4,269
Views
124
CrossRef citations to date
0
Altmetric
Reviews

Tenascin C in metastasis: A view from the invasive front

&
Pages 112-124 | Received 12 Sep 2014, Accepted 09 Jan 2015, Published online: 20 Mar 2015

References

  • Gupta GP, Massague J. Cancer metastasis: building a framework. Cell 2006; 127:679-95; PMID:17110329; http://dx.doi.org/10.1016/j.cell.2006.11.001
  • Vanharanta S, Massague J. Origins of metastatic traits. Cancer cell 2013; 24:410-21; PMID:24135279; http://dx.doi.org/10.1016/j.ccr.2013.09.007
  • Joyce JA, Pollard JW. Microenvironmental regulation of metastasis. Nat Rev Cancer 2009; 9:239-52; PMID:19279573; http://dx.doi.org/10.1038/nrc2618
  • Bissell MJ, Hines WC. Why don't we get more cancer? A proposed role of the microenvironment in restraining cancer progression. Nat Med 2011; 17:320-9; PMID:21383745; http://dx.doi.org/10.1038/nm.2328
  • Oskarsson T, Batlle E, Massague J. Metastatic stem cells: sources, niches, and vital pathways. Cell Stem Cell 2014; 14:306-21; PMID:24607405; http://dx.doi.org/10.1016/j.stem.2014.02.002
  • Hynes RO. The extracellular matrix: not just pretty fibrils. Science 2009; 326:1216-9; PMID:19965464; http://dx.doi.org/10.1126/science.1176009
  • Lu P, Takai K, Weaver VM, Werb Z. Extracellular matrix degradation and remodeling in development and disease. Cold Spring Harb Perspect Biol 2011; 3:1-24; PMID:21917992.
  • Bourdon MA, Wikstrand CJ, Furthmayr H, Matthews TJ, Bigner DD. Human glioma-mesenchymal extracellular matrix antigen defined by monoclonal antibody. Cancer Res 1983; 43:2796-805; PMID:6342760
  • Chiquet M, Fambrough DM. Chick myotendinous antigen. II. A novel extracellular glycoprotein complex consisting of large disulfide-linked subunits. J Cell Biol 1984; 98:1937-46; PMID:6202699; http://dx.doi.org/10.1083/jcb.98.6.1937
  • Jones FS, Jones PL. The tenascin family of ECM glycoproteins: structure, function, and regulation during embryonic development and tissue remodeling. Dev Dyn 2000; 218:235-59; PMID:10842355; http://dx.doi.org/10.1002/(SICI)1097-0177(200006)218:2%3c235::AID-DVDY2%3e3.0.CO;2-G
  • Hancox RA, Allen MD, Holliday DL, Edwards DR, Pennington CJ, Guttery DS, Shaw JA, Walker RA, Pringle JH, Jones JL. Tumour-associated tenascin-C isoforms promote breast cancer cell invasion and growth by matrix metalloproteinase-dependent and independent mechanisms. Breast Cancer Res 2009; 11:R24; PMID:19405959; http://dx.doi.org/10.1186/bcr2251
  • Chiquet-Ehrismann R, Mackie EJ, Pearson CA, Sakakura T. Tenascin: an extracellular matrix protein involved in tissue interactions during fetal development and oncogenesis. Cell 1986; 47:131-9; PMID:2428505; http://dx.doi.org/10.1016/0092-8674(86)90374-0
  • Tucker RP, Chiquet-Ehrismann R. The regulation of tenascin expression by tissue microenvironments. Biochim Biophys Acta 2009; 1793:888-92; PMID:19162090; http://dx.doi.org/10.1016/j.bbamcr.2008.12.012
  • Chiquet-Ehrismann R, Orend G, Chiquet M, Tucker RP, Midwood KS. Tenascins in stem cell niches. Matrix Biol 2014; 37:112-23.
