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Scientifica
Volume 2013 (2013), Article ID 143589, 17 pages
http://dx.doi.org/10.1155/2013/143589
Review Article

Free-Radical Polymer Science Structural Cancer Model: A Review

Department of Biomaterials and Biomedical Engineering, The University of Alabama at Birmingham, SDB 539, 1919 7th Avenue South, Birmingham, AL 35294, USA

Received 2 December 2012; Accepted 20 December 2012

Academic Editors: S. Fukushige, K. Jung, and S.-Y. Shieh

Copyright © 2013 Richard C. Petersen. 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. National Cancer Institute/National Institutes of Health/Department of Health and Human Services, What You Need To Know About Cancer, NIH, 2006.
  2. T. S. Deisboeck and G. S. Stamatakos, Multiscale Cancer Modeling, Chapman & Hall/ CRC Press, Boca Raton, Fla, USA, 2011.
  3. B. Kwabi-Addo and T. L. Lindstrom, Cancer Causes and Controversies, Praeger, Barbara, Calif, USA, 2011.
  4. R. A. Weinberg, The Biology of Cancer, Garland Science, New York, NY, USA, 2007.
  5. R. Doll and A. B. Hill, “Lung cancer and other causes of death in relation to smoking: a second report on the mortality of British doctors,” British Medical Journal, vol. 233, pp. 1071–1076, 1956.
  6. G. M. Findlay, “Ultra-violet light and skin cancer,” The Lancet, vol. 212, no. 5491, pp. 1070–1073, 1928. View at Scopus
  7. H. J. Muller, “The production of mutations by X-rays,” Proceedings of the National Academy of Sciences of the United States of America, vol. 14, no. 9, pp. 714–726, 1928.
  8. I. Berenblum, “The mechanism of carcinogenesis. A study of the significance of cocarcinogenic action and related phenomena,” Cancer Research, vol. 1, article 807, 1941.
  9. J. G. Kidd and P. Rous, “The carcinogenic effect of a papilloma virus on the tarred skin of radibts: II Major factors determining the phenomenon: the manifold effects of tarring,” The Journal of Experimental Medicine, vol. 68, pp. 529–562, 1938.
  10. C. Huggins and C. V. Hodges, “Studies on prostatic cancer: I. The effect of castration, of estrogen and of androgen injection on serum phosphatases in metastatic carcinoma of the prostate,” Cancer Research, vol. 1, article 293, 1941.
  11. A. Tanenbaum and H. Silverstone, “The influence of the degree of caloric restriction on the formation of skin tumors and hepatomas in mice,” Cancer Research, vol. 9, no. 12, pp. 724–727, 1949. View at Scopus
  12. O. Warburg, K. Posener, and E. Negelein, “The metabolism of the cancer cell,” Biochemische Zeitschrift, vol. 152, pp. 319–344, 1924.
  13. S. Weinhouse, O. Warburg, D. Burk, and A. L. Schade, “On respiratory impairment in cancer cells,” Science, vol. 124, no. 3215, pp. 269–270, 1956. View at Scopus
  14. R. J. Gillies, The Tumour Microenvironment: Causes and Consequences of Hypoxia and Acidity, Novartis Foundation Symposium 240, John Wiley & Sons, New York, NY, USA, 2001.
  15. J. C. Stavridis, Oxidation: the Cornerstone of Carcinogenesis, Springer, New York, NY, USA, 2008.
  16. V. C. Fogg, N. J. Lanning, and J. P. MacKeigan, “Mitochondria in cancer: at the crossroads of life and death,” Chinese Journal of Cancer, vol. 30, no. 8, pp. 526–539, 2011. View at Publisher · View at Google Scholar
  17. L. Sherwood, Human Physiology, Thompson Brooks/Cole, Belmont, Calif, USA, 5th edition, 2004.
  18. R. Harvey and D. Ferrier, Biochemistry, Wolters Kluwer/Lippincott Williams & Wilkins, Philadelphia, Pa, USA, 5th edition, 2011.
