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Journal of Immunology Research
Volume 2016, Article ID 4684268, 13 pages
http://dx.doi.org/10.1155/2016/4684268
Review Article

NK Cells, Tumor Cell Transition, and Tumor Progression in Solid Malignancies: New Hints for NK-Based Immunotherapy?

1Department of Experimental Medicine (DIMES), University of Genoa, 16132 Genova, Italy
2Center of Excellence for Biomedical Research (CEBR), University of Genoa, 16132 Genova, Italy
3Istituto Giannina Gaslini, 16147 Genova, Italy
4IRCCS AOU San Martino-IST, 16132 Genova, Italy
5Department of Functional Biology, IUOPA, University of Oviedo, 33006 Oviedo, Spain
6U1068, CRCM, Immunity and Cancer, INSERM, 1312 Marseille, France

Received 2 November 2015; Accepted 10 April 2016

Academic Editor: Stuart Berzins

Copyright © 2016 Claudia Cantoni 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. H. Spits, D. Artis, M. Colonna et al., “Innate lymphoid cells—a proposal for uniform nomenclature,” Nature Reviews Immunology, vol. 13, no. 2, pp. 145–149, 2013. View at Publisher · View at Google Scholar
  2. E. Montaldo, P. Vacca, L. Moretta, and M. C. Mingari, “Development of human natural killer cells and other innate lymphoid cells,” Seminars in Immunology, vol. 26, no. 2, pp. 107–113, 2014. View at Publisher · View at Google Scholar · View at Scopus
  3. E. Vivier, D. H. Raulet, A. Moretta et al., “Innate or adaptive immunity? The example of natural killer cells,” Science, vol. 331, no. 6013, pp. 44–49, 2011. View at Publisher · View at Google Scholar · View at Scopus
  4. E. Montaldo, P. Vacca, C. Vitale et al., “Human innate lymphoid cells,” Immunology Letters, 2016. View at Publisher · View at Google Scholar
  5. A. Cerwenka and L. L. Lanier, “Natural killer cell memory in infection, inflammation and cancer,” Nature Reviews Immunology, vol. 16, no. 2, pp. 112–123, 2016. View at Publisher · View at Google Scholar
  6. L. Moretta, C. Bottino, D. Pende, M. Vitale, M. C. Mingari, and A. Moretta, “Different checkpoints in human NK-cell activation,” Trends in Immunology, vol. 25, no. 12, pp. 670–676, 2004. View at Publisher · View at Google Scholar · View at Scopus
  7. C. Fauriat, E. O. Long, H.-G. Ljunggren, and Y. T. Bryceson, “Regulation of human NK-cell cytokine and chemokine production by target cell recognition,” Blood, vol. 115, no. 11, pp. 2167–2176, 2010. View at Publisher · View at Google Scholar · View at Scopus
  8. A. Moretta, E. Marcenaro, S. Sivori, M. D. Chiesa, M. Vitale, and L. Moretta, “Early liaisons between cells of the innate immune system in inflamed peripheral tissues,” Trends in Immunology, vol. 26, no. 12, pp. 668–675, 2005. View at Publisher · View at Google Scholar · View at Scopus
  9. F. Bellora, R. Castriconi, A. Dondero et al., “TLR activation of tumor-associated macrophages from ovarian cancer patients triggers cytolytic activity of NK cells,” European Journal of Immunology, vol. 44, no. 6, pp. 1814–1822, 2014. View at Publisher · View at Google Scholar · View at Scopus
  10. F. B. Thorén, R. E. Riise, J. Ousbäck et al., “Human NK cells induce neutrophil apoptosis via an NKp46- and Fas-dependent mechanism,” The Journal of Immunology, vol. 188, no. 4, pp. 1668–1674, 2012. View at Publisher · View at Google Scholar · View at Scopus
  11. A. Martín-Fontecha, L. L. Thomsen, S. Brett et al., “Induced recruitment of NK cells to lymph nodes provides IFN-γ for TH1 priming,” Nature Immunology, vol. 5, no. 12, pp. 1260–1265, 2004. View at Publisher · View at Google Scholar · View at Scopus
  12. F. Ghiringhelli, C. Ménard, F. Martin, and L. Zitvogel, “The role of regulatory T cells in the control of natural killer cells: relevance during tumor progression,” Immunological Reviews, vol. 214, no. 1, pp. 229–238, 2006. View at Publisher · View at Google Scholar · View at Scopus
  13. S. Sivori, M. Falco, M. Della Chiesa et al., “CpG and double-stranded RNA trigger human NK cells by toll-like receptors: induction of cytokine release and cytotoxicity against tumors dendritic cells,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 27, pp. 10116–10121, 2004. View at Publisher · View at Google Scholar · View at Scopus
  14. S. Sivori, S. Carlomagno, S. Pesce, A. Moretta, M. Vitale, and E. Marcenaro, “TLR/NCR/KIR: which one to use and when?” Frontiers in Immunology, vol. 5, article 105, 2014. View at Publisher · View at Google Scholar · View at Scopus
  15. M. A. Cooper, T. A. Fehniger, and M. A. Caligiuri, “The biology of human natural killer-cell subsets,” Trends in Immunology, vol. 22, no. 11, pp. 633–640, 2001. View at Publisher · View at Google Scholar · View at Scopus
  16. N. K. Björkström, P. Riese, F. Heuts et al., “Expression patterns of NKG2A, KIR, and CD57 define a process of CD56 dim NK-cell differentiation uncoupled from NK-cell education,” Blood, vol. 116, no. 19, pp. 3853–3864, 2010. View at Publisher · View at Google Scholar · View at Scopus
  17. S. Lopez-Vergès, J. M. Milush, S. Pandey et al., “CD57 defines a functionally distinct population of mature NK cells in the human CD56dimCD16+ NK-cell subset,” Blood, vol. 116, no. 19, pp. 3865–3874, 2010. View at Publisher · View at Google Scholar · View at Scopus
  18. L. Moretta, “Dissecting CD56dim human NK cells,” Blood, vol. 116, no. 19, pp. 3689–3691, 2010. View at Publisher · View at Google Scholar · View at Scopus
  19. T. Pradeu, S. Jaeger, and E. Vivier, “The speed of change: towards a discontinuity theory of immunity?” Nature Reviews Immunology, vol. 13, no. 10, pp. 764–769, 2013. View at Publisher · View at Google Scholar · View at Scopus
