Deiry, “Suppression of caspase-8- and -10-associated RING proteins results in sensitization to death ligands and inhibition of tumor cell growth,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 16, pp. 6170–6175, 2004. View at Publisher · View at Google Scholar · View at Scopus
  61. V. S. Marsden, L. O'Connor, L. A. O'Reilly et al., “Apoptosis initiated by Bcl-2-regulated caspase activation independently of the cytochrome c/Apaf-1/caspase-9 apoptosome,” Nature, vol. 419, no. 6907, pp. 634–637, 2002. View at Publisher · View at Google Scholar · View at Scopus
  62. K. L. Simpson, C. Cawthorne, C. Zhou et al., “A caspase-3 “death-switch” in colorectal cancer cells for induced and synchronous tumor apoptosis in vitro and in vivo facilitates the development of minimally invasive cell death biomarkers,” Cell Death & Disease, vol. 4, article e613, 2013. View at Google Scholar
  63. K. P. Singh, A. S. Jaffe, and B. T. Liang, “The clinical impact of circulating caspase-3 p17 level: a potential new biomarker for myocardial injury and cardiovascular disease,” Future Cardiology, vol. 7, no. 4, pp. 443–445, 2011. View at Publisher · View at Google Scholar · View at Scopus
  64. A. W. Abu-Qare and M. B. Abou-Donia, “Biomarkers of apoptosis: release of cytochrome c, activation of caspase-3, induction of 8-hydroxy-2′-deoxyguanosine, increased 3-nitrotyrosine, and alteration of p53 gene,” Journal of Toxicology and Environmental Health B: Critical Reviews, vol. 4, no. 3, pp. 313–332, 2001. View at Google Scholar · View at Scopus
  65. R. G. Oshima, “Apoptosis and keratin intermediate filaments,” Cell Death and Differentiation, vol. 9, no. 5, pp. 486–492, 2002. View at Publisher · View at Google Scholar · View at Scopus
  66. K. John, S. Wielgosz, K. Schulze-Osthoff, H. Bantel, and R. Hass, “Increased plasma levels of CK-18 as potential cell death biomarker in patients with HELLP syndrome,” Cell Death & Disease, vol. 4, article e886, 2013. View at Google Scholar
  67. S. Linder, A. M. Havelka, T. Ueno, and M. C. Shoshan, “Determining tumor apoptosis and necrosis in patient serum using cytokeratin 18 as a biomarker,” Cancer Letters, vol. 214, no. 1, pp. 1–9, 2004. View at Publisher · View at Google Scholar · View at Scopus
  68. M. B. Fisher, X.-Q. Zhang, D. J. McConkey, and W. F. Benedict, “Measuring soluble forms of extracellular cytokeratin 18 identifies both apoptotic and necrotic mechanisms of cell death produced by adenoviral-mediated interferon α: possible use as a surrogate marker,” Cancer Gene Therapy, vol. 16, no. 7, pp. 567–572, 2009. View at Publisher · View at Google Scholar · View at Scopus
  69. M. B. Vos, S. Barve, S. Joshi-Barve, J. D. Carew, P. F. Whitington, and C. J. McClain, “Cytokeratin 18, a marker of cell death, is increased in children with suspected nonalcoholic fatty liver disease,” Journal of Pediatric Gastroenterology and Nutrition, vol. 47, no. 4, pp. 481–485, 2008. View at Google Scholar · View at Scopus
  70. D. W. Amory, J. L. Steffenson, and R. P. Forsyth, “Systemic and regional blood flow changes during halothane anesthesia in the Rhesus monkey,” Anesthesiology, vol. 35, no. 1, pp. 81–90, 1971. View at Google Scholar · View at Scopus
  71. A. E. Feldstein, N. Alkhouri, R. de Vito, A. Alisi, R. Lopez, and V. Nobili, “Serum cytokeratin-18 fragment levels are useful biomarkers for nonalcoholic steatohepatitis in children,” The American Journal of Gastroenterology, vol. 108, pp. 1526–1531, 2013. View at Google Scholar
  72. Y. Yilmaz, “Systematic review: caspase-cleaved fragments of cytokeratin 18—the promises and challenges of a biomarker for chronic liver disease,” Alimentary Pharmacology and Therapeutics, vol. 30, no. 11-12, pp. 1103–1109, 2009. View at Publisher · View at Google Scholar · View at Scopus
  73. H. X. Yan, H. P. Wu, H. L. Zhang et al., “DNA damage-induced sustained p53 activation contributes to inflammation-associated hepatocarcinogenesis in rats,” Oncogene, vol. 32, pp. 4565–4571, 2013. View at Google Scholar
  74. W. P. Roos and B. Kaina, “DNA damage-induced cell death by apoptosis,” Trends in Molecular Medicine, vol. 12, no. 9, pp. 440–450, 2006. View at Publisher · View at Google Scholar · View at Scopus
  75. T. Iwakuma and G. Lozano, “MDM2, an Introduction,” Molecular Cancer Research, vol. 1, no. 14, pp. 993–1000, 2003. View at Google Scholar · View at Scopus
