Abstract
The emergence of highly aggressive subtypes of human cutaneous squamous cell carcinoma (SCC) often reflects increased autocrine/paracrine TGF-
The emergence of highly aggressive subtypes of human cutaneous squamous cell carcinoma (SCC) often reflects increased autocrine/paracrine TGF-
M. J. Eide and M. A. Weinstock, “Epidemiology of skin cancer,” in Cancer of the Skin, D. S. Rigel, R. J. Friedman, L. M. Dzubow, D. S. Reintgen, J.-C. Bystryn, and R. Marks, Eds., pp. 47–60, Elsevier, Philadelphia, Pa, USA, 2005.
View at: Google ScholarA. Dlugosz, G. Merlino, and S. H. Yuspa, “Progress in cutaneous cancer research,” Journal of Investigative Dermatology Symposium Proceedings, vol. 7, no. 1, pp. 17–26, 2002.
View at: Publisher Site | Google ScholarP. Boukamp, “UV-induced skin cancer: similarities-variations,” Journal of the German Society of Dermatology, vol. 3, no. 7, pp. 493–503, 2005.
View at: Publisher Site | Google ScholarM. Dans and S. S. Fakharzadeh, “Genetic basis of skin cancer,” in Cancer of the Skin, D. S. Rigel, R. J. Friedman, L. M. Dzubow, D. S. Reintgen, J.-C. Bystryn, and R. Marks, Eds., pp. 15–27, Elsevier, Philadelphia, Pa, USA, 2005.
View at: Google ScholarB. R. Smoller, “Squamous cell carcinoma: from precursor lesions to high-risk variants,” Modern Pathology, vol. 19, supplement 2, pp. S88–S92, 2006.
View at: Publisher Site | Google ScholarK. Y. Tsai and H. Tsao, “The genetics of skin cancer,” American Journal of Medical Genetics—Part C: Seminars in Medical Genetics, vol. 131 C, no. 1, pp. 82–92, 2004.
View at: Publisher Site | Google ScholarR. J. Akhurst and A. Balmain, “Genetic events and the role of TGF in epithelial tumour progression,” Journal of Pathology, vol. 187, no. 1, pp. 82–90, 1999.
View at: Publisher Site | Google ScholarW. Cui, D. J. Fowlis, S. Bryson et al., “TGF1 inhibits the formation of benign skin tumors, but enhances progression to invasive spindle carcinomas in transgenic mice,” Cell, vol. 86, no. 4, pp. 531–542, 1996.
View at: Publisher Site | Google ScholarG. Portella, S. A. Cumming, J. Liddell et al., “Transforming growth factor is essential for spindle cell conversion of mouse skin carcinoma in vivo: implications for tumor invasion,” Cell Growth and Differentiation, vol. 9, no. 5, pp. 393–404, 1998.
View at: Google ScholarR. Derynck, R. J. Akhurst, and A. Balmain, “TGF- signaling in tumor suppression and cancer progression,” Nature Genetics, vol. 29, no. 2, pp. 117–129, 2001.
View at: Publisher Site | Google ScholarC. Go, P. Li, and X.-J. Wang, “Blocking transforming growth factor signaling in transgenic epidermis accelerates chemical carcinogenesis: a mechanism associated with increased angiogenesis,” Cancer Research, vol. 59, no. 12, pp. 2861–2868, 1999.
View at: Google ScholarG. Han, S.-L. Lu, A. G. Li et al., “Distinct mechanisms of TGF-1-mediated epithelial-to-mesenchymal transition and metastasis during skin carcinogenesis,” Journal of Clinical Investigation, vol. 115, no. 7, pp. 1714–1723, 2005.
View at: Publisher Site | Google ScholarR. R. Allen and P. J. Higgins, “Plasminogen activator inhibitor type-1 expression and the pathophysiology of TGF-1-incuced epithelial-to-mesechymal transition,” Recent Research Developments in Physiology, vol. 2, pp. 355–366, 2004.
View at: Google ScholarO. Rho, L. M. Beltran, I. B. Gimenez-Conti, and J. DiGiovanni, “Altered expression of the epidermal growth factor receptor and transforming growth factor- during multistage skin carcinogenesis in SENCAR mice,” Molecular Carcinogenesis, vol. 11, no. 1, pp. 19–28, 1994.
