參考文獻 |
1. Hsieh, J.J., et al., Renal cell carcinoma. Nature Reviews Disease Primers, 2017. 3: p.17009.
2. Cohen, H.T. and F.J. McGovern, Renal-cell carcinoma. New England Journal of Medicine, 2005. 353(23): p. 2477-2490.
3. Network, C.G.A.R., Comprehensive molecular characterization of clear cell renal cell carcinoma. Nature, 2013. 499(7456): p. 43.
4. Peña-Llopis, S., et al., BAP1 loss defines a new class of renal cell carcinoma. Nature genetics, 2012. 44(7): p. 751.
5. Ricketts, C.J., et al., Genome-wide CpG island methylation analysis implicates novel genes in the pathogenesis of renal cell carcinoma. Epigenetics, 2012. 7(3): p. 278-290.
6. Pritchett, T.L., et al., Conditional inactivation of the mouse von Hippel-Lindau tumor suppressor gene results in wide-spread hyperplastic, inflammatory and fibrotic lesions in the kidney. Oncogene, 2015. 34(20): p. 2631-9.
7. Hagiwara, Yuki, Study of the association between inflammation and the initiation of renal cell carcinoma: microarray-based gene profiling analysis. National Central
Unoversity, Master Thesis, 2016.
8. Czerniak, B., C. Dinney, and D. McConkey, Origins of Bladder Cancer. Annu Rev Pathol, 2016. 11: p. 149-74.
9. Roupret, M., et al., European Association of Urology Guidelines on Upper Urinary Tract Urothelial Cell Carcinoma: 2015 Update. Eur Urol, 2015. 68(5): p. 868-79.
10. Sjodahl, G., et al., A molecular taxonomy for urothelial carcinoma. Clin Cancer Res, 2012. 18(12): p. 3377-86.
11. Van Batavia, J., et al., Bladder cancers arise from distinct urothelial sub-populations. Nat Cell Biol, 2014. 16(10): p. 982-91, 1-5.
12. Chen, C.H., et al., Aristolochic acid-associated urothelial cancer in Taiwan. Proc Natl Acad Sci U S A, 2012. 109(21): p. 8241-6.
13. Turesky, R.J., et al., Aristolochic acid exposure in Romania and implications for renal cell carcinoma. British journal of cancer, 2016. 114(1): p. 76.
14. Hoang, M.L., et al., Aristolochic acid in the etiology of renal cell carcinoma. Cancer Epidemiology and Prevention Biomarkers, 2016.
15. Feldman, D.E., et al., Formation of the VHL–elongin BC tumor suppressor complex is mediated by the chaperonin TRiC. Molecular cell, 1999. 4(6): p. 1051-1061.
16. Zhang, J., et al., VHL substrate transcription factor ZHX2 as an oncogenic driver in clear cell renal cell carcinoma. Science, 2018. 361(6399): p. 290-295.
17. Kuo, C.Y., C.H. Lin, and T. Hsu, VHL Inactivation in Precancerous Kidney Cells Induces an Inflammatory Response via ER Stress-Activated IRE1alpha Signaling.
Cancer Res, 2017. 77(13): p. 3406-3416.
18. Butler, M.R., et al., Endoplasmic reticulum (ER) Ca(2+)-channel activity contributes to ER stress and cone death in cyclic nucleotide-gated channel deficiency. J Biol Chem, 2017. 292(27): p. 11189-11205.
19. Wu, X., et al., A genome-wide association study identifies a novel susceptibility locus for renal cell carcinoma on 12p11.23. Hum Mol Genet, 2012. 21(2): p. 456-62.
20. Nowak, G., P.M. Price, and R.G. Schnellmann, Lack of a functional p21 WAF1/CIP1 gene accelerates caspase-independent apoptosis induced by cisplatin in renal cells.
American Journal of Physiology-Renal Physiology, 2003. 285(3): p. F440-F450.
21. Klagsbrun, M. and A. Eichmann, A role for axon guidance receptors and ligands in blood vessel development and tumor angiogenesis. Cytokine Growth Factor Rev,
2005. 16(4-5): p. 535-48.
22. Biankin, A.V., et al., Pancreatic cancer genomes reveal aberrations in axon guidance pathway genes. Nature, 2012. 491(7424): p. 399-405.