  20. S. Kim, K. Iizuka, H. L. Aguila, I. L. Weissman, and W. M. Yokoyama, “In vivo natural killer cell activities revealed by natural killer cell-deficient mice,” Proceedings of the National Academy of Sciences of the United States of America, vol. 97, no. 6, pp. 2731–2736, 2000. View at Publisher · View at Google Scholar · View at Scopus
  21. T. Lakshmikanth, S. Burke, T. H. Ali et al., “NCRs and DNAM-1 mediate NK cell recognition and lysis of human and mouse melanoma cell lines in vitro and in vivo,” The Journal of Clinical Investigation, vol. 119, no. 5, pp. 1251–1263, 2009. View at Publisher · View at Google Scholar · View at Scopus
  22. K. Imai, S. Matsuyama, S. Miyake, K. Suga, and K. Nakachi, “Natural cytotoxic activity of peripheral-blood lymphocytes and cancer incidence: an 11-year follow-up study of a general population,” The Lancet, vol. 356, no. 9244, pp. 1795–1799, 2000. View at Publisher · View at Google Scholar · View at Scopus
  23. A. Stojanovic and A. Cerwenka, “Natural killer cells and solid tumors,” Journal of Innate Immunity, vol. 3, no. 4, pp. 355–364, 2011. View at Publisher · View at Google Scholar · View at Scopus
  24. M. Vitale, C. Cantoni, G. Pietra, M. C. Mingari, and L. Moretta, “Effect of tumor cells and tumor microenvironment on NK-cell function,” European Journal of Immunology, vol. 44, no. 6, pp. 1582–1592, 2014. View at Publisher · View at Google Scholar · View at Scopus
  25. R. Castriconi, A. Dondero, F. Bellora et al., “Neuroblastoma-derived TGF-β1 modulates the chemokine receptor repertoire of human resting NK cells,” Journal of Immunology, vol. 190, no. 10, pp. 5321–5328, 2013. View at Publisher · View at Google Scholar · View at Scopus
  26. M. Della Chiesa, S. Carlomagno, G. Frumento et al., “The tryptophan catabolite L-kynurenine inhibits the surface expression of NKp46- and NKG2D-activating receptors and regulates NK-cell function,” Blood, vol. 108, no. 13, pp. 4118–4125, 2006. View at Publisher · View at Google Scholar · View at Scopus
  27. E. Schlecker, N. Fiegler, A. Arnold et al., “Metalloprotease-mediated tumor cell shedding of B7-H6, the ligand of the natural killer cell-activating receptor NKp30,” Cancer Research, vol. 74, no. 13, pp. 3429–3440, 2014. View at Publisher · View at Google Scholar · View at Scopus
  28. R. Castriconi, C. Cantoni, M. D. Chiesa et al., “Transforming growth factor β1 inhibits expression of NKP30 and NKG2d receptors: consequences for the NK-mediated killing of dendritic cells,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 7, pp. 4120–4125, 2003. View at Publisher · View at Google Scholar · View at Scopus
  29. B. Hoechst, T. Voigtlaender, L. Ormandy et al., “Myeloid derived suppressor cells inhibit natural killer cells in patients with hepatocellular carcinoma via the NKp30 receptor,” Hepatology, vol. 50, no. 3, pp. 799–807, 2009. View at Publisher · View at Google Scholar · View at Scopus
  30. M. F. Sprinzl, F. Reisinger, A. Puschnik et al., “Sorafenib perpetuates cellular anticancer effector functions by modulating the crosstalk between macrophages and natural killer cells,” Hepatology, vol. 57, no. 6, pp. 2358–2368, 2013. View at Publisher · View at Google Scholar · View at Scopus
  31. M. Balsamo, F. Scordamaglia, G. Pietra et al., “Melanoma-associated fibroblasts modulate NK cell phenotype and antitumor cytotoxicity,” Proceedings of the National Academy of Sciences of the United States of America, vol. 106, no. 49, pp. 20847–20852, 2009. View at Publisher · View at Google Scholar · View at Scopus
  32. G. Pietra, C. Manzini, S. Rivara et al., “Melanoma cells inhibit natural killer cell function by modulating the expression of activating receptors and cytolytic activity,” Cancer Research, vol. 72, no. 6, pp. 1407–1415, 2012. View at Publisher · View at Google Scholar · View at Scopus
  33. C. Pasero, G. W. Gravis, M. Guerin et al., “Inherent and tumor-driven immune tolerance in the prostate microenvironment impairs natural killer cell antitumor activity,” Cancer Research, vol. 76, no. 8, pp. 2153–2165, 2016. View at Publisher · View at Google Scholar
  34. B. Le Maux Chansac, A. Moretta, I. Vergnon et al., “NK cells infiltrating a MHC class I-deficient lung adenocarcinoma display impaired cytotoxic activity toward autologous tumor cells associated with altered NK Cell-triggering receptors,” The Journal of Immunology, vol. 175, no. 9, pp. 5790–5798, 2005. View at Publisher · View at Google Scholar · View at Scopus
  35. P. Carrega, I. Bonaccorsi, E. Di Carlo et al., “CD56brightperforinlow noncytotoxic human NK cells are abundant in both healthy and neoplastic solid tissues and recirculate to secondary lymphoid organs via afferent lymph,” The Journal of Immunology, vol. 192, no. 8, pp. 3805–3815, 2014. View at Publisher · View at Google Scholar
  36. P. Carrega, B. Morandi, R. Costa et al., “Natural killer cells infiltrating human nonsmall-cell lung cancer are enriched in CD56 bright CD16(−) cells and display an impaired capability to kill tumor cells,” Cancer, vol. 112, no. 4, pp. 863–875, 2008. View at Google Scholar
  37. S. Platonova, J. Cherfils-Vicini, D. Damotte et al., “Profound coordinated alterations of intratumoral NK cell phenotype and function in lung carcinoma,” Cancer Research, vol. 71, no. 16, pp. 5412–5422, 2011. View at Publisher · View at Google Scholar · View at Scopus
  38. C. S. Vetter, V. Groh, P. Thor Straten, T. Spies, E.-B. Bröcker, and J. C. Becker, “Expression of stress-induced MHC class I related chain molecules on human melanoma,” Journal of Investigative Dermatology, vol. 118, no. 4, pp. 600–605, 2002. View at Publisher · View at Google Scholar · View at Scopus
  39. G. Erdag, J. T. Schaefer, M. E. Smolkin et al., “Immunotype and immunohistologic characteristics of tumor-infiltrating immune cells are associated with clinical outcome in metastatic melanoma,” Cancer Research, vol. 72, no. 5, pp. 1070–1080, 2012. View at Publisher · View at Google Scholar · View at Scopus