View at: Google ScholarS. H. Yuspa, “The pathogenesis of squamous cell cancer: lessons learned from studies of skin carcinogenesis,” Journal of Dermatological Science, vol. 17, no. 1, pp. 1–7, 1998.
View at: Publisher Site | Google ScholarP. O-Charoenrat, P. H. Rhys-Evans, H. Modjtahedi, W. Court, G. Box, and S. Eccles, “Overexpression of epidermal growth factor receptor in human head and neck squamous carcinoma cell lines correlates with matrix metalloproteinase-9 expression and in vitro invasion,” International Journal of Cancer, vol. 86, no. 3, pp. 307–317, 2000.
View at: Publisher Site | Google ScholarP. O-charoenrat, P. H. Rhys-Evans, D. J. Archer, and S. A. Eccles, “C- receptors in squamous cell carcinomas of the head and neck: clinical significance and correlation with matrix metalloproteinases and vascular endothelial growth factors,” Oral Oncology, vol. 38, no. 1, pp. 73–80, 2002.
View at: Publisher Site | Google ScholarN. Moghal and P. W. Sternberg, “Multiple positive and negative regulators of signaling by the EGF-receptor,” Current Opinion in Cell Biology, vol. 11, no. 2, pp. 190–196, 1999.
View at: Publisher Site | Google ScholarJ. Zavadil and E. P. Böttinger, “TGF- and epithelial-to-mesenchymal transitions,” Oncogene, vol. 24, no. 37, pp. 5764–5774, 2005.
View at: Publisher Site | Google ScholarJ. Zavadil, M. Bitzer, D. Liang et al., “Genetic programs of epithelial cell plasticity directed by transforming growth factor-,” Proceedings of the National Academy of Sciences of the United States of America, vol. 98, no. 12, pp. 6686–6691, 2001.
View at: Publisher Site | Google ScholarT. A. Lehman, R. Modali, P. Boukamp et al., “p53 mutations in human immortalized epithelial cell lines,” Carcinogenesis, vol. 14, no. 5, pp. 833–839, 1993.
View at: Publisher Site | Google ScholarC. E. Wilkins-Port, J. Freytag, and P. J. Higgins, “TGF1/EGF modulate pericellular proteolysis by stimulating collagenolytic activity in pre-malignant human epidermal keratinocytes,” in Proceedings of the Epithelial Mesenchymal Transition (EMT) Conference, vol. 56, p. 31, Vancouver, British Columbia, Canada, October 2005.
View at: Google ScholarC. E. Wilkins-Port and P. J. Higgins, “Regulation of extracellular matrix remodeling following TGF1/EGF stimulated EMT in human pre-malignant keratinocytes,” to appear in Cells Tissues Organs.
View at: Google ScholarR. R. Isseroff and D. B. Rifkin, “Plasminogen is present in the basal layer of the epidermis,” Journal of Investigative Dermatology, vol. 80, no. 4, pp. 297–299, 1983.
View at: Publisher Site | Google ScholarH. R. Lijnen, “Matrix metalloproteinases and cellular fibrinolytic activity,” Biochemistry, vol. 67, no. 1, pp. 92–98, 2002.
View at: Google ScholarP. A. Andreasen, L. Kjøller, L. Christensen, and M. J. Duffy, “The urokinase-type plasminogen activator system in cancer metastasis: a review,” International Journal of Cancer, vol. 72, no. 1, pp. 1–22, 1997.
View at: Publisher Site | Google ScholarB. Hundsdorfer, H. F. Zeilhofer, K. P. Bock, P. Dettmar, M. Schmitt, and H. H. Horch, “The prognostic importance of urokinase type plasminogen activators (uPA) and plasminogen activator inhibitors (PAI-1) in primary resection of oral squamous cell carcinoma,” Mund Kiefer Grsichtschir, vol. 8, no. 3, pp. 173–179, 2004.
View at: Publisher Site | Google ScholarE. Bacharach, A. Itin, and E. Keshet, “Apposition-dependent induction of plasminogen activator inhibitor type 1 expression: a mechanism for balancing pericellular proteolysis during angiogenesis,” Blood, vol. 92, no. 3, pp. 939–945, 1998.