  19. A. J. Schetter, N. H. H. Heegaard, and C. C. Harris, “Inflammation and cancer: interweaving microRNA, free radical, cytokine and p53 pathways,” Carcinogenesis, vol. 31, no. 1, pp. 37–49, 2009. View at Publisher · View at Google Scholar · View at Scopus
  20. J. Wang and J. Yi, “Cancer cell killing via ROS: to increase or decrease, that is a question,” Cancer Biology and Therapy, vol. 7, no. 12, pp. 1875–1884, 2008. View at Scopus
  21. M. P. Murphy, “How mitochondria produce reactive oxygen species,” Biochemical Journal, vol. 417, no. 1, pp. 1–13, 2009. View at Publisher · View at Google Scholar · View at Scopus
  22. R. C. Petersen, “Reactive secondary sequence oxidative pathology polymer model and antioxidant tests,” International Journal of Pure and Applied Chemistry, vol. 2, no. 4, pp. 247–285, 2012.
  23. J. McMurry, Organic Chemistry, Thomson/Brooks/Cole, Belmont, Calif, USA, 6th edition, 2004.
  24. J. M. Lü, P. H. Lin, Q. Yao, and C. Chen, “Chemical and molecular mechanisms of antioxidants: experimental approaches and model systems,” Journal of Cellular and Molecular Medicine, vol. 14, no. 4, pp. 840–860, 2010. View at Publisher · View at Google Scholar · View at Scopus
  25. X. A. J. Peacock and A. Calhoun, Polymer Chemistry Properties and Applications, Hanser, Munich, Germany, 2006.
  26. I. Mironi-Harpaz, M. Narkis, and A. Siegmann, “Peroxide crosslinking of a styrene-free unsaturated polyester,” Journal of Applied Polymer Science, vol. 105, no. 2, pp. 885–892, 2007. View at Publisher · View at Google Scholar · View at Scopus
  27. Y. Wang, L. Woodworth, and B. Han, “Simultaneous measurement of effective chemical shrinkage and modulus evolutions during polymerization,” Experimental Mechanics, vol. 51, no. 7, pp. 1155–1169, 2011. View at Publisher · View at Google Scholar · View at Scopus
  28. D. Recupero, L. Annaratone, F. Maletta, and G. Bussolati, “Nuclear shape in papillary thyroid carcinoma: a role for lamin b receptor?” Romanian Journal of Morphology and Embryology, vol. 51, no. 4, pp. 615–620, 2010. View at Scopus
  29. V. A. McCormack and I. Dos Santos Silva, “Breast density and parenchymal patterns as markers of breast cancer risk: a meta-analysis,” Cancer Epidemiology Biomarkers and Prevention, vol. 15, no. 6, pp. 1159–1169, 2006. View at Publisher · View at Google Scholar · View at Scopus
  30. C. M. Kraning-Rush, J. P. Califano, and C. A. Reinhart-King, “Cellular traction stresses increase with increasing metastatic potential,” PLoS ONE, vol. 7, no. 2, Article ID e32572, 2012. View at Publisher · View at Google Scholar
  31. G. Y. Li and J. L. Koenig, “FTIR imaging of oxidation of polyisoprene 2. The role of N-phenyl-N′-dimethyl-butyl-p-phenylenediamine antioxidant,” Polymer Degradation and Stability, vol. 81, no. 3, pp. 377–385, 2003. View at Publisher · View at Google Scholar · View at Scopus
  32. G. Helmlinger, F. Yuan, M. Dellian, and R. K. Jain, “Interstitial pH and pO2 gradients in solid tumors in vivo: high-resolution measurements reveal a lack of correlation,” Nature Medicine, vol. 3, no. 2, pp. 177–182, 1997. View at Publisher · View at Google Scholar · View at Scopus
  33. J. Michael and S. Sircar, Fundamentals of Medical Physiology, Thieme, New York, NY, USA, 2011.
  34. B. Alberts, A. Johnson, J. Lewis, M. Raff, K. Roberts, and P. Walters, Molecular Biology of the Cell, Garland Science, New York, NY, USA, 4th edition, 2002.