  40. M. Messaoudene, G. Fregni, E. Fourmentraux-Neves et al., “Mature cytotoxic CD56bright/CD16+ natural killer cells can infiltrate lymph nodes adjacent to metastatic melanoma,” Cancer Research, vol. 74, no. 1, pp. 81–92, 2014. View at Publisher · View at Google Scholar · View at Scopus
  41. T. H. Ali, S. Pisanti, E. Ciaglia et al., “Enrichment of ​CD56dimKIR+​CD57+ highly cytotoxic NK cells in tumour-infiltrated lymph nodes of melanoma patients,” Nature Communications, vol. 5, article 5639, 2014. View at Publisher · View at Google Scholar
  42. N. Halama, M. Braun, C. Kahlert et al., “Natural killer cells are scarce in colorectal carcinoma tissue despite high levels of chemokines and cytokines,” Clinical Cancer Research, vol. 17, no. 4, pp. 678–689, 2011. View at Publisher · View at Google Scholar · View at Scopus
  43. Y. S. Rocca, M. P. Roberti, J. M. Arriaga et al., “Altered phenotype in peripheral blood and tumor-associated NK cells from colorectal cancer patients,” Innate Immunity, vol. 19, no. 1, pp. 76–85, 2013. View at Publisher · View at Google Scholar · View at Scopus
  44. R. Remark, M. Alifano, I. Cremer et al., “Characteristics and clinical impacts of the immune environments in colorectal and renal cell carcinoma lung metastases: influence of tumor origin,” Clinical Cancer Research, vol. 19, no. 15, pp. 4079–4091, 2013. View at Publisher · View at Google Scholar · View at Scopus
  45. E. Mamessier, A. Sylvain, M.-L. Thibult et al., “Human breast cancer cells enhance self tolerance by promoting evasion from NK cell antitumor immunity,” Journal of Clinical Investigation, vol. 121, no. 9, pp. 3609–3622, 2011. View at Publisher · View at Google Scholar · View at Scopus
  46. N. F. Delahaye, S. Rusakiewicz, I. Martins et al., “Alternatively spliced NKp30 isoforms affect the prognosis of gastrointestinal stromal tumors,” Nature Medicine, vol. 17, no. 6, pp. 700–707, 2011. View at Publisher · View at Google Scholar
  47. S. Rusakiewicz, M. Semeraro, M. Sarabi et al., “Immune infiltrates are prognostic factors in localized gastrointestinal stromal tumors,” Cancer Research, vol. 73, no. 12, pp. 3499–3510, 2013. View at Publisher · View at Google Scholar
  48. J. P. Thiery, H. Acloque, R. Y. J. Huang, and M. A. Nieto, “Epithelial-mesenchymal transitions in development and disease,” Cell, vol. 139, no. 5, pp. 871–890, 2009. View at Publisher · View at Google Scholar · View at Scopus
  49. K. Polyak and R. A. Weinberg, “Transitions between epithelial and mesenchymal states: acquisition of malignant and stem cell traits,” Nature Reviews Cancer, vol. 9, no. 4, pp. 265–273, 2009. View at Publisher · View at Google Scholar · View at Scopus
  50. K. Kemper, P. L. de Goeje, D. S. Peeper, and R. van Amerongen, “Phenotype switching: tumor cell plasticity as a resistance mechanism and target for therapy,” Cancer Research, vol. 74, no. 21, pp. 5937–5941, 2014. View at Publisher · View at Google Scholar · View at Scopus
  51. M. Balsamo, C. Manzini, G. Pietra et al., “Hypoxia downregulates the expression of activating receptors involved in NK-cell-mediated target cell killing without affecting ADCC,” European Journal of Immunology, vol. 43, no. 10, pp. 2756–2764, 2013. View at Publisher · View at Google Scholar · View at Scopus
  52. R. Kang, Q. Zhang, H. J. Zeh III, M. T. Lotze, and D. Tang, “HMGB1 in cancer: good, bad, or both?” Clinical Cancer Research, vol. 19, no. 15, pp. 4046–4057, 2013. View at Publisher · View at Google Scholar · View at Scopus
  53. L. Zhu, X. Li, Y. Chen, J. Fang, and Z. Ge, “High-mobility group Box 1: a novel inducer of the epithelial-mesenchymal transition in colorectal carcinoma,” Cancer Letters, vol. 357, no. 2, pp. 527–534, 2015. View at Publisher · View at Google Scholar · View at Scopus
  54. C. E. Meacham and S. J. Morrison, “Tumour heterogeneity and cancer cell plasticity,” Nature, vol. 501, no. 7467, pp. 328–337, 2013. View at Publisher · View at Google Scholar · View at Scopus
  55. J. H. Tsai and J. Yang, “Epithelial-mesenchymal plasticity in carcinoma metastasis,” Genes and Development, vol. 27, no. 20, pp. 2192–2206, 2013. View at Publisher · View at Google Scholar · View at Scopus
  56. J. P. Thiery and J. P. Sleeman, “Complex networks orchestrate epithelial-mesenchymal transitions,” Nature Reviews Molecular Cell Biology, vol. 7, no. 2, pp. 131–142, 2006. View at Publisher · View at Google Scholar · View at Scopus
  57. E. Pirilä, N. S. Ramamurthy, T. Sorsa, T. Salo, J. Hietanen, and P. Maisi, “Gelatinase A (MMP-2), collagenase-2 (MMP-8), and laminin-5 γ2-chain expression in murine inflammatory bowel disease (ulcerative colitis),” Digestive Diseases and Sciences, vol. 48, no. 1, pp. 93–98, 2003. View at Publisher · View at Google Scholar · View at Scopus
  58. G. Giannelli, C. Bergamini, E. Fransvea, C. Sgarra, and S. Antonaci, “Laminin-5 with transforming growth factor-β1 induces epithelial to mesenchymal transition in hepatocellular carcinoma,” Gastroenterology, vol. 129, no. 5, pp. 1375–1383, 2005. View at Publisher · View at Google Scholar · View at Scopus
  59. K. Cheng, G. Xie, and J.-P. Raufman, “Matrix metalloproteinase-7-catalyzed release of HB-EGF mediates deoxycholyltaurine-induced proliferation of a human colon cancer cell line,” Biochemical Pharmacology, vol. 73, no. 7, pp. 1001–1012, 2007. View at Publisher · View at Google Scholar · View at Scopus
  60. B. De Craene and G. Berx, “Regulatory networks defining EMT during cancer initiation and progression,” Nature Reviews Cancer, vol. 13, no. 2, pp. 97–110, 2013. View at Publisher · View at Google Scholar · View at Scopus