View at: Google ScholarK. Bajou, V. Masson, R. D. Gerard et al., “The plasminogen activator inhibitor PAI-1 controls in vivo tumor vascularization by interaction with proteases, not vitronectin: implications for antiangiogenic strategies,” Journal of Cell Biology, vol. 152, no. 4, pp. 777–784, 2001.
View at: Publisher Site | Google ScholarK. Bajou, A. Noël, R. D. Gerard et al., “Absence of host plasminogen activator inhibitor 1 prevents cancer invasion and vascularization,” Nature Medicine, vol. 4, no. 8, pp. 923–928, 1998.
View at: Publisher Site | Google ScholarY.-J. Chen, S.-C. Lin, T. Kao et al., “Genome-wide profiling of oral squamous cell carcinoma,” Journal of Pathology, vol. 204, no. 3, pp. 326–332, 2004.
View at: Publisher Site | Google ScholarP. Lindberg, A. Larsson, and B. S. Nielsen, “Expression of plasminogen activator inhibitor-1, urokinase receptor and laminin -2 chain is an early coordinated event in incipient oral squamous cell carcinoma,” International Journal of Cancer, vol. 118, no. 12, pp. 2948–2956, 2006.
View at: Publisher Site | Google ScholarE. Vairaktaris, C. Yapijakis, Z. Serefoglou et al., “Plasminogen activator inhibitor-1 polymorphism is associated with increased risk for oral cancer,” Oral Oncology, vol. 42, no. 9, pp. 888–892, 2006.
View at: Publisher Site | Google ScholarL. Christensen, A. C. Wiborg Simonsen, C. W. Heegaard, S. K. Moestrup, J. A. Andersen, and P. A. Andreasen, “Immunohistochemical localization of urokinase-type plasminogen activator, type-1 plasminogen-activator inhibitor, urokinase receptor and -macroglobulin receptor in human breast carcinomas,” International Journal of Cancer, vol. 66, no. 4, pp. 441–452, 1996.
View at: Publisher Site | Google ScholarM. Illemann, U. Hansen, H. J. Nielsen et al., “Leading-edge myofibroblasts in human colon cancer express plasminogen activator inhibitor-1,” American Journal of Clinical Pathology, vol. 122, no. 2, pp. 256–265, 2004.
View at: Publisher Site | Google ScholarB. V. Offersen, B. S. Nielsen, G. Høyer-Hansen et al., “The myofibroblast is the predominant plasminogen activator inhibitor-1-expressing cell type in human breast carcinomas,” American Journal of Pathology, vol. 163, no. 5, pp. 1887–1899, 2003.
View at: Google ScholarD. Chin, G. M. Boyle, P. G. Parsons, and W. B. Coman, “What is transforming growth factor-beta (TGF-)?” British Journal of Plastic Surgery, vol. 57, no. 3, pp. 215–221, 2004.
View at: Publisher Site | Google ScholarC. H. Streuli, C. Schmidhauser, M. Kobrin, M. J. Bissell, and R. Derynck, “Extracellular matrix regulates expression of the TGF-1 gene,” Journal of Cell Biology, vol. 120, no. 1, pp. 253–260, 1993.
View at: Publisher Site | Google ScholarT. M. Vollberg, M. D. George, and A. M. Jetten, “Induction of extracellular matrix gene expression in normal human keratinocytes by transforming growth factor is altered by cellular differentiation,” Experimental Cell Research, vol. 193, no. 1, pp. 93–100, 1991.
View at: Publisher Site | Google ScholarN. E. Wikner, J. T. Elder, K. A. Persichitte, P. Mink, and R. A. F. Clark, “Transforming growth factor- modulates plasminogen activator activity and plasminogen activator inhibitor type-1 expression in human keratinocytes in vitro,” Journal of Investigative Dermatology, vol. 95, no. 5, pp. 607–613, 1990.
View at: Publisher Site | Google ScholarK. Ahokas, J. Lohi, S. A. Illman et al., “Matrix metalloproteinase-21 is expressed epithelially during development and in cancer and is up-regulated by transforming growth factor-1 in Keratinocytes,” Laboratory Investigation, vol. 83, no. 12, pp. 1887–1899, 2003.