  • Midwood KS, Orend G. The role of tenascin-C in tissue injury and tumorigenesis. J Cell Commun Signal 2009; 3:287-310; PMID:19838819; http://dx.doi.org/10.1007/s12079-009-0075-1
  • Jones PL, Boudreau N, Myers CA, Erickson HP, Bissell MJ. Tenascin-C inhibits extracellular matrix-dependent gene expression in mammary epithelial cells. Localization of active regions using recombinant tenascin fragments. J Cell Sci 1995; 108 (Pt 2):519-27; PMID:7539436
  • McDaniel SM, Rumer KK, Biroc SL, Metz RP, Singh M, Porter W, Schedin P. Remodeling of the mammary microenvironment after lactation promotes breast tumor cell metastasis. Am J Pathol 2006; 168:608-20; PMID:16436674; http://dx.doi.org/10.2353/ajpath.2006.050677
  • Schedin P. Pregnancy-associated breast cancer and metastasis. Nat Rev Cancer 2006; 6:281-91; PMID:16557280; http://dx.doi.org/10.1038/nrc1839
  • Maseruka H, Bonshek RE, Tullo AB. Tenascin-C expression in normal, inflamed, and scarred human corneas. Br J Ophthalmol 1997; 81:677-82; PMID:9349157; http://dx.doi.org/10.1136/bjo.81.8.677
  • Orend G, Chiquet-Ehrismann R. Tenascin-C induced signaling in cancer. Cancer Lett 2006; 244:143-63; PMID:16632194; http://dx.doi.org/10.1016/j.canlet.2006.02.017
  • Midwood KS, Hussenet T, Langlois B, Orend G. Advances in tenascin-C biology. Cell Mol Life Sci 2011; 68:3175-99; PMID:21818551; http://dx.doi.org/10.1007/s00018-011-0783-6
  • Jemal A, Bray F, Center MM, Ferlay J, Ward E, Forman D. Global cancer statistics. CA Cancer J Clin 2011; 61:69-90; PMID:21296855
  • Weigelt B, Peterse JL, van 't Veer LJ. Breast cancer metastasis: markers and models. Nat Rev Cancer 2005; 5:591-602; PMID:16056258; http://dx.doi.org/10.1038/nrc1670
  • Mackie EJ, Chiquet-Ehrismann R, Pearson CA, Inaguma Y, Taya K, Kawarada Y, Sakakura T. Tenascin is a stromal marker for epithelial malignancy in the mammary gland. Proc Natl Acad Sci U S A 1987; 84:4621-5; PMID:2440026; http://dx.doi.org/10.1073/pnas.84.13.4621
  • Minn AJ, Gupta GP, Siegel PM, Bos PD, Shu W, Giri DD, Viale A, Olshen AB, Gerald WL, Massagué J. Genes that mediate breast cancer metastasis to lung. Nature 2005; 436:518-24; PMID:16049480; http://dx.doi.org/10.1038/nature03799
  • Tavazoie SF, Alarcon C, Oskarsson T, Padua D, Wang Q, Bos PD, Gerald WL, Massagué J. Endogenous human microRNAs that suppress breast cancer metastasis. Nature 2008; 451:147-52; PMID:18185580; http://dx.doi.org/10.1038/nature06487
  • Gurbuz I, Ferralli J, Roloff T, Chiquet-Ehrismann R, Asparuhova MB. SAP domain-dependent Mkl1 signaling stimulates proliferation and cell migration by induction of a distinct gene set indicative of poor prognosis in breast cancer patients. Mol Cancer 2014; 13:22; PMID:24495796; http://dx.doi.org/10.1186/1476-4598-13-22
  • Ioachim E, Charchanti A, Briasoulis E, Karavasilis V, Tsanou H, Arvanitis DL, Agnantis NJ, Pavlidis N. Immunohistochemical expression of extracellular matrix components tenascin, fibronectin, collagen type IV and laminin in breast cancer: their prognostic value and role in tumour invasion and progression. Eur J Cancer 2002; 38:2362-70; PMID:12460779; http://dx.doi.org/10.1016/S0959-8049(02)00210-1
  • Dandachi N, Hauser-Kronberger C, More E, Wiesener B, Hacker GW, Dietze O, Wirl G. Co-expression of tenascin-C and vimentin in human breast cancer cells indicates phenotypic transdifferentiation during tumour progression: correlation with histopathological parameters, hormone receptors, and oncoproteins. J Pathol 2001; 193:181-9; PMID:11180164; http://dx.doi.org/10.1002/1096-9896(2000)9999:9999%3c::AID-PATH752%3e3.0.CO;2-V
  • Ferguson JE, Schor AM, Howell A, Ferguson MW. Tenascin distribution in the normal human breast is altered during the menstrual cycle and in carcinoma. Differentiation 1990; 42:199-207; PMID:1692795; http://dx.doi.org/10.1111/j.1432-0436.1990.tb00762.x
  • Shoji T, Kamiya T, Tsubura A, Hatano T, Sakakura T, Yamamoto M, Morii S. Immunohistochemical staining patterns of tenascin in invasive breast carcinomas. Virchows Archiv A Pathol Anat Histopathol 1992; 421:53-6; PMID:1378984; http://dx.doi.org/10.1007/BF01607139