  61. A. Cano, M. A. Pérez-Moreno, I. Rodrigo et al., “The transcription factor Snail controls epithelial-mesenchymal transitions by repressing E-cadherin expression,” Nature Cell Biology, vol. 2, no. 2, pp. 76–83, 2000. View at Publisher · View at Google Scholar · View at Scopus
  62. J. Comijn, G. Berx, P. Vermassen et al., “The two-handed E box binding zinc finger protein SIP1 downregulates E-cadherin and induces invasion,” Molecular Cell, vol. 7, no. 6, pp. 1267–1278, 2001. View at Publisher · View at Google Scholar · View at Scopus
  63. K. M. Hajra, David Y-S. Chen, and E. R. Fearon, “The SLUG zinc-finger protein represses E-cadherin in breast cancer,” Cancer Research, vol. 62, no. 6, pp. 1613–1618, 2002. View at Google Scholar · View at Scopus
  64. V. Bolós, H. Peinado, M. A. Pérez-Moreno, M. F. Fraga, M. Esteller, and A. Cano, “The transcription factor Slug represses E-cadherin expression and induces epithelial to mesenchymal transitions: a comparison with Snail and E47 repressors,” Journal of Cell Science, vol. 116, part 3, pp. 499–511, 2003. View at Publisher · View at Google Scholar · View at Scopus
  65. J. Yang, S. A. Mani, J. L. Donaher et al., “Twist, a master regulator of morphogenesis, plays an essential role in tumor metastasis,” Cell, vol. 117, no. 7, pp. 927–939, 2004. View at Publisher · View at Google Scholar · View at Scopus
  66. P. A. Gregory, A. G. Bert, E. L. Paterson et al., “The miR-200 family and miR-205 regulate epithelial to mesenchymal transition by targeting ZEB1 and SIP1,” Nature Cell Biology, vol. 10, no. 5, pp. 593–601, 2008. View at Publisher · View at Google Scholar · View at Scopus
  67. N. R. Christoffersen, A. Silahtaroglu, U. A. Ørom, S. Kauppinen, and A. H. Lund, “miR-200b mediates post-transcriptional repression of ZFHX1B,” RNA, vol. 13, no. 8, pp. 1172–1178, 2007. View at Publisher · View at Google Scholar · View at Scopus
  68. K. S. Hoek, O. M. Eichhoff, N. C. Schlegel et al., “In vivo switching of human melanoma cells between proliferative and invasive states,” Cancer Research, vol. 68, no. 3, pp. 650–656, 2008. View at Publisher · View at Google Scholar · View at Scopus
  69. M. Sáez-Ayala, M. F. Montenegro, L. Sánchez-del-Campo et al., “Directed phenotype switching as an effective antimelanoma strategy,” Cancer Cell, vol. 24, no. 1, pp. 105–119, 2013. View at Publisher · View at Google Scholar · View at Scopus
  70. S. Huang, M. Hölzel, T. Knijnenburg et al., “MED12 controls the response to multiple cancer drugs through regulation of TGF-β receptor signaling,” Cell, vol. 151, no. 5, pp. 937–950, 2012. View at Publisher · View at Google Scholar · View at Scopus
  71. F. Z. Li, A. S. Dhillon, R. L. Anderson, G. McArthur, and P. T. Ferrao, “Phenotype switching in melanoma: implications for progression and therapy,” Frontiers in Oncology, vol. 5, article 31, 2015. View at Publisher · View at Google Scholar
  72. G. P. Dunn, L. J. Old, and R. D. Schreiber, “The three Es of cancer immunoediting,” Annual Review of Immunology, vol. 22, pp. 329–360, 2004. View at Publisher · View at Google Scholar · View at Scopus
  73. M. J. Smyth, “NK cells and NKT cells collaborate in host protection from methylcholanthrene-induced fibrosarcoma,” International Immunology, vol. 20, no. 4, p. 631, 2008. View at Publisher · View at Google Scholar · View at Scopus
  74. M. J. Smyth, N. Y. Crowe, and D. I. Godfrey, “NK cells and NKT cells collaborate in host protection from methylcholanthrene-induced fibrosarcoma,” International Immunology, vol. 13, no. 4, pp. 459–463, 2001. View at Publisher · View at Google Scholar · View at Scopus
  75. M. Girardi, D. E. Oppenheim, C. R. Steele et al., “Regulation of cutaneous malignancy by γδ T cells,” Science, vol. 294, no. 5542, pp. 605–609, 2001. View at Publisher · View at Google Scholar · View at Scopus
  76. D. Hanahan and L. M. Coussens, “Accessories to the crime: functions of cells recruited to the tumor microenvironment,” Cancer Cell, vol. 21, no. 3, pp. 309–322, 2012. View at Publisher · View at Google Scholar · View at Scopus
  77. C.-Y. Liu, J.-Y. Xu, X.-Y. Shi et al., “M2-polarized tumor-associated macrophages promoted epithelial-mesenchymal transition in pancreatic cancer cells, partially through TLR4/IL-10 signaling pathway,” Laboratory Investigation, vol. 93, no. 7, pp. 844–854, 2013. View at Publisher · View at Google Scholar · View at Scopus
  78. D. Marvel and D. I. Gabrilovich, “Myeloid-derived suppressor cells in the tumor microenvironment: expect the unexpected,” Journal of Clinical Investigation, vol. 125, no. 9, pp. 3356–3364, 2015. View at Publisher · View at Google Scholar · View at Scopus
  79. K. Oguma, H. Oshima, M. Aoki et al., “Activated macrophages promote Wnt signalling through tumour necrosis factor-α in gastric tumour cells,” The EMBO Journal, vol. 27, no. 12, pp. 1671–1681, 2008. View at Publisher · View at Google Scholar · View at Scopus
  80. B. Toh, X. Wang, J. Keeble et al., “Mesenchymal transition and dissemination of cancer cells is driven by myeloid-derived suppressor cells infiltrating the primary tumor,” PLoS Biology, vol. 9, no. 9, Article ID e1001162, 2011. View at Publisher · View at Google Scholar · View at Scopus
  81. C. Kudo-Saito, H. Shirako, T. Takeuchi, and Y. Kawakami, “Cancer metastasis is accelerated through immunosuppression during snail-induced EMT of cancer cells,” Cancer Cell, vol. 15, no. 3, pp. 195–206, 2009. View at Publisher · View at Google Scholar · View at Scopus
  82. C. Mayer, S. Darb-Esfahani, A. Meyer et al., “Neutrophil granulocytes in ovarian cancer—induction of epithelial-to-mesenchymal-transition and tumor cell migration,” Journal of Cancer, vol. 7, no. 5, pp. 546–554, 2016. View at Publisher · View at Google Scholar