View at: Publisher Site | Google ScholarN. Johansson, J. Westermarck, S. Leppä et al., “Collagenase 3 (matrix metalloproteinase 13) gene expression by HaCaT keratinocytes is enhanced by tumor necrosis factor and transforming growth factor ,” Cell Growth and Differentiation, vol. 8, no. 2, pp. 243–250, 1997.
View at: Google ScholarE.-S. Kim, M.-S. Kim, and A. Moon, “TGF--induced upregulation of MMP-2 and MMP-9 depends on p38 MAPK, but not ERK signaling in MCF10A human breast epithelial cells,” International Journal of Oncology, vol. 25, no. 5, pp. 1375–1382, 2004.
View at: Google ScholarE.-S. Kim, M.-S. Kim, and A. Moon, “Transforming growth factor (TGF)- in conjunction with H-ras activation promotes malignant progression of MCF10A breast epithelial cells,” Cytokine, vol. 29, no. 2, pp. 84–91, 2005.
View at: Publisher Site | Google ScholarH.-S. Kim, T. Shang, Z. Chen, S. C. Pflugfelder, and D.-Q. Li, “TGF-1 stimulates production of gelatinase (MMP-9), collagenases (MMP-1, -13) and stromelysins (MMP-3, -10, -11) by human corneal epithelial cells,” Experimental Eye Research, vol. 79, no. 2, pp. 263–274, 2004.
View at: Publisher Site | Google ScholarM. Madlener, C. Mauch, W. Conca, M. Brauchle, W. C. Parks, and S. Werner, “Regulation of the expression of stromelysin-2 by growth factors in keratinocytes: implications for normal and impaired wound healing,” Biochemical Journal, vol. 320, no. 2, pp. 659–664, 1996.
View at: Google ScholarH. G. Munshi, Y. I. Wu, S. Mukhopadhyay et al., “Differential regulation of membrane type 1-matrix metalloproteinase activity by ERK 1/2- and p38 MAPK-modulated tissue inhibitor of metalloproteinases 2 expression controls transforming growth factor-1-induced pericellular collagenolysis,” Journal of Biological Chemistry, vol. 279, no. 37, pp. 39042–39050, 2004.
View at: Publisher Site | Google ScholarM. J. Newman, “Transforming growth factor beta and the cell surface in tumor progression,” Cancer and Metastasis Reviews, vol. 12, no. 3-4, pp. 239–254, 1993.
View at: Publisher Site | Google ScholarA. B. Roberts, B. K. McCune, and M. B. Sporn, “TGF-: regulation of extracellular matrix,” Kidney International, vol. 41, no. 3, pp. 557–559, 1992.
View at: Google ScholarA. B. Roberts and L. M. Wakefield, “The two faces of transforming growth factor in carcinogenesis,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 15, pp. 8621–8623, 2003.
View at: Publisher Site | Google ScholarJ. A. Wright, E. A. Turley, and A. H. Greenberg, “Transforming growth factor and fibroblast growth factor as promoters of tumor progression to malignancy,” Critical Reviews in Oncogenesis, vol. 4, no. 5, pp. 473–492, 1993.
View at: Google ScholarT. Sato, M. Iwai, T. Sakai et al., “Enhancement of membrane-type 1-matrix metalloproteinase (MT1-MMP) production and sequential activation of progelatinase A on human squamous carcinoma cells co-cultured with human dermal fibroblasts,” British Journal of Cancer, vol. 80, no. 8, pp. 1137–1143, 1999.
View at: Publisher Site | Google ScholarB. D. Sudbeck, P. Baumann, G. J. Ryan et al., “Selective loss of PMA-stimulated expression of matrix metalloproteinase 1 in HaCaT keratinocytes is correlated with the inability to induce mitogen-activated protein family kinases,” Biochemical Journal, vol. 339, no. 1, pp. 167–175, 1999.