  35. L. Stryer, Biochemistry, W. H. Freeman and Company, New York, NY, USA, 4th edition, 1995.
  36. J. B. Wenger, S. Y. Chun, D. T. Dang, H. Luesch, and L. H. Dang, “Combination therapy targeting cancer metabolism,” Medical Hypotheses, vol. 76, no. 2, pp. 169–172, 2011. View at Publisher · View at Google Scholar · View at Scopus
  37. N. J. Vardaxis, A Textbook of Pathology, Elsevier, New York, NY, USA, 2010.
  38. S. L. Robbins and M. Angell, Basic Pathology, WB Saunders, Philadelphia, Pa, USA, 1971.
  39. J. F. Kerr, A. H. Wyllie, and A. R. Currie, “Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics,” British Journal of Cancer, vol. 26, no. 4, pp. 239–257, 1972. View at Scopus
  40. L. A. Liotta, K. Tryggvason, and S. Garbisa, “Metastatic potential correlates with enzymatic degradation of basement membrane collagen,” Nature, vol. 284, no. 5751, pp. 67–68, 1980. View at Scopus
  41. P. A. Jones and S. M. Taylor, “Cellular differentiation, cytidine analogs and DNA methylation,” Cell, vol. 20, no. 1, pp. 85–93, 1980. View at Scopus
  42. A. Loveless, “Possible relevance of O-6 alkylation of deoxyguanosine to the mutagenicity and carcinogenicity of nitrosamines and nitrosamides,” Nature, vol. 223, no. 5202, pp. 206–207, 1969. View at Publisher · View at Google Scholar · View at Scopus
  43. P. F. Swann and P. N. Magee, “Nitrosamine-induced carcinogenesis. The alklylation of nucleic acids of the rat by N-methyl-N-nitrosourea, dimethylnitrosamine, dimethyl sulphate and methyl methanesulphonate,” Biochemical Journal, vol. 110, no. 1, pp. 39–47, 1968. View at Scopus
  44. M. Bignami, M. O'Driscoll, G. Aquilina, and P. Karran, “Unmasking a killer: DNA O6-methylguanine and the cytotoxicity of methylating agents,” Mutation Research, vol. 462, no. 2-3, pp. 71–82, 2000. View at Publisher · View at Google Scholar · View at Scopus
  45. P. Whyte, K. J. Buchkovich, J. M. Horowitz et al., “Association between an oncogene and an anti-oncogene: the adenovirus E1A proteins bind to the retinoblastoma gene product,” Nature, vol. 334, no. 6178, pp. 124–129, 1988. View at Scopus
  46. J. M. Nigro, S. J. Baker, A. C. Preisinger et al., “Mutations in the p53 gene occur in diverse human tumour types,” Nature, vol. 342, no. 6250, pp. 705–708, 1989. View at Publisher · View at Google Scholar · View at Scopus
  47. S. J. Baker, E. R. Fearon, J. M. Nigro et al., “Chromosome 17 deletions and p53 gene mutations in colorectal carcinomas,” Science, vol. 244, no. 4901, pp. 217–221, 1989. View at Scopus
  48. C. J. Tabin, S. M. Bradley, and C. I. Bargmann, “Mechanism of activation of a human oncogene,” Nature, vol. 300, no. 5888, pp. 143–149, 1982. View at Scopus
  49. E. P. Reddy, R. K. Reynolds, E. Santos, and M. Barbacid, “A point mutation is responsible for the acquisition of transforming properties by the T24 human bladder carcinoma oncogene,” Nature, vol. 300, no. 5888, pp. 149–152, 1982. View at Scopus
  50. E. Taparowsky, Y. Suard, and O. Fasano, “Activation of the T24 bladder carcinoma transforming gene is linked to a single amino acid change,” Nature, vol. 300, no. 5894, pp. 762–765, 1982. View at Scopus
  51. S. T. Peters, Handbook of Composites, Chapman and Hall, New York, NY, USA, 2nd edition, 1998.
  52. K. M. B. Jansen, J. Vreugd de, and L. J. Ernst, “Analytical estimate for curing-induced stress and warpage in coating layers,” Journal of Applied Polymer Science, vol. 126, pp. 1623–1630, 2012.