  83. M. Ricciardi, M. Zanotto, G. Malpeli et al., “Epithelial-to-mesenchymal transition (EMT) induced by inflammatory priming elicits mesenchymal stromal cell-like immune-modulatory properties in cancer cells,” British Journal of Cancer, vol. 112, pp. 1067–1075, 2015. View at Publisher · View at Google Scholar · View at Scopus
  84. M. Kmieciak, K. L. Knutson, C. I. Dumur, and M. H. Manjili, “HER-2/neu antigen loss and relapse of mammary carcinoma are actively induced by T cell-mediated anti-tumor immune responses,” European Journal of Immunology, vol. 37, no. 3, pp. 675–685, 2007. View at Publisher · View at Google Scholar · View at Scopus
  85. K. L. Knutson, H. Lu, B. Stone et al., “Immunoediting of cancers may lead to epithelial to mesenchymal transition,” Journal of Immunology, vol. 177, no. 3, pp. 1526–1533, 2006. View at Publisher · View at Google Scholar · View at Scopus
  86. A. López-Soto, L. Huergo-Zapico, J. A. Galvan et al., “Epithelial-mesenchymal transition induces an antitumor immune response mediated by NKG2D receptor,” Journal of Immunology, vol. 190, no. 8, pp. 4408–4419, 2013. View at Publisher · View at Google Scholar · View at Scopus
  87. L. Huergo-Zapico, A. Acebes-Huerta, A. López-Soto, M. Villa-Álvarez, A. P. Gonzalez-Rodriguez, and S. Gonzalez, “Molecular bases for the regulation of NKG2D ligands in cancer,” Frontiers in Immunology, vol. 5, article 106, 2014. View at Publisher · View at Google Scholar · View at Scopus
  88. X.-H. Chen, Z.-C. Liu, G. Zhang et al., “TGF-β and EGF induced HLA-I downregulation is associated with epithelial-mesenchymal transition (EMT) through upregulation of snail in prostate cancer cells,” Molecular Immunology, vol. 65, no. 1, pp. 34–42, 2015. View at Publisher · View at Google Scholar · View at Scopus
  89. M. Balsamo, W. Vermi, M. Parodi et al., “Melanoma cells become resistant to NK-cell-mediated killing when exposed to NK-cell numbers compatible with NK-cell infiltration in the tumor,” European Journal of Immunology, vol. 42, no. 7, pp. 1833–1842, 2012. View at Publisher · View at Google Scholar · View at Scopus
  90. J. M. Taube, R. A. Anders, G. D. Young et al., “Colocalization of inflammatory response with B7-H1 expression in human melanocytic lesions supports an adaptive resistance mechanism of immune escape,” Science Translational Medicine, vol. 4, no. 127, Article ID 127ra37, 2012. View at Publisher · View at Google Scholar · View at Scopus
  91. D. M. Pardoll, “The blockade of immune checkpoints in cancer immunotherapy,” Nature Reviews Cancer, vol. 12, no. 4, pp. 252–264, 2012. View at Publisher · View at Google Scholar · View at Scopus
  92. J. M. Taube, G. D. Young, T. L. McMiller et al., “Differential expression of immune-regulatory genes associated with PD-L1 display in melanoma: implications for PD-1 pathway blockade,” Clinical Cancer Research, vol. 21, no. 17, pp. 3969–3976, 2015. View at Publisher · View at Google Scholar · View at Scopus
  93. R. Bellucci, A. Martin, D. Bommarito et al., “Interferon-γ-induced activation of JAK1 and JAK2 suppresses tumor cell susceptibility to NK cells through upregulation of PD-L1 expression,” OncoImmunology, vol. 4, no. 6, Article ID e1008824, 2015. View at Publisher · View at Google Scholar · View at Scopus
  94. L. Chen, D. L. Gibbons, S. Goswami et al., “Metastasis is regulated via microRNA-200/ZEB1 axis control of tumour cell PD-L1 expression and intratumoral immunosuppression,” Nature Communications, vol. 5, article 5241, 2014. View at Publisher · View at Google Scholar · View at Scopus
  95. N.-K. V. Cheung and M. A. Dyer, “Neuroblastoma: developmental biology, cancer genomics and immunotherapy,” Nature Reviews Cancer, vol. 13, no. 6, pp. 397–411, 2013. View at Publisher · View at Google Scholar · View at Scopus
  96. C. Bottino, A. Dondero, F. Bellora et al., “Natural killer cells and neuroblastoma: tumor recognition, escape mechanisms, and possible novel immunotherapeutic approaches,” Frontiers in Immunology, vol. 5, article 56, 2014. View at Publisher · View at Google Scholar · View at Scopus
  97. A. Dondero, F. Pastorino, M. Della Chiesa et al., “PD-L1 expression in metastatic neuroblastoma as an additional mechanism for limiting immune surveillance,” OncoImmunology, vol. 5, no. 1, Article ID e1064578, 2016. View at Publisher · View at Google Scholar
  98. S. Burke, T. Lakshmikanth, F. Colucci, and E. Carbone, “New views on natural killer cell-based immunotherapy for melanoma treatment,” Trends in Immunology, vol. 31, no. 9, pp. 339–345, 2010. View at Publisher · View at Google Scholar · View at Scopus
  99. M. H. Sandel, F. M. Speetjens, A. G. Menon et al., “Natural killer cells infiltrating colorectal cancer and MHC class I expression,” Molecular Immunology, vol. 42, no. 4, pp. 541–546, 2005. View at Publisher · View at Google Scholar · View at Scopus
  100. G. Esendagli, K. Bruderek, T. Goldmann et al., “Malignant and non-malignant lung tissue areas are differentially populated by natural killer cells and regulatory T cells in non-small cell lung cancer,” Lung Cancer, vol. 59, no. 1, pp. 32–40, 2008. View at Publisher · View at Google Scholar · View at Scopus
  101. D. R. Strayer, W. A. Carter, S. D. Mayberry, E. Pequignot, and I. Brodsky, “Low natural cytotoxicity of peripheral blood mononuclear cells in individuals with high familial incidence of cancer,” Cancer Research, vol. 44, no. 1, pp. 370–374, 1984. View at Google Scholar · View at Scopus
  102. G. Sconocchia, R. Arriga, L. Tornillo, L. Terracciano, S. Ferrone, and G. C. Spagnoli, “Melanoma cells inhibit NK cell functions,” Cancer Research, vol. 72, no. 20, pp. 5428–5430, 2012. View at Publisher · View at Google Scholar · View at Scopus