View at: Publisher Site | Google ScholarL. L. Chen, R. Narayanan, M. S. Hibbs et al., “Altered epidermal growth factor signal transduction in activated Ha-ras- transformed human keratinocytes,” Biochemical and Biophysical Research Communications, vol. 193, no. 1, pp. 167–174, 1993.
View at: Publisher Site | Google ScholarP. O-charoenrat, P. H. Rhys-Evans, and S. A. Eccles, “Expression of matrix metalloproteinases and their inhibitors correlates with invasion and metastasis in squamous cell carcinoma of the head and neck,” Archives of Otolaryngology—Head & Neck Surgery, vol. 127, no. 7, pp. 813–820, 2001.
View at: Google ScholarL. J. Windsor, H. Grenett, B. Birkedal-Hansen, M. K. Bodden, J. A. Engler, and H. Birkedal-Hansen, “Cell type-specific regulation of SL-1 and SL-2 genes. Induction of the SL-2 gene but not the SL-1 gene by human keratinocytes in response to cytokines and phorbolesters,” Journal of Biological Chemistry, vol. 268, no. 23, pp. 17341–17347, 1993.
View at: Google ScholarS. Chakraborti, M. Mandal, S. Das, A. Mandal, and T. Chakraborti, “Regulation of matrix metalloproteinases: an overview,” Molecular and Cellular Biochemistry, vol. 253, no. 1-2, pp. 269–285, 2003.
View at: Publisher Site | Google ScholarN. H. Cho, K. P. Hong, S. H. Hong, S. Kang, K. Y. Chung, and S. H. Cho, “MMP expression profiling in recurred stage IB lung cancer,” Oncogene, vol. 23, no. 3, pp. 845–851, 2004.
View at: Publisher Site | Google ScholarJ. H. Gill, I. G. Kirwan, J. M. Seargent et al., “MMP-10 is overexpressed, proteolytically active, and a potential target for therapeutic intervention in human lung carcinomas,” Neoplasia, vol. 6, no. 6, pp. 777–785, 2004.
View at: Publisher Site | Google ScholarM. Krampert, W. Bloch, T. Sasaki et al., “Activities of the matrix metalloproteinase stromelysin-2 (MMP-10) in matrix degradation and keratinocyte organization in wounded skin,” Molecular Biology of the Cell, vol. 15, no. 12, pp. 5242–5254, 2004.
View at: Publisher Site | Google ScholarO. Rechardt, O. Elomaa, M. Vaalamo et al., “Stromelysin-2 is upregulated during normal wound repair and is induced by cytokines,” Journal of Investigative Dermatology, vol. 115, no. 5, pp. 778–787, 2000.
View at: Publisher Site | Google ScholarU. Impola, V. J. Uitto, J. Hietanen et al., “Differential expression of matrilysin-I (MMP-7), 92 kD gelatinase (MMP-9), and metalloelastase (MMP-12) in oral verrucous and squamous cell cancer,” Journal of Pathology, vol. 202, no. 1, pp. 14–22, 2004.
View at: Publisher Site | Google ScholarE. Kerkelä, R. Ala-aho, L. Jeskanen et al., “Differential patterns of stromelysin-2 (MMP-10) and MT1-MMP (MMP-14) expression in epithelial skin cancers,” British Journal of Cancer, vol. 84, no. 5, pp. 659–669, 2001.
View at: Publisher Site | Google ScholarR. Mathew, R. Khanna, R. Kumar, M. Mathur, N. K. Shukla, and R. Ralhan, “Stromelysin-2 overexpression in human esophageal squamous cell carcinoma: potential clinical implications,” Cancer Detection and Prevention, vol. 26, no. 3, pp. 222–228, 2002.
View at: Publisher Site | Google ScholarP. J. Higgins, “TGF-1-stimulated -ERK signaling regulates expression of the angiogenic SERPIN PAI-1,” Recent Research Developments in Biochemistry, vol. 7, pp. 31–45, 2006.
View at: Google ScholarS. M. Kutz, C. E. Higgins, R. Samarakoon et al., “TGF-1-induced PAI-1 expression is E box/USF-dependent and requires EGFR signaling,” Experimental Cell Research, vol. 312, no. 7, pp. 1093–1105, 2006.
