References
- Alves, T.R., da Fonseca, A.C.C., Nunes, S.S., da Silva, A.O., Dubois, L.G.F., Faria, J., Kahn, S.A., Viana, N.B., Marcondes, J., Legrand, C., et al. (2011). Tenascin-C in the extracellular matrix promotes the selection of highly proliferative and tubulogenesis-defective endothelial cells. Exp. Cell Res. 317, 2073-2085. https://doi.org/10.1016/j.yexcr.2011.06.006
- Andrianarivo, A.G., Robinson, J.A., Mann, K.G., and Tracy, R.P. (1992). Growth on type I collagen promotes expression of the osteoblastic phenotype in human osteosarcoma MG-63 cells. J. Cell. Physiol. 153, 256-265. https://doi.org/10.1002/jcp.1041530205
- Bielack, S., Carrle, D., Casali, P.G., and Group, O.b.o.t.E.G.W. (2009). Osteosarcoma: ESMO Clinical Recommendations for diagnosis, treatment and follow-up. Ann. Oncol. 20, iv137-iv139. https://doi.org/10.1093/annonc/mdn526
- Chung, C.Y., and Erickson, H. (1994). Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C. J. Cell Biol. 126, 539-548. https://doi.org/10.1083/jcb.126.2.539
- Ehrlich, P., and Lanyon, L. (2002). Mechanical strain and bone cell function: a review. Osteoporosis Int. 13, 688-700. https://doi.org/10.1007/s001980200095
-
Feng, X., Zhang, Y., Xu, R., Xie, X., Tao, L., Gao, H., Gao, Y., He, Z., and Wang, H. (2010). Lipopolysaccharide up-regulates the expression of
$Fc{\alpha}/{\mu}$ receptor and promotes the binding of oxidized low-density lipoprotein and its IgM antibody complex to activated human macrophages. Atherosclerosis 208, 396-405. https://doi.org/10.1016/j.atherosclerosis.2009.07.035 - Gill, J., Ahluwalia, M.K., Geller, D., and Gorlick, R. (2012). New targets and approaches in osteosarcoma. Pharmacol. Ther. 137, 89-99.
- Hirata, E., Arakawa, Y., Shirahata, M., Yamaguchi, M., Kishi, Y., Okada, T., Takahashi, J.A., Matsuda, M., and Hashimoto, N. (2009). Endogenous tenascin-C enhances glioblastoma invasion with reactive change of surrounding brain tissue. Cancer Sci. 100, 1451-1459. https://doi.org/10.1111/j.1349-7006.2009.01189.x
- Jahkola, T., Toivonen, T., Virtanen, I., von Smitten, K., Nordling, S., von Boguslawski, K., Haglund, C., Nevanlinna, H., and Blomqvist, C. (1998). Tenascin-C expression in invasion border of early breast cancer: a predictor of local and distant recurrence. Br. J. Cancer 78, 1507. https://doi.org/10.1038/bjc.1998.714
- Jiang, L., Wei, X., Yi, D., Xu, P., Liu, H., Chang, Q., Yang, S., Li, Z., Gao, H., and Hao, G. (2008). Synergistic effects of cyclic strain and Th1-like cytokines on tenascin-C production by rheumatic aortic valve interstitial cells. Clin. Exp. Immunol. 155, 216-223.
- Leins, A., Riva, P., Lindstedt, R., Davidoff, M.S., Mehraein, P., and Weis, S. (2003). Expression of tenascin-C in various human brain tumors and its relevance for survival in patients with astrocytoma. Cancer 98, 2430-2439. https://doi.org/10.1002/cncr.11796
- Lelievre, S., Bisseil, M.J., and Pujuguet, P. (2000). Cell nucleus in context. Crit. Rev. Eukaryot. Gene Exp. 10, 30-37.
- Li, R., Maminishkis, A., Wang, F.E., and Miller, S.S. (2007). PDGFC and-D induced proliferation/migration of human RPE is abolished by inflammatory cytokines. Invest. Ophthalmol. Vis. Sci. 48, 5722-5732. https://doi.org/10.1167/iovs.07-0327
- Lv, Z., Yang, D., Li, J., Hu, M., Luo, M., Zhan, X., Song, P., Liu, C., Bai, H., and Li, B. (2013). Bone morphogenetic protein 9 overexpression reduces osteosarcoma cell migration and invasion. Mol. Cells 36, 119-126. https://doi.org/10.1007/s10059-013-0043-8
- Ma, X.M., and Blenis, J. (2009). Molecular mechanisms of mTOR-mediated translational control. Nat. Rev. Mol. Cell Biol. 10, 307-318. https://doi.org/10.1038/nrm2672
- Midwood, K.S., and Orend, G. (2009). The role of tenascin-C in tissue injury and tumorigenesis. J. Cell Commun. Signal. 3, 287-310. https://doi.org/10.1007/s12079-009-0075-1
- Midwood, K.S., Hussenet, T., Langlois, B., and Orend, G. (2011). Advances in tenascin-C biology. Cell. Mol. Life Sci. 68, 3175-3199. https://doi.org/10.1007/s00018-011-0783-6
- Murphy-Ullrich, J.E. (2001). The de-adhesive activity of matricellular proteins: is intermediate cell adhesion an adaptive state? J. Clin. Invest. 107, 785-790. https://doi.org/10.1172/JCI12609
- Oh, W.J., and Jacinto, E. (2011). mTOR complex 2 signaling and functions. Cell Cycle 10, 2305-2316. https://doi.org/10.4161/cc.10.14.16586
- Osborne, T., and Khanna, C. (2012). A review of the association between osteosarcoma metastasis and protein translation. J. Comp. Pathol. 146, 132-142. https://doi.org/10.1016/j.jcpa.2011.12.007
- Pazzaglia, L., Conti, A., Chiechi, A., Novello, C., Magagnoli, G., Astolfi, A., Pession, A., Krenacs, T., Alberghini, M., and Picci, P. (2010). Differential gene expression in classic giant cell tumours of bone: tenascin C as biological risk factor for local relapses and metastases. Histopathology 57, 59-72. https://doi.org/10.1111/j.1365-2559.2010.03597.x
- Ramos, D.M., Chen, B., Regezi, J., Zardi, L., and Pytela, R. (1998). Tenascin-C matrix assembly in oral squamous cell carcinoma. Int. J. Cancer 75, 680-687. https://doi.org/10.1002/(SICI)1097-0215(19980302)75:5<680::AID-IJC4>3.0.CO;2-V
- Rhee, S.H., Han, I., Lee, M.R., Cho, H.S., Oh, J.H., and Kim, H.S. (2013). Role of integrin-linked kinase in osteosarcoma progression. J. Orthopaedic. Res. 31, 1668-1675. https://doi.org/10.1002/jor.22409
- Sage, E., and Bornstein, P. (1991). Extracellular proteins that modulate cell-matrix interactions. SPARC, tenascin, and thrombospondin. J. Biol. Chem. 266, 14831-14834.