  76. Q. Yang, L. Liao, X. Deng et al., “BMK1 is involved in the regulation of p53 through disrupting the PML-MDM2 interaction,” Oncogene, vol. 32, pp. 3156–3164, 2013. View at Google Scholar
  77. S. Kurki, L. Latonen, and M. Laiho, “Cellular stress and DNA damage invoke temporally distinct Mdm2, p53 and PML complexes and damage-specific nuclear relocalization,” Journal of Cell Science, vol. 116, no. 19, pp. 3917–3925, 2003. View at Publisher · View at Google Scholar · View at Scopus
  78. J. Yu, Z. Wang, K. W. Kinzler, B. Vogelstein, and L. Zhang, “PUMA mediates the apoptotic response to p53 in colorectal cancer cells,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 4, pp. 1931–1936, 2003. View at Publisher · View at Google Scholar · View at Scopus
  79. Y. Shen and E. White, “p53-dependent apoptosis pathways,” Advances in Cancer Research, vol. 82, pp. 55–84, 2001. View at Publisher · View at Google Scholar · View at Scopus
  80. G. Barone, D. A. Tweddle, J. M. Shohet et al., “MDM2-p53 interaction in paediatric solid tumours: preclinical rationale, biomarkers and resistance,” Current Drug Targets, vol. 15, pp. 114–123, 2014. View at Google Scholar
  81. C. Saddler, P. Ouillette, L. Kujawski et al., “Comprehensive biomarker and genomic analysis identifies p53 status as the major determinant of response to MDM2 inhibitors in chronic lymphocytic leukemia,” Blood, vol. 111, no. 3, pp. 1584–1593, 2008. View at Publisher · View at Google Scholar · View at Scopus
  82. V. W. Patil, M. B. Tayade, S. A. Pingale et al., “The p53 breast cancer tissue biomarker in Indian women,” Breast Cancer, vol. 3, pp. 71–78, 2011. View at Google Scholar
  83. L. Li, M. Fukumoto, and D. Liu, “Prognostic significance of p53 immunoexpression in the survival of oral squamous cell carcinoma patients treated with surgery and neoadjuvant chemotherapy,” Oncology Letters, vol. 6, pp. 1611–1615, 2013. View at Google Scholar
  84. K. Chen and N. Rajewsky, “The evolution of gene regulation by transcription factors and microRNAs,” Nature Reviews Genetics, vol. 8, no. 2, pp. 93–103, 2007. View at Publisher · View at Google Scholar · View at Scopus
  85. Y. Li, L. Zhuang, Y. Wang et al., “Connect the dots: a systems level approach for analyzing the miRNA-mediated cell death network,” Autophagy, vol. 9, pp. 436–439, 2013. View at Google Scholar
  86. B. T. Kren, P. Y.-P. Wong, A. Sarver, X. Zhang, Y. Zeng, and C. J. Steer, “microRNAs identified in highly purified liver-derived mitochondria may play a role in apoptosis,” RNA Biology, vol. 6, no. 1, pp. 65–72, 2009. View at Google Scholar · View at Scopus
  87. J. Xu, Y. Wang, X. Tan, and H. Jing, “MicroRNAs in autophagy and their emerging roles in crosstalk with apoptosis,” Autophagy, vol. 8, pp. 873–882, 2012. View at Google Scholar
  88. G. Deng and G. Sui, “Noncoding RNA in oncogenesis: a new era of identifying key players,” International Journal of Molecular Sciences, vol. 14, pp. 18319–18349, 2013. View at Google Scholar
  89. J. Krishnan and R. K. Mishra, “Emerging trends of long non-coding RNAs in gene activation,” The FEBS Journal, vol. 281, pp. 34–45, 2014. View at Google Scholar
  90. Y. Wang, L. Chen, B. Chen et al., “Mammalian ncRNA-disease repository: a global view of ncRNA-mediated disease network,” Cell Death & Disease, vol. 4, article e765, 2013. View at Google Scholar
  91. Y. F. Li, Y. Jing, J. Hao et al., “MicroRNA-21 in the pathogenesis of acute kidney injury,” Protein Cell, vol. 4, pp. 813–819, 2013. View at Google Scholar
  92. M. Luo, D. Shen, X. Zhou, X. Chen, and W. Wang, “MicroRNA-497 is a potential prognostic marker in human cervical cancer and functions as a tumor suppressor by targeting the insulin-like growth factor 1 receptor,” Surgery, vol. 153, pp. 836–847, 2013. View at Google Scholar
  93. Y. Chen, G. Ke, D. Han, S. Liang, G. Yang, and X. Wu, “MicroRNA-181a enhances the chemoresistance of human cervical squamous cell carcinoma to cisplatin by targeting PRKCD,” Experimental Cell Research, vol. 320, pp. 12–20, 2014. View at Google Scholar
  94. Y. Zhao, Q. Guo, J. Chen, J. Hu, S. Wang, and Y. Sun, “Role of long non-coding RNA HULC in cell proliferation, apoptosis and tumor metastasis of gastric cancer: a clinical and in vitro investigation,” Oncology Reports, vol. 31, pp. 358–364, 2014. View at Google Scholar