View at: Publisher Site | Google ScholarR. Samarakoon, C. E. Higgins, S. P. Higgins, S. M. Kutz, and P. J. Higgins, “Plasminogen activator inhibitor type-1 gene expression and induced migration in TGF-1-stimulated smooth muscle cells is /MEK-dependent,” Journal of Cellular Physiology, vol. 204, no. 1, pp. 236–246, 2005.
View at: Publisher Site | Google ScholarP. P.-C. Hu, X. Shen, D. Huang, Y. Liu, C. Counter, and X.-F. Wang, “The MEK pathway is required for stimulation of p21(WAF1/CIP1) by transforming growth factor-,” Journal of Biological Chemistry, vol. 274, no. 50, pp. 35381–35387, 1999.
View at: Publisher Site | Google ScholarM. Sato, K. Kawai-Kowase, H. Sato et al., “c-Src and hydrogen peroxide mediate transforming growth factor-1-induced smooth muscle cell-gene expression in 10T1/2 cells,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 25, no. 2, pp. 341–347, 2005.
View at: Publisher Site | Google ScholarH. Sato, M. Sato, H. Kanai et al., “Mitochondrial reactive oxygen species and c-Src play a critical role in hypoxic response in vascular smooth muscle cells,” Cardiovascular Research, vol. 67, no. 4, pp. 714–722, 2005.
View at: Publisher Site | Google ScholarF. Viñals and J. Pouysségur, “Transforming growth factor 1 (TGF-1) promotes endothelial cell survival during in vitro angiogenesis via an autocrine mechanism implicating TGF- signaling,” Molecular and Cellular Biology, vol. 21, no. 21, pp. 7218–7230, 2001.
View at: Publisher Site | Google ScholarJ. Guerrero, J. F. Santibañez, A. González, and J. Martínez, “EGF receptor transactivation by urokinase receptor stimulus through a mechanism involving Src and matrix metalloproteinases,” Experimental Cell Research, vol. 292, no. 1, pp. 201–208, 2004.
View at: Publisher Site | Google ScholarY. Uchiyama-Tanaka, H. Matsubara, Y. Mori et al., “Involvement of HB-EGF and EGF receptor transactivation in TGF--mediated fibronectin expression in mesangial cells,” Kidney International, vol. 62, no. 3, pp. 799–808, 2002.
View at: Publisher Site | Google ScholarL. Moro, L. Dolce, S. Cabodi et al., “Integrin-induced epidermal growth factor (EGF) receptor activation requires c-Src and p130Cas and leads to phosphorylation of specific EGF receptor tyrosines,” Journal of Biological Chemistry, vol. 277, no. 11, pp. 9405–9414, 2002.
View at: Publisher Site | Google ScholarJ. S. Biscardi, M.-C. Maa, D. A. Tice, M. E. Cox, T.-H. Leu, and S. J. Parsons, “c-Src-mediated phosphorylation of the epidermal growth factor receptor on and is associated with modulation of receptor function,” Journal of Biological Chemistry, vol. 274, no. 12, pp. 8335–8343, 1999.
View at: Publisher Site | Google ScholarC. K. Miranti and J. S. Brugge, “Sensing the environment: a historical perspective on integrin signal transduction,” Nature Cell Biology, vol. 4, no. 4, pp. E83–E90, 2002.
View at: Publisher Site | Google ScholarA. Alavi, J. D. Hood, R. Frausto, D. G. Stupack, and D. A. Cheresh, “Role of Raf in vascular protection from distinct apoptotic stimuli,” Science, vol. 301, no. 5629, pp. 94–96, 2003.
View at: Publisher Site | Google ScholarF. Chang, L. S. Steelman, J. T. Lee et al., “Signal transduction mediated by the Ras/Raf/MEK/ERK pathway from cytokine receptors to transcription factors: potential targeting for therapeutic intervention,” Leukemia, vol. 17, no. 7, pp. 1263–1293, 2003.
View at: Publisher Site | Google ScholarA. Ziogas, K. Moelling, and G. Radziwill, “CNK1 is a scaffold protein that regulates Src-mediated Raf-1 activation,” Journal of Biological Chemistry, vol. 280, no. 25, pp. 24205–24211, 2005.
View at: Publisher Site | Google Scholar