  103. P. A. Albertsson, P. H. Basse, M. Hokland et al., “NK cells and the tumour microenvironment: implications for NK-cell function and anti-tumour activity,” Trends in Immunology, vol. 24, no. 11, pp. 603–609, 2003. View at Publisher · View at Google Scholar · View at Scopus
  104. J. J. Campbell, S. Qin, D. Unutmaz et al., “Unique subpopulations of CD56+ NK and NK-T peripheral blood lymphocytes identified by chemokine receptor expression repertoire,” Journal of Immunology, vol. 166, no. 11, pp. 6477–6482, 2001. View at Publisher · View at Google Scholar · View at Scopus
  105. M. Inngjerdingen, B. Damaj, and A. A. Maghazachi, “Expression and regulation of chemokine receptors in human natural killer cells,” Blood, vol. 97, no. 2, pp. 367–375, 2001. View at Publisher · View at Google Scholar · View at Scopus
  106. G. Bernardini, A. Gismondi, and A. Santoni, “Chemokines and NK cells: regulators of development, trafficking and functions,” Immunology Letters, vol. 145, no. 1-2, pp. 39–46, 2012. View at Publisher · View at Google Scholar · View at Scopus
  107. F. Casilli, A. Bianchini, I. Gloaguen et al., “Inhibition of interleukin-8 (CXCL8/IL-8) responses by repertaxin, a new inhibitor of the chemokine receptors CXCR1 and CXCR2,” Biochemical Pharmacology, vol. 69, no. 3, pp. 385–394, 2005. View at Publisher · View at Google Scholar · View at Scopus
  108. M. J. Robertson, “Role of chemokines in the biology of natural killer cells,” Journal of Leukocyte Biology, vol. 71, no. 2, pp. 173–183, 2002. View at Google Scholar · View at Scopus
  109. D. L. Hodge, W. B. Schill, J. M. Wang et al., “IL-2 and IL-12 alter NK cell responsiveness to IFN-γ-inducible protein 10 by down-regulating CXCR3 expression,” Journal of Immunology, vol. 168, no. 12, pp. 6090–6098, 2002. View at Publisher · View at Google Scholar · View at Scopus
  110. S. Parolini, A. Santoro, E. Marcenaro et al., “The role of chemerin in the colocalization of NK and dendritic cell subsets into inflamed tissues,” Blood, vol. 109, no. 9, pp. 3625–3632, 2007. View at Publisher · View at Google Scholar · View at Scopus
  111. J. Barlic, J. M. Sechler, and P. M. Murphy, “IL-15 and IL-2 oppositely regulate expression of the chemokine receptor CX3CR1,” Blood, vol. 102, no. 10, pp. 3494–3503, 2003. View at Publisher · View at Google Scholar · View at Scopus
  112. R. B. Mailliard, S. M. Alber, H. Shen et al., “IL-18-induced CD83+CCR7+ NK helper cells,” The Journal of Experimental Medicine, vol. 202, no. 7, pp. 941–953, 2005. View at Publisher · View at Google Scholar · View at Scopus
  113. M. Wendel, I. E. Galani, E. Suri-Payer, and A. Cerwenka, “Natural killer cell accumulation in tumors is dependent on IFN-γ and CXCR3 ligands,” Cancer Research, vol. 68, no. 20, pp. 8437–8445, 2008. View at Publisher · View at Google Scholar · View at Scopus
  114. F. Vianello, N. Papeta, T. Chen et al., “Murine B16 melanomas expressing high levels of the chemokine stromal-derived factor-1/CXCL12 induce tumor-specific T cell chemorepulsion and escape from immune control,” The Journal of Immunology, vol. 176, no. 5, pp. 2902–2914, 2006. View at Publisher · View at Google Scholar · View at Scopus
  115. R. K. Pachynski, B. A. Zabel, H. E. Kohrt et al., “The chemoattractant chemerin suppresses melanoma by recruiting natural killer cell antitumor defenses,” Journal of Experimental Medicine, vol. 209, no. 8, pp. 1427–1435, 2012. View at Publisher · View at Google Scholar · View at Scopus
  116. J. O. Thomas and A. A. Travers, “HMG1 and 2, and related ‘architectural’ DNA-binding proteins,” Trends in Biochemical Sciences, vol. 26, no. 3, pp. 167–174, 2001. View at Publisher · View at Google Scholar · View at Scopus
  117. H. Lee, N. Shin, M. Song et al., “Analysis of nuclear high mobility group box 1 (HMGB1)-binding proteins in colon cancer cells: clustering with proteins involved in secretion and extranuclear function,” Journal of Proteome Research, vol. 9, no. 9, pp. 4661–4670, 2010. View at Publisher · View at Google Scholar · View at Scopus
  118. H. S. Hreggvidsdottir, T. Östberg, H. Wähämaa et al., “The alarmin HMGB1 acts in synergy with endogenous and exogenous danger signals to promote inflammation,” Journal of Leukocyte Biology, vol. 86, no. 3, pp. 655–662, 2009. View at Publisher · View at Google Scholar · View at Scopus
  119. A. Didangelos, M. Puglia, M. Iberl, C. Sanchez-Bellot, B. Roschitzki, and E. J. Bradbury, “High-throughput proteomics reveal alarmins as amplifiers of tissue pathology and inflammation after spinal cord injury,” Scientific Reports, vol. 6, Article ID 21607, 2016. View at Publisher · View at Google Scholar
  120. J. Thorburn, A. E. Frankel, and A. Thorburn, “Regulation of HMGB1 release by autophagy,” Autophagy, vol. 5, no. 2, pp. 247–249, 2009. View at Publisher · View at Google Scholar · View at Scopus
  121. M. T. Lotze, H. J. Zeh, A. Rubartelli et al., “The grateful dead: damage-associated molecular pattern molecules and reduction/oxidation regulate immunity,” Immunological Reviews, vol. 220, no. 1, pp. 60–81, 2007. View at Publisher · View at Google Scholar · View at Scopus
  122. H. Yang, P. Lundbäck, L. Ottosson et al., “Redox modification of cysteine residues regulates the cytokine activity of high mobility group box-1 (HMGB1),” Molecular Medicine, vol. 18, no. 2, pp. 250–259, 2012. View at Publisher · View at Google Scholar · View at Scopus
  123. E. Venereau, M. Casalgrandi, M. Schiraldi et al., “Mutually exclusive redox forms of HMGB1 promote cell recruitment or proinflammatory cytokine release,” Journal of Experimental Medicine, vol. 209, no. 9, pp. 1519–1528, 2012. View at Publisher · View at Google Scholar · View at Scopus
  124. R. R. Kew, M. Penzo, D. M. Habiel, and K. B. Marcu, “The IKKα-dependent NF-κB p52/RelB noncanonical pathway is essential to sustain a CXCL12 autocrine loop in cells migrating in response to HMGB1,” The Journal of Immunology, vol. 188, no. 5, pp. 2380–2386, 2012. View at Publisher · View at Google Scholar · View at Scopus