23. Basile, J.R., et al., Semaphorin 4D provides a link between axon guidance processes and tumor-induced angiogenesis. Proceedings of the National Academy of Sciences,
2006. 103(24): p. 9017-9022.
24. Van Buul, J.D. and P.L. Hordijk, Signaling in leukocyte transendothelial migration. Arteriosclerosis, thrombosis, and vascular biology, 2004. 24(5): p. 824-833.
25. Cook‐Mills, J.M. and T.L. Deem, Active participation of endothelial cells in inflammation. Journal of leukocyte biology, 2005. 77(4): p. 487-495.
26. Imhof, B.A. and M. Aurrand-Lions, Adhesion mechanisms regulating the migration of monocytes. Nature Reviews Immunology, 2004. 4(6): p. 432.
27. Polyak, S.J., Hepatitis C virus–cell interactions and their role in pathogenesis. Clinics in liver disease, 2003. 7(1): p. 67-88.
28. Gale Jr, M. and E.M. Foy, Evasion of intracellular host defence by hepatitis C virus. Nature, 2005. 436(7053): p. 939.
29. Kountouras, J., C. Zavos, and D. Chatzopoulos, Apoptosis in hepatitis C. Journal of viral hepatitis, 2003. 10(5): p. 335-342.
30. Pieperhoff, S., Gene Mutations Resulting in the Development of ARVC/D Could Affect Cells of the Cardiac Conduction System. Front Physiol, 2012. 3: p. 22.
31. Zhang, M., et al., PKP2 Mutations in Sudden Death From Arrhythmogenic Right Ventricular Cardiomyopathy (ARVC) and Sudden Unexpected Death With Negative
Autopsy (SUDNA). Circulation Journal, 2012. 76(1): p. 189-194.
32. Fatkin, D. and R.M. Graham, Molecular mechanisms of inherited cardiomyopathies. Physiological reviews, 2002. 82(4): p. 945-980.
33. Shapiro-Shelef, M. and K. Calame, Regulation of plasma-cell development. Nature Reviews Immunology, 2005. 5(3): p. 230.
34. Radtke, F., et al., Notch regulation of lymphocyte development and function. Nature immunology, 2004. 5(3): p. 247.
35. Zihni, C., et al., Tight junctions: from simple barriers to multifunctional molecular gates. Nature reviews Molecular cell biology, 2016. 17(9): p. 564.
36. Martin-Belmonte, F. and M. Perez-Moreno, Epithelial cell polarity, stem cells and cancer. Nature Reviews Cancer, 2012. 12(1): p. 23.
37. Takimoto, E., Cyclic GMP-dependent signaling in cardiac myocytes. Circulation Journal, 2012. 76(8): p. 1819-1825.
38. Murthy, K.S., Signaling for contraction and relaxation in smooth muscle of the gut. Annu. Rev. Physiol., 2006. 68: p. 345-374.
39. Li, N., et al., Sulindac selectively inhibits colon tumor cell growth by activating the cGMP/PKG pathway to suppress Wnt/β-catenin signaling. Molecular cancer
therapeutics, 2013: p. molcanther. 0048.2013.
40. Montoya, M.C., et al., Cell adhesion and polarity during immune interactions. Immunological reviews, 2002. 186(1): p. 68-82.
41. Yamagata, M., J.R. Sanes, and J.A. Weiner, Synaptic adhesion molecules. Current opinion in cell biology, 2003. 15(5): p. 621-632.
42. Dejana, E., Endothelial cell–cell junctions: happy together. Nature reviews Molecular cell biology, 2004. 5(4): p. 261.
43. Tahara, M., et al., RhoA/Rho-kinase cascade is involved in oxytocin-induced rat uterine contraction. Endocrinology, 2002. 143(3): p. 920-929.
44. Gutkowska, J., et al., Oxytocin releases atrial natriuretic peptide by combining with oxytocin receptors in the heart. Proceedings of the National Academy of Sciences, 1997. 94(21): p. 11704-11709.
45. Cassoni, P., et al., Oxytocin inhibits the proliferation of MDA‐MB231 human breastcancer cells via cyclic adenosine monophosphate and protein kinase A. International journal of cancer, 1997. 72(2): p. 340-344.