  53. L. J. Deterding, D. C. Ramirez, J. R. Dubin, R. P. Mason, and K. B. Tomer, “Identification of free radicals on hemoglobin from its self-peroxidation using mass spectrometry and immuno-spin trapping: observation of a histidinyl radical,” The Journal of Biological Chemistry, vol. 279, no. 12, pp. 11600–11607, 2004. View at Publisher · View at Google Scholar · View at Scopus
  54. I. Ayala, K. Range, D. York, and B. A. Barry, “Spectroscopic properties of tyrosyl radicals in dipeptides,” Journal of the American Chemical Society, vol. 124, no. 19, pp. 5496–5505, 2002. View at Publisher · View at Google Scholar · View at Scopus
  55. I. R. Vassiliev, A. R. Offenbacher, and B. A. Barry, “Redox-active tyrosine residues in pentapeptides,” Journal of Physical Chemistry B, vol. 109, no. 48, pp. 23077–23085, 2005. View at Publisher · View at Google Scholar · View at Scopus
  56. T. Vinogradova, P. M. Miller, and I. Kaverina, “Microtubule network asymmetry in motile cells: role of Golgi-derived array,” Cell Cycle, vol. 8, no. 14, pp. 2168–2174, 2009. View at Scopus
  57. U. Lindberg, R. Karlsson, I. Lassing, C. E. Schutt, and A. S. Höglund, “The microfilament system and malignancy,” Seminars in Cancer Biology, vol. 18, no. 1, pp. 2–11, 2008. View at Publisher · View at Google Scholar · View at Scopus
  58. A. San Martín and K. K. Griendling, “Redox control of vascular smooth muscle migration,” Antioxidants and Redox Signaling, vol. 12, no. 5, pp. 625–640, 2010. View at Publisher · View at Google Scholar · View at Scopus
  59. L.-E. Copstead and J. Banasik, Pathophysiology, Elsevier Saunders, St. Louis, Mo, USA, 6th edition, 2005.
  60. Z. Li, M. Hannigan, Z. Mo et al., “Directional Sensing Requires Gβγ-Mediated PAK1 and PIXα-Dependent Activation of Cdc42,” Cell, vol. 114, no. 2, pp. 215–227, 2003. View at Publisher · View at Google Scholar · View at Scopus
  61. H. Hattori, K. K. Subramanian, J. Sakai, Y. Jia, Y. Li, T. F. Porter, et al., “Small-molecule screen identifies reacive oxygen species as key regulators of neutorphil chemotaxis,” PNAS, vol. 107, no. 8, pp. 3546–3551, 2010. View at Publisher · View at Google Scholar
  62. F. Parisi and M. Vidal, “Epithelial delamination and migration: lessons from Drosophila,” Cell Adhesion & Migration, vol. 5, no. 4, pp. 366–372, 2011.
  63. A. I. M. Barth, H. Y. Caro-Gonzalez, and W. J. Nelson, “Role of adenomatous polyposis coli (APC) and microtubules in directional cell migration and neuronal polarization,” Seminars in Cell and Developmental Biology, vol. 19, no. 3, pp. 245–251, 2008. View at Publisher · View at Google Scholar · View at Scopus
  64. E. W. Dent, S. L. Gupton, and F. B. Gertler, “The growth cone cytoskeleton in axon outgrowth and guidance,” Cold Spring Harbor Perspectives in Biologyl, vol. 3, no. 3, article 42, 2010.
  65. B. D. Ratner, A. S. Hoffman, F. J. Schoen, and J. E. Lemons, Biomaterials Science, Elsevier, San Diego, Calif, USA, 2004.
  66. J. Pokorný, A. Jandová, M. Nedbalová, et al., “Mitochondrial metabolism-neglected link of cancer transformation and treatment,” Prague Medical Report, vol. 113, no. 2, pp. 81–94, 2012.