-
Saito, Y., Imazeki, H., Miura, S., Yoshimura, T., Okutsu, H., Harada, Y., Ohwaki, T., Nagao, O., Kamiya, S., and Hayashi, R. (2007). A peptide derived from tenascin-C induces
${\beta}1$ integrin activation through syndecan-4. J. Biol. Chem. 282, 34929-34937. https://doi.org/10.1074/jbc.M705608200 - Shimoyama, T., Hiraoka, S., Takemoto, M., Koshizaka, M., Tokuyama, H., Tokuyama, T., Watanabe, A., Fujimoto, M., Kawamura, H., and Sato, S. (2010). CCN3 inhibits neointimal hyperplasia through modulation of smooth muscle cell growth and migration. Arterioscler. Thromb. Vasc. Biol. 30, 675-682. https://doi.org/10.1161/ATVBAHA.110.203356
- Si, Y., Wang, J., Guan, J., Han, Q., and Hui, Y. (2013). Plateletderived growth factor induced alpha-smooth muscle actin expression by human retinal pigment epithelium cell. J. Ocul. Pharmacol. Ther. 29, 310-318. https://doi.org/10.1089/jop.2012.0137
-
Skelly, D.T., Hennessy, E., Dansereau, M.-A., and Cunningham, C. (2013). A systematic analysis of the peripheral and CNS effects of systemic LPS, IL-1B, TNF-
${\alpha}$ and IL-6 challenges in C57BL/6 mice. PLoS One 8, e69123. https://doi.org/10.1371/journal.pone.0069123 - Tamaoki, M., Imanaka-Yoshida, K., Yokoyama, K., Nishioka, T., Inada, H., Hiroe, M., Sakakura, T., and Yoshida, T. (2005). Tenascin-C regulates recruitment of myofibroblasts during tissue repair after myocardial injury. Am. J. Pathol. 167, 71-80. https://doi.org/10.1016/S0002-9440(10)62954-9
- Tucker, R., Drabikowski, K., Hess, J., Ferralli, J., Chiquet-Ehrismann, R., and Adams, J. (2006). Phylogenetic analysis of the tenascin gene family: evidence of origin early in the chordate lineage. BMC Evol. Biol. 6, 60. https://doi.org/10.1186/1471-2148-6-60
- Tucker, R.P., and Chiquet-Ehrismann, R. (2009). The regulation of tenascin expression by tissue microenvironments. Biochim. Biophys. Acta 1793, 888-892. https://doi.org/10.1016/j.bbamcr.2008.12.012
- Wachtel, M., and Schafer, B.W. (2010). Targets for cancer therapy in childhood sarcomas. Cancer Treat. Rev. 36, 318-327. https://doi.org/10.1016/j.ctrv.2010.02.007
- Wang, Y., Man, Y., Ding, Y., Ma, B., Qiu, X., Fan, Q., Zheng, L. (2006). Mechanical strain and growth factors regulate expression of tenascin-C by OS cells additively. Oncol. Res. 20, 509-516.
- Wang, Y., Zheng, L., Ma, B., Zhou, Y., and Fan, Q. (2010). Generation and identification of monoclonal antibodies against FNIII domain D of human tenascin-C. Hybridoma (Larchmt) 29, 13-16. https://doi.org/10.1089/hyb.2009.0059
- Wu, G., Wang, J., Zhou, Z., Li, T., and Tang, F. (2013). Combined staining for immunohistochemical markers in the diagnosis of papillary thyroid carcinoma: Improvement in the sensitivity or specificity? J. Int. Med. Res. 41, 975-983. https://doi.org/10.1177/0300060513490617
- Wullschleger, S., Loewith, R., and Hall, M.N. (2006). TOR signaling in growth and metabolism. Cell 124, 471-484. https://doi.org/10.1016/j.cell.2006.01.016
- Yuan, T., and Cantley, L. (2008). PI3K pathway alterations in cancer: variations on a theme. Oncogene 27, 5497-5510. https://doi.org/10.1038/onc.2008.245
- Zhang, Y., and Zheng, X.S. (2012). mTOR-independent 4E-BP1 phosphorylation is associated with cancer resistance to mTOR kinase inhibitors. Cell Cycle 11, 594-603. https://doi.org/10.4161/cc.11.3.19096
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