46. del Peso, L., et al., The von Hippel Lindau/hypoxia-inducible factor (HIF) pathway regulates the transcription of the HIF-proline hydroxylase genes in response to low oxygen. J Biol Chem, 2003. 278(49): p. 48690-5.
47. Lee, S., et al., Neuronal apoptosis linked to EglN3 prolyl hydroxylase and familial pheochromocytoma genes: developmental culling and cancer. Cancer Cell, 2005. 8(2):p. 155-67.
48. Fu, J., et al., EGLN3 prolyl hydroxylase regulates skeletal muscle differentiation and myogenin protein stability. J Biol Chem, 2007. 282(17): p. 12410-8.
49. Melo, R.C.C., et al., CXCR7 is highly expressed in acute lymphoblastic leukemia and potentiates CXCR4 response to CXCL12. PLoS One, 2014. 9(1): p. e85926.
50. Guo, F., et al., CXCL12/CXCR4: a symbiotic bridge linking cancer cells and their stromal neighbors in oncogenic communication networks. Oncogene, 2016. 35(7): p.
816-26.
51. Collins, P.J., et al., Epithelial chemokine CXCL14 synergizes with CXCL12 via allosteric modulation of CXCR4. FASEB J, 2017. 31(7): p. 3084-3097.
52. Kanter, J.A., et al., Decreased CXCL12 is associated with impaired alveolar epithelial cell migration and poor lung healing after lung resection. Surgery, 2015. 158(4): p. 1073-80; discussion 1080-2.
53. Yang, S.M., et al., Joint Effect of Urinary Total Arsenic Level and VEGF-A Genetic Polymorphisms on the Recurrence of Renal Cell Carcinoma. PLoS One, 2015. 10(12):
p. e0145410.
54. Claesson‐Welsh, L. and M. Welsh, VEGFA and tumour angiogenesis. Journal of internal medicine, 2013. 273(2): p. 114-127.
55. Brito, M.J., et al., Association of transforming growth factor alpha (TGFA) and its precursors with malignant change in Barrett′s epithelium: biological and clinical variables. International journal of cancer, 1995. 60(1): p. 27-32.
56. Degl′Innocenti, D., et al., Integrated ligand-receptor bioinformatic and in vitro functional analysis identifies active TGFA/EGFR signaling loop in papillary thyroid carcinomas. PLoS One, 2010. 5(9): p. e12701.
57. Siveke, J.T., et al., Concomitant pancreatic activation of Kras(G12D) and Tgfa results in cystic papillary neoplasms reminiscent of human IPMN. Cancer Cell, 2007. 12(3):p. 266-79.
58. Yamasaki, T., et al., Tumor-suppressive microRNA-1291 directly regulates glucose transporter 1 in renal cell carcinoma. Cancer Sci, 2013. 104(11): p. 1411-9.
59. Chan, D.A., et al., Targeting GLUT1 and the Warburg effect in renal cell carcinoma by chemical synthetic lethality. Sci Transl Med, 2011. 3(94): p. 94ra70.
60. Xu, J., et al., Claudin 8 Contributes to Malignant Proliferation in Human Osteosarcoma U2OS Cells. Cancer Biother Radiopharm, 2015. 30(9): p. 400-4.
61. Angelow, S., E.E. Schneeberger, and A.S. Yu, Claudin-8 expression in renal epithelial cells augments the paracellular barrier by replacing endogenous claudin-2. J Membr Biol, 2007. 215(2-3): p. 147-59.
62. Ashikari, D., et al., CLDN8, an androgen-regulated gene, promotes prostate cancer cell proliferation and migration. Cancer Sci, 2017. 108(7): p. 1386-1393.
63. Zavala-Zendejas, V.E., et al., Claudin-6, 7, or 9 overexpression in the human gastric adenocarcinoma cell line AGS increases its invasiveness, migration, and proliferation rate. Cancer investigation, 2011. 29(1): p. 1-11.
64. Park, S.K., et al., Innate immunity and non-Hodgkin′s lymphoma (NHL) related genes in a nested case-control study for gastric cancer risk. PLoS One, 2012. 7(9): p.
e45274.