  67. X. Zhu, M. M. Gallogly, J. J. Mieyal, V. E. Anderson, and L. M. Sayre, “Covalent cross-linking of glutathione and carnosine to proteins by 4-oxo-2-nonenal,” Chemical Research in Toxicology, vol. 22, no. 6, pp. 1050–1059, 2009. View at Publisher · View at Google Scholar · View at Scopus
  68. S. Saraswathy, G. Wu, and N. A. Rao, “Retinal microglial activation and chemotaxis by docosahexaenoic acid hydroperoxide,” Investigative Ophthalmology and Visual Science, vol. 47, no. 8, pp. 3656–3663, 2006. View at Publisher · View at Google Scholar · View at Scopus
  69. H. Zhang, B. C. Gau, L. M. Jones, I. Vidavsky, and M. L. Gross, “Fast photochemical oxidation of proteins for comparing structures of protein-ligand complexes: the calmodulin-peptide model system,” Analytical Chemistry, vol. 83, no. 1, pp. 311–318, 2011. View at Publisher · View at Google Scholar · View at Scopus
  70. R. Torosantucci, O. Mozziconacci, V. Sharov, C. Schöneich, and W. Jiskoot, “Chemical modifications in aggregates of recombinant human insulin induced by metal-catalyzed oxidation: covalent cross-linking via michael addition to tyrosine oxidation products,” Pharmaceutical Research, vol. 29, no. 8, pp. 2276–2293, 2012. View at Publisher · View at Google Scholar
  71. R. A. Dunlop, R. T. Dean, and K. J. Rodgers, “The impact of specific oxidized amino acids on protein turnover in J774 cells,” Biochemical Journal, vol. 410, no. 1, pp. 131–140, 2008. View at Publisher · View at Google Scholar · View at Scopus
  72. E. M. Darling, S. Zauscher, J. A. Block, and F. Guilak, “A thin-layer model for viscoelastic, stress-relaxation testing of cells using atomic force microscopy: do cell properties reflect metastatic potential?” Biophysical Journal, vol. 92, no. 5, pp. 1784–1791, 2007. View at Publisher · View at Google Scholar · View at Scopus
  73. F. Fleischer, R. Ananthakrishnan, S. Eckel et al., “Actin network architecture and elasticity in lamellipodia of melanoma cells,” New Journal of Physics, vol. 9, article 420, 2007. View at Publisher · View at Google Scholar · View at Scopus
  74. V. C. Abraham, V. Krishnamurthi, D. Lansing Taylor, and F. Lanni, “The actin-based nanomachine at the leading edge of migrating cells,” Biophysical Journal, vol. 77, no. 3, pp. 1721–1732, 1999. View at Scopus
  75. E. Atilgan, D. Wirtz, and S. X. Sun, “Morphology of the lamellipodium and organization of actin filaments at the leading edge of crawling cells,” Biophysical Journal, vol. 89, no. 5, pp. 3589–3602, 2005. View at Publisher · View at Google Scholar · View at Scopus
  76. Y. Qian, J. Luo, S. S. Leonard et al., “Hydrogen peroxide formation and actin filament reorganization by Cdc42 are essential for ethanol-induced in vitro angiogenesis,” The Journal of Biological Chemistry, vol. 278, no. 18, pp. 16189–16197, 2003. View at Publisher · View at Google Scholar · View at Scopus
  77. B. Gawdzik, J. Ksiȩzopolski, and T. Matynia, “Synthesis of new free-radical initiators for polymerization,” Journal of Applied Polymer Science, vol. 87, no. 14, pp. 2238–2243, 2003. View at Publisher · View at Google Scholar · View at Scopus
  78. Y. I. Miller, D. S. Worrall, C. D. Funk, J. R. Feramisco, and J. L. Witztum, “Actin polymerization in macrophages in response to oxidized LDL and apoptotic cells: role of 12/15-lipoxygenase and phosphoinositide 3-kinase,” Molecular Biology of the Cell, vol. 14, no. 10, pp. 4196–4206, 2003. View at Publisher · View at Google Scholar · View at Scopus
  79. M. Ushio-Fukai and Y. Nakamura, “Reactive oxygen species and angiogenesis: NADPH oxidase as target for cancer therapy,” Cancer Letters, vol. 266, no. 1, pp. 37–52, 2008. View at Publisher · View at Google Scholar · View at Scopus
  80. M. J. Hitchler and F. E. Domann, “Metabolic defects provide a spark for the epigenetic switch in cancer,” Free Radical Biology and Medicine, vol. 47, no. 2, pp. 115–127, 2009. View at Publisher · View at Google Scholar · View at Scopus
  81. C. L. Grek and K. D. Twe, “Redox metabolism and malignancy,” Current Opinion in Pharmacology, vol. 10, no. 4, pp. 362–368, 2010.