  95. D. G. Weber, G. Johnen, S. Casjens et al., “Evaluation of long noncoding RNA MALAT1 as a candidate blood-based biomarker for the diagnosis of non-small cell lung cancer,” BMC Research Notes, vol. 6, article 518, 2013. View at Google Scholar
  96. A. G. Porter and R. U. Jänicke, “Emerging roles of caspase-3 in apoptosis,” Cell Death and Differentiation, vol. 6, no. 2, pp. 99–104, 1999. View at Google Scholar · View at Scopus
  97. E. C. Zeestraten, A. Benard, M. S. Reimers et al., “The prognostic value of the apoptosis pathway in colorectal cancer: a review of the literature on biomarkers identified by immunohistochemistry,” Biomark Cancer, vol. 5, pp. 13–129, 2013. View at Google Scholar
  98. J. B. Chakraborty, F. Oakley, and M. J. Walsh, “Mechanisms and biomarkers of apoptosis in liver disease and fibrosis,” International Journal of Hepatology, vol. 2012, Article ID 648915, 10 pages, 2012. View at Publisher · View at Google Scholar
  99. N.-O. Ku, D. M. Toivola, P. Strnad, and M. B. Omary, “Cytoskeletal keratin glycosylation protects epithelial tissue from injury,” Nature Cell Biology, vol. 12, no. 9, pp. 876–885, 2010. View at Publisher · View at Google Scholar · View at Scopus
  100. B. Kronenberger, M. Von Wagner, E. Herrmann et al., “Apoptotic cytokeratin 18 neoepitopes in serum of patients with chronic hepatitis C,” Journal of Viral Hepatitis, vol. 12, no. 3, pp. 307–314, 2005. View at Publisher · View at Google Scholar · View at Scopus
  101. D. Montes-Berrueta, L. Ramirez, S. Salmen, and L. Berrueta, “Fas and FasL expression in leukocytes from chronic granulomatous disease patients,” Investigación Clínica, vol. 53, pp. 157–167, 2012. View at Google Scholar
  102. A. E. Weant, R. D. Michalek, I. U. Khan, B. C. Holbrook, M. C. Willingham, and J. M. Grayson, “Apoptosis regulators Bim and Fas function concurrently to control autoimmunity and CD8+ T cell contraction,” Immunity, vol. 28, no. 2, pp. 218–230, 2008. View at Publisher · View at Google Scholar · View at Scopus
  103. S. M. El-Karaksy, N. M. Kholoussi, R. M. Shahin, M. M. El-Ghar, and S. Gheith Rel, “TRAIL mRNA expression in peripheral blood mononuclear cells of Egyptian SLE patients,” Gene, vol. 527, pp. 211–214, 2013. View at Google Scholar
  104. J. Fullgrabe, D. J. Klionsky, and B. Joseph, “The return of the nucleus: transcriptional and epigenetic control of autophagy,” Nature Reviews Molecular Cell Biology, vol. 15, pp. 65–74, 2014. View at Google Scholar
  105. I. Tanida, T. Ueno, and E. Kominami, “LC3 conjugation system in mammalian autophagy,” International Journal of Biochemistry and Cell Biology, vol. 36, no. 12, pp. 2503–2518, 2004. View at Publisher · View at Google Scholar · View at Scopus
  106. X. H. Liang, S. Jackson, M. Seaman et al., “Induction of autophagy and inhibition of tumorigenesis by beclin 1,” Nature, vol. 402, no. 6762, pp. 672–676, 1999. View at Publisher · View at Google Scholar · View at Scopus
  107. Y. Murakami, J. W. Miller, and D. G. Vavvas, “RIP kinase-mediated necrosis as an alternative mechanisms of photoreceptor death,” Oncotarget, vol. 2, no. 6, pp. 497–509, 2011. View at Google Scholar · View at Scopus
  108. P. Vandenabeele, W. Declercq, F. Van Herreweghe, and T. V. Berghe, “The role of the kinases RIP1 and RIP3 in TNF-induced necrosis,” Science Signaling, vol. 3, no. 115, p. re4, 2010. View at Publisher · View at Google Scholar · View at Scopus
  109. N. Holler, R. Zaru, O. Micheau et al., “Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule,” Nature Immunology, vol. 1, no. 6, pp. 489–495, 2000. View at Google Scholar · View at Scopus
  110. J. Lin, H. Li, M. Yang et al., “A role of RIP3-mediated macrophage necrosis in atherosclerosis development,” Cell Reports, vol. 3, pp. 200–210, 2013. View at Google Scholar
  111. P.-S. Welz, A. Wullaert, K. Vlantis et al., “FADD prevents RIP3-mediated epithelial cell necrosis and chronic intestinal inflammation,” Nature, vol. 477, no. 7364, pp. 330–334, 2011. View at Publisher · View at Google Scholar · View at Scopus
  112. D.-W. Zhang, J. Shao, J. Lin et al., “RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis,” Science, vol. 325, no. 5938, pp. 332–336, 2009. View at Publisher · View at Google Scholar · View at Scopus