  125. M. Schiraldi, A. Raucci, L. M. Muñoz et al., “HMGB1 promotes recruitment of inflammatory cells to damaged tissues by forming a complex with CXCL12 and signaling via CXCR4,” The Journal of Experimental Medicine, vol. 209, no. 3, pp. 551–563, 2012. View at Publisher · View at Google Scholar · View at Scopus
  126. D. Yang, Q. Chen, H. Yang, K. J. Tracey, M. Bustin, and J. J. Oppenheim, “High mobility group box-1 protein induces the migration and activation of human dendritic cells and acts as an alarmin,” Journal of Leukocyte Biology, vol. 81, no. 1, pp. 59–66, 2007. View at Publisher · View at Google Scholar · View at Scopus
  127. H. Yang, H. S. Hreggvidsdottir, K. Palmblad et al., “A critical cysteine is required for HMGB1 binding to toll-like receptor 4 and activation of macrophage cytokine release,” Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 26, pp. 11942–11947, 2010. View at Publisher · View at Google Scholar · View at Scopus
  128. H. Kazama, J.-E. Ricci, J. M. Herndon, G. Hoppe, D. R. Green, and T. A. Ferguson, “Induction of immunological tolerance by apoptotic cells requires caspase-dependent oxidation of high-mobility group box-1 protein,” Immunity, vol. 29, no. 1, pp. 21–32, 2008. View at Publisher · View at Google Scholar · View at Scopus
  129. D. Tang, R. Kang, C.-W. Cheh et al., “HMGB1 release and redox regulates autophagy and apoptosis in cancer cells,” Oncogene, vol. 29, no. 38, pp. 5299–5310, 2010. View at Publisher · View at Google Scholar · View at Scopus
  130. T. Bonaldi, F. Talamo, P. Scaffidi et al., “Monocytic cells hyperacetylate chromatin protein HMGB1 to redirect it towards secretion,” The EMBO Journal, vol. 22, no. 20, pp. 5551–5560, 2003. View at Publisher · View at Google Scholar · View at Scopus
  131. B. Lu, D. J. Antoine, K. Kwan et al., “JAK/STAT1 signaling promotes HMGB1 hyperacetylation and nuclear translocation,” Proceedings of the National Academy of Sciences of the United States of America, vol. 111, no. 8, pp. 3068–3073, 2014. View at Publisher · View at Google Scholar · View at Scopus
  132. K. Davis, S. Banerjee, A. Friggeri, C. Bell, E. Abraham, and M. Zerfaoui, “Poly(ADP-Ribosyl)ation of high mobility group box 1 (HMGB1) protein enhances inhibition of efferocytosis,” Molecular Medicine, vol. 18, no. 3, pp. 359–369, 2012. View at Publisher · View at Google Scholar · View at Scopus
  133. X. Zhang, D. Wheeler, Y. Tang et al., “Calcium/calmodulin-dependent protein kinase (CaMK) IV mediates nucleocytoplasmic shuttling and release of HMGB1 during lipopolysaccharide stimulation of macrophages,” The Journal of Immunology, vol. 181, no. 7, pp. 5015–5023, 2008. View at Publisher · View at Google Scholar · View at Scopus
  134. Y. J. Oh, J. H. Youn, Y. Ji et al., “HMGB1 is phosphorylated by classical protein kinase C and is secreted by a calcium-dependent mechanism,” Journal of Immunology, vol. 182, no. 9, pp. 5800–5809, 2009. View at Publisher · View at Google Scholar · View at Scopus
  135. H. Lee, M. Park, N. Shin et al., “High mobility group box-1 is phosphorylated by protein kinase C zeta and secreted in colon cancer cells,” Biochemical and Biophysical Research Communications, vol. 424, no. 2, pp. 321–326, 2012. View at Publisher · View at Google Scholar · View at Scopus
  136. J. Taira and Y. Higashimoto, “Evaluation of in vitro properties of predicted kinases that phosphorylate serine residues within nuclear localization signal 1 of high mobility group box 1,” Journal of Peptide Science, vol. 20, no. 8, pp. 613–617, 2014. View at Publisher · View at Google Scholar · View at Scopus
  137. H. Wähämaa, H. Schierbeck, H. S. Hreggvidsdottir et al., “High mobility group box protein 1 in complex with lipopolysaccharide or IL-1 promotes an increased inflammatory phenotype in synovial fibroblasts,” Arthritis Research and Therapy, vol. 13, no. 4, article R136, 2011. View at Publisher · View at Google Scholar · View at Scopus
  138. H. S. Hreggvidsdóttir, A. M. Lundberg, A.-C. Aveberger, L. Klevenvall, U. Andersson, and H. E. Harris, “High mobility group box protein 1 (HMGB1)-partner molecule complexes enhance cytokine production by signaling through the partner molecule receptor,” Molecular Medicine, vol. 18, no. 2, pp. 224–230, 2012. View at Publisher · View at Google Scholar · View at Scopus
  139. G. Li, X. Liang, and M. T. Lotze, “HMGB1: the central cytokine for all lymphoid cells,” Frontiers in Immunology, vol. 4, article 68, 2013. View at Publisher · View at Google Scholar · View at Scopus
  140. S. Chiba, M. Baghdadi, H. Akiba et al., “Tumor-infiltrating DCs suppress nucleic acid-mediated innate immune responses through interactions between the receptor TIM-3 and the alarmin HMGB1,” Nature Immunology, vol. 13, no. 9, pp. 832–842, 2012. View at Publisher · View at Google Scholar · View at Scopus
  141. M. Pedrazzi, M. Averna, B. Sparatore et al., “Potentiation of NMDA receptor-dependent cell responses by extracellular high mobility group box 1 protein,” PLoS ONE, vol. 7, no. 8, Article ID e44518, 2012. View at Publisher · View at Google Scholar · View at Scopus
  142. S. Qin, H. Wang, R. Yuan et al., “Role of HMGB1 in apoptosis-mediated sepsis lethality,” The Journal of Experimental Medicine, vol. 203, no. 7, pp. 1637–1642, 2006. View at Publisher · View at Google Scholar · View at Scopus
  143. H. Wang, O. Bloom, M. Zhang et al., “HMG-1 as a late mediator of endotoxin lethality in mice,” Science, vol. 285, no. 5425, pp. 248–251, 1999. View at Publisher · View at Google Scholar · View at Scopus