  82. M. Höckel and P. Vaupel, “Tumor hypoxia: definitions and current clinical, biologic, and molecular aspects,” Journal of the National Cancer Institute, vol. 93, no. 4, pp. 266–276, 2001. View at Scopus
  83. P. Vaupel, “The role of hypoxia-induced factors in tumor progression,” Oncologist, vol. 9, no. 5, pp. 10–17, 2004. View at Scopus
  84. D. M. Brizel, S. P. Scully, J. M. Harrelson et al., “Tumor oxygenation predicts for the likelihood of distant metastases in human soft tissue sarcoma,” Cancer Research, vol. 56, no. 5, pp. 941–943, 1996. View at Scopus
  85. S. P. Hussain and C. C. Harris, “Inflammation and cancer: an ancient link with novel potentials,” International Journal of Cancer, vol. 121, no. 11, pp. 2373–2380, 2007. View at Publisher · View at Google Scholar · View at Scopus
  86. G. W. Burton, K. H. Cheeseman, T. Doba, K. U. Ingold, and T. F. Slater, “Vitamin E as an antioxidant in vitro and in vivo,” Ciba Foundation symposium, vol. 101, pp. 4–18, 1983. View at Scopus
  87. G. W. Burton, K. H. Cheeseman, T. Doba, K. U. Ingold, and T. F. Slater, “Vitamin E as an antioxidant in vitro and in vivo,” in Ciba Foundation Symposium 101, Biology of Vitamin E, Pitman, London, UK, 1983.
  88. N. A. Porter, S. E. Caldwell, and K. A. Mills, “Mechanisms of free radical oxidation of unsaturated lipids,” Lipids, vol. 30, no. 4, pp. 277–290, 1995. View at Scopus
  89. C. Schneider, “An update on products and mechanisms of lipid peroxidation,” Molecular Nutrition and Food Research, vol. 53, no. 3, pp. 315–321, 2009. View at Publisher · View at Google Scholar · View at Scopus
  90. X. Lu and Y. Kang, “Hypoxia and hypoxia-inducible factors: master regulators of metastasis,” Clinical Cancer Research, vol. 16, no. 24, pp. 5928–5935, 2010. View at Publisher · View at Google Scholar · View at Scopus
  91. V. Swaminathan, K. Mythreye, E. Tim O'Brien, A. Berchuck, G. C. Blobe, and R. Superfine, “Mechanical Stiffness grades metastatic potential in patient tumor cells and in cancer cell lines,” Cancer Research, vol. 71, no. 15, pp. 5075–5080, 2011. View at Publisher · View at Google Scholar · View at Scopus
  92. G. L. Johanning, “Modulation of breast cancer cell adhesion by unsaturated fatty acids,” Nutrition, vol. 12, no. 11-12, pp. 810–816, 1996. View at Publisher · View at Google Scholar · View at Scopus
  93. Y. Yang, H. Hong, Y. Zhang, and W. Cai, “Molecular imaging of proteases in cancer,” Cancer Growth Metast, vol. 17, no. 2, pp. 13–27, 2009.