65. Loboda, A., et al., EMT is the dominant program in human colon cancer. BMC medical genomics, 2011. 4(1): p. 9.
66. Zhang, J.W., et al., Matrine inhibits the adhesion and migration of BCG823 gastric cancer cells by affecting the structure and function of the vasodilator-stimulated phosphoprotein (VASP). Acta Pharmacol Sin, 2013. 34(8): p. 1084-92.
67. Su, Z.-Z., et al., PEG-3, a nontransforming cancer progression gene, is a positive regulator of cancer aggressiveness and angiogenesis. Proceedings of the National
Academy of Sciences, 1999. 96(26): p. 15115-15120.
68. Kwon, H.J., et al., Expression of CD9 and CD82 in clear cell renal cell carcinoma and its clinical significance. Pathol Res Pract, 2014. 210(5): p. 285-90.
69. Yang, C.H., et al., EGFR over-expression in non-small cell lung cancers harboring EGFR mutations is associated with marked down-regulation of CD82. Biochim
Biophys Acta, 2015. 1852(7): p. 1540-9.
70. Yusenko, M.V., D. Zubakov, and G. Kovacs, Gene expression profiling of chromophobe renal cell carcinomas and renal oncocytomas by Affymetrix GeneChip
using pooled and individual tumours. International journal of biological sciences, 2009. 5(6): p. 517.
71. Liao, C., W. Chen, and J. Wang, MicroRNA-20a Regulates Glioma Cell Proliferation, Invasion, and Apoptosis by Targeting CUGBP Elav-Like Family Member 2. World
Neurosurg, 2018.
72. Deckers, I.A., et al., Promoter CpG island methylation in ion transport mechanisms and associated dietary intakes jointly influence the risk of clear-cell renal cell cancer. Int J Epidemiol, 2017. 46(2): p. 622-631.
73. Qian, Y., et al., Sodium Channel Subunit SCNN1B Suppresses Gastric Cancer Growth and Metastasis via GRP78 Degradation. Cancer Res, 2017. 77(8): p. 1968-1982.
74. Dardiotis, E., et al., Genetic variations in the SULF1 gene alter the risk of cervical cancer and precancerous lesions. Oncol Lett, 2018. 16(3): p. 3833-3841.
75. Lai, J.P., et al., The tumor suppressor function of human sulfatase 1 (SULF1) in carcinogenesis. J Gastrointest Cancer, 2008. 39(1-4): p. 149-58.
76. Lin, C.Y., et al., ADAM9 promotes lung cancer metastases to brain by a plasminogen activator-based pathway. Cancer Res, 2014. 74(18): p. 5229-43.
77. Erin, N., et al., Changes in expressions of ADAM9, 10, and 17 as well as alphasecretase activity in renal cell carcinoma. Urol Oncol, 2017. 35(1): p. 36 e15-36 e22.
78. Cuadros, T., et al., HAVCR/KIM-1 activates the IL-6/STAT-3 pathway in clear cell renal cell carcinoma and determines tumor progression and patient outcome. Cancer
Res, 2014. 74(5): p. 1416-28.
79. Bhattacharyya, S., et al., Cystathionine beta-synthase (CBS) contributes to advanced ovarian cancer progression and drug resistance. PLoS One, 2013. 8(11): p. e79167.
80. Szabo, C., et al., Tumor-derived hydrogen sulfide, produced by cystathionine-betasynthase, stimulates bioenergetics, cell proliferation, and angiogenesis in colon
cancer. Proc Natl Acad Sci U S A, 2013. 110(30): p. 12474-9.
81. Hinrichsen, I., et al., Reduced migration of MLH1 deficient colon cancer cells depends on SPTAN1. Molecular cancer, 2014. 13(1): p. 11.
82. Bloch, M., et al., KCNMA1 gene amplification promotes tumor cell proliferation in human prostate cancer. Oncogene, 2007. 26(17): p. 2525-34.
83. Oeggerli, M., et al., Role of KCNMA1 in breast cancer. PLoS One, 2012. 7(8): p.e41664.
84. Khaitan, D., et al., Role of KCNMA1 gene in breast cancer invasion and metastasis to brain. BMC Cancer, 2009. 9: p. 258. |