  144. M. Parodi, M. Pedrazzi, C. Cantoni et al., “Natural Killer (NK)/melanoma cell interaction induces NK-mediated release of chemotactic High Mobility Group Box-1 (HMGB1) capable of amplifying NK cell recruitment,” OncoImmunology, vol. 4, no. 12, 2015. View at Publisher · View at Google Scholar · View at Scopus
  145. I. Ito, J. Fukazawa, and M. Yoshida, “Post-translational methylation of high mobility group box 1 (HMGB1) causes its cytoplasmic localization in neutrophils,” The Journal of Biological Chemistry, vol. 282, no. 22, pp. 16336–16344, 2007. View at Publisher · View at Google Scholar · View at Scopus
  146. M. M. Rabadi, M.-C. Kuo, T. Ghaly et al., “Interaction between uric acid and HMGB1 translocation and release from endothelial cells,” American Journal of Physiology—Renal Physiology, vol. 302, no. 6, pp. F730–F741, 2012. View at Publisher · View at Google Scholar · View at Scopus
  147. K. Feghali, K. Iwasaki, K. Tanaka et al., “Human gingival fibroblasts release high-mobility group box-1 protein through active and passive pathways,” Oral Microbiology and Immunology, vol. 24, no. 4, pp. 292–298, 2009. View at Publisher · View at Google Scholar · View at Scopus
  148. Y. Moriwaka, Y. Luo, H. Ohmori et al., “HMGB1 attenuates anti-metastatic defense of the lymph nodes in colorectal cancer,” Pathobiology, vol. 77, no. 1, pp. 17–23, 2010. View at Publisher · View at Google Scholar · View at Scopus
  149. F. Berthelot, L. Fattoum, S. Casulli, J. Gozlan, V. Maréchal, and C. Elbim, “The effect of HMGB1, a damage-associated molecular pattern molecule, on polymorphonuclear neutrophil migration depends on its concentration,” Journal of Innate Immunity, vol. 4, no. 1, pp. 41–58, 2012. View at Publisher · View at Google Scholar · View at Scopus
  150. J. L. Guerriero, D. Ditsworth, J. M. Catanzaro et al., “DNA alkylating therapy induces tumor regression through an HMGB1-mediated activation of innate immunity,” The Journal of Immunology, vol. 186, no. 6, pp. 3517–3526, 2011. View at Publisher · View at Google Scholar · View at Scopus
  151. P.-L. Liu, J.-R. Tsai, J.-J. Hwang et al., “High-mobility group box 1-mediated matrix metalloproteinase-9 expression in non-small cell lung cancer contributes to tumor cell invasiveness,” American Journal of Respiratory Cell and Molecular Biology, vol. 43, no. 5, pp. 530–538, 2010. View at Publisher · View at Google Scholar · View at Scopus
  152. G.-L. Yang, L.-H. Zhang, J.-J. Bo et al., “Increased expression of HMGB1 is associated with poor prognosis in human bladder cancer,” Journal of Surgical Oncology, vol. 106, no. 1, pp. 57–61, 2012. View at Publisher · View at Google Scholar · View at Scopus
  153. X. Yao, G. Zhao, H. Yang, X. Hong, L. Bie, and G. Liu, “Overexpression of high-mobility group box 1 correlates with tumor progression and poor prognosis in human colorectal carcinoma,” Journal of Cancer Research and Clinical Oncology, vol. 136, no. 5, pp. 677–684, 2010. View at Publisher · View at Google Scholar · View at Scopus
  154. C. A. Wild, S. Brandau, R. Lotfi et al., “HMGB1 is overexpressed in tumor cells and promotes activity of regulatory T cells in patients with head and neck cancer,” Oral Oncology, vol. 48, no. 5, pp. 409–416, 2012. View at Publisher · View at Google Scholar · View at Scopus
  155. C. B. Zhao, J. M. Bao, Y. J. Lu et al., “Co-expression of RAGE and HMGB1 is associated with cancer progression and poor patient outcome of prostate cancer,” American Journal of Cancer Research, vol. 4, no. 4, pp. 369–377, 2014. View at Google Scholar
  156. L. Zhang, J. Han, H. Wu et al., “The association of HMGB1 expression with clinicopathological significance and prognosis in hepatocellular carcinoma: a meta-analysis and literature review,” PLoS ONE, vol. 9, no. 10, Article ID e110626, 2014. View at Publisher · View at Google Scholar · View at Scopus
  157. G. Bao, Q. Qiao, H. Zhao, and X. He, “Prognostic value of HMGB1 overexpression in resectable gastric adenocarcinomas,” World Journal of Surgical Oncology, vol. 8, article 52, 2010. View at Publisher · View at Google Scholar · View at Scopus
  158. Q. Li, J. Li, T. Wen et al., “Overexpression of HMGB1 in melanoma predicts patient survival and suppression of HMGB1 induces cell cycle arrest and senescence in association with p21 (Waf1/Cip1) up-regulation via a p53-independent, Sp1-dependent pathway,” Oncotarget, vol. 5, no. 15, pp. 6387–6403, 2014. View at Publisher · View at Google Scholar · View at Scopus
  159. W. Yan, Y. Chang, X. Liang et al., “High-mobility group box 1 activates caspase-1 and promotes hepatocellular carcinoma invasiveness and metastases,” Hepatology, vol. 55, no. 6, pp. 1863–1875, 2012. View at Publisher · View at Google Scholar · View at Scopus
  160. J. R. van Beijnum, P. Nowak-Sliwinska, E. van Den Boezem, P. Hautvast, W. A. Buurman, and A. W. Griffioen, “Tumor angiogenesis is enforced by autocrine regulation of high-mobility group box 1,” Oncogene, vol. 32, no. 3, pp. 363–374, 2013. View at Publisher · View at Google Scholar · View at Scopus
  161. S. Mitola, M. Belleri, C. Urbinati et al., “Cutting edge: extracellular high mobility group box-1 protein is a proangiogenic cytokine,” Journal of Immunology, vol. 176, no. 1, pp. 12–15, 2006. View at Publisher · View at Google Scholar · View at Scopus
  162. S. Jost, U. Y. Moreno-Nieves, W. F. Garcia-Beltran et al., “Dysregulated Tim-3 expression on natural killer cells is associated with increased Galectin-9 levels in HIV-1 infection,” Retrovirology, vol. 10, article 74, 2013. View at Publisher · View at Google Scholar · View at Scopus
  163. A. A. Boldyrev, E. A. Bryushkova, and E. A. Vladychenskaya, “NMDA receptors in immune competent cells,” Biochemistry, vol. 77, no. 2, pp. 128–134, 2012. View at Publisher · View at Google Scholar · View at Scopus