  94. J. Kim, W. Yu, K. Kovalski, and L. Ossowski, “Requirement for specific proteases in cancer cell intravasation as revealed by a novel semiquantitative PCR-based assay,” Cell, vol. 94, no. 3, pp. 353–362, 1998. View at Publisher · View at Google Scholar · View at Scopus
  95. E. Lee, J. Jeong, S. E. Kim, E. J. Song, S. W. Kang, and K. J. Lee, “Multiple functions of Nm23-H1 are regulated by oxido-reduction system,” PLoS ONE, vol. 4, no. 11, Article ID e7949, 2009. View at Publisher · View at Google Scholar · View at Scopus
  96. W. Xu, R. Mezencev, B. Kim, L. Wang, J. McDonald, and T. Sulchek, “Cell stiffness is a biomarker of the metastatic potential of ovarian cancer cells,” PLoS ONE, vol. 7, no. 10, Article ID e46609, 2012. View at Publisher · View at Google Scholar
  97. S. Ghosh, T. Kang, H. Wang, Y. Hu, and R. Li, “Mechanical phenotype is important for stromal aromatase expression,” Steroids, vol. 76, no. 8, pp. 797–801, 2011. View at Publisher · View at Google Scholar · View at Scopus
  98. K. Hoyt, B. Castaneda, M. Zhang et al., “Tissue elasticity properties as biomarkers for prostate cancer,” Cancer Biomarkers, vol. 4, no. 4-5, pp. 213–225, 2008. View at Scopus
  99. L. Trichet, J. Le Digabel, R. J. Hawkins et al., “Evidence of a large-scale mechanosensing mechanism for cellular adaptation to substrate stiffness,” Proceedings of the National Academy of Sciences of the United States of America, vol. 109, no. 18, pp. 6933–6938, 2012. View at Publisher · View at Google Scholar
  100. E. M. Darling, S. Zauscher, J. A. Block, and F. Guilak, “A thin-layer model for viscoelastic, stress-relaxation testing of cells using atomic force microscopy: do cell properties reflect metastatic potential?” Biophysical Journal, vol. 92, no. 5, pp. 1784–1791, 2007. View at Publisher · View at Google Scholar · View at Scopus
  101. R. A. Marcus and N. Sutin, “Electron transfers in chemistry and biology,” Biochimica et Biophysica Acta, vol. 811, no. 3, pp. 265–322, 1985. View at Publisher · View at Google Scholar · View at Scopus
  102. Y. H. Soung, J. L. Clifford, and J. Chung, “Crosstalk between integrin and receptor tyrosine kinase signaling in breast carcinoma progression,” BMB Reports, vol. 43, no. 5, pp. 311–318, 2010. View at Scopus
  103. R. R. Valiathan, M. Marco, B. Leitinger, C. G. Kleer, and R. Fridman, “Discoidin domain receptor tyrosine kinases: new players in cancer progression,” Cancer and Metastasis Reviews, vol. 31, no. 1-2, pp. 295–321, 2012. View at Publisher · View at Google Scholar
  104. K. Wolf, I. Mazo, H. Leung et al., “Compensation mechanism in tumor cell migration: mesenchymal-amoeboid transition after blocking of pericellular proteolysis,” Journal of Cell Biology, vol. 160, no. 2, pp. 267–277, 2003. View at Publisher · View at Google Scholar · View at Scopus
  105. American Cancer Society, “Nutrition and physical activity guidelines for cancer survivors,” CA—Cancer Journal for Clinicians, vol. 62, no. 4, pp. 275–276, 2012. View at Publisher · View at Google Scholar
  106. M. Goodman, R. M. Bostick, O. Kucuk, and D. P. Jones, “Clinical trials of antioxidants as cancer prevention agents: past, present, and future,” Free Radical Biology and Medicine, vol. 51, no. 5, pp. 1068–1084, 2011. View at Publisher · View at Google Scholar
  107. F. Rodriquez, Principles of Polymer SystemsEdition, Taylor & Francis, Washington, DC, USA, 4th edition, 1996.
  108. M. Jaffar, N. Abou-Zeid, L. Bai et al., “Quinone bioreductive prodrugs as delivery agents,” Current Drug Delivery, vol. 1, no. 4, pp. 345–350, 2004. View at Scopus
  109. S. J. Ralph, S. Rodríguez-Enríquez, J. Neuzil, E. Saavedra, and R. Moreno-Sánchez, “The causes of cancer revisited: “Mitochondrial malignancy” and ROS-induced oncogenic transformation—why mitochondria are targets for cancer therapy,” Molecular Aspects of Medicine, vol. 31, no. 2, pp. 145–170, 2010. View at Publisher · View at Google Scholar · View at Scopus
  110. N. Raghunand and R. J. Gillies In:, “pH and chemotherapy,” in The Tumour Microenvironment: Causes and Consequence of Hypoxia and Acidity, Novartis Foundation Symposium 240, pp. 199–211, Wiley, Chichester, UK, 2001.