  • Goepel C, Buchmann J, Schultka R, Koelbl H. Tenascin-A marker for the malignant potential of preinvasive breast cancers. Gynecol Oncol 2000; 79:372-8; PMID:11104607; http://dx.doi.org/10.1006/gyno.2000.5978
  • Jahkola T, Toivonen T, Nordling S, von Smitten K, Virtanen I. Expression of tenascin-C in intraductal carcinoma of human breast: relationship to invasion. Eur J Cancer 1998; 34:1687-92; PMID:9893653; http://dx.doi.org/10.1016/S0959-8049(98)00215-9
  • Jahkola T, Toivonen T, Virtanen I, von Smitten K, Nordling S, von Boguslawski K, Haglund C, Nevanlinna H, Blomqvist C. Tenascin-C expression in invasion border of early breast cancer: a predictor of local and distant recurrence. Br J Cancer 1998; 78:1507-13; PMID:9836485; http://dx.doi.org/10.1038/bjc.1998.714
  • Ishihara A, Yoshida T, Tamaki H, Sakakura T. Tenascin expression in cancer cells and stroma of human breast cancer and its prognostic significance. Clin Cancer Res 1995; 1:1035-41; PMID:9816077
  • Oskarsson T, Acharyya S, Zhang XH, Vanharanta S, Tavazoie SF, Morris PG, Downey RJ, Manova-Todorova K, Brogi E, Massagué J. Breast cancer cells produce tenascin C as a metastatic niche component to colonize the lungs. Nat Med 2011; 17:867-74; PMID:21706029; http://dx.doi.org/10.1038/nm.2379
  • Suwiwat S, Ricciardelli C, Tammi R, Tammi M, Auvinen P, Kosma VM, LeBaron RG, Raymond WA, Tilley WD, Horsfall DJ. Expression of extracellular matrix components versican, chondroitin sulfate, tenascin, and hyaluronan, and their association with disease outcome in node-negative breast cancer. Clin Cancer Res 2004; 10:2491-8; PMID:15073129; http://dx.doi.org/10.1158/1078-0432.CCR-03-0146
  • Keith RL, Miller YE. Lung cancer chemoprevention: current status and future prospects. Nat Rev Clin Oncol 2013; 10:334-43; PMID:23689750; http://dx.doi.org/10.1038/nrclinonc.2013.64
  • Silacci M, Brack SS, Spath N, Buck A, Hillinger S, Arni S, Weder W, Zardi L, Neri D. Human monoclonal antibodies to domain C of tenascin-C selectively target solid tumors in vivo. Protein Eng Des Sel 2006; 19:471-8; http://dx.doi.org/10.1093/protein/gzl033
  • Pedretti M, Soltermann A, Arni S, Weder W, Neri D, Hillinger S. Comparative immunohistochemistry of L19 and F16 in non-small cell lung cancer and mesothelioma: two human antibodies investigated in clinical trials in patients with cancer. Lung Cancer 2009; 64:28-33; PMID:18799229; http://dx.doi.org/10.1016/j.lungcan.2008.07.013
  • Parekh K, Ramachandran S, Cooper J, Bigner D, Patterson A, Mohanakumar T. Tenascin-C, over expressed in lung cancer down regulates effector functions of tumor infiltrating lymphocytes. Lung Cancer 2005; 47:17-29; PMID:15603851; http://dx.doi.org/10.1016/j.lungcan.2004.05.016
  • Kang H, Kiess A, Chung CH. Emerging biomarkers in head and neck cancer in the era of genomics. Nat Rev Clin Oncol 2014; 12:11-26; PMID:25403939.
  • Raitz R, Martins MD, Araujo VC. A study of the extracellular matrix in salivary gland tumors. J Oral Pathol Med 2003; 32:290-6; http://dx.doi.org/10.1034/j.1600-0714.2003.00019.x
  • Wang Z, Han B, Zhang Z, Pan J, Xia H. Expression of angiopoietin-like 4 and tenascin C but not cathepsin C mRNA predicts prognosis of oral tongue squamous cell carcinoma. Biomarkers 2010; 15:39-46; PMID:19775228; http://dx.doi.org/10.3109/13547500903261362
  • Juhasz A, Bardos H, Repassy G, Adany R. Characteristic distribution patterns of tenascin in laryngeal and hypopharyngeal cancers. Laryngoscope 2000; 110:84-92; PMID:10646721; http://dx.doi.org/10.1097/00005537-200001000-00016
  • Eggermont AM, Spatz A, Robert C. Cutaneous melanoma. Lancet 2014; 383:816-27; PMID:24054424; http://dx.doi.org/10.1016/S0140-6736(13)60802-8
  • Natali PG, Nicotra MR, Bartolazzi A, Mottolese M, Coscia N, Bigotti A, Zardi L. Expression and production of tenascin in benign and malignant lesions of melanocyte lineage. Int J Cancer 1990; 46:586-90; PMID:1698727; http://dx.doi.org/10.1002/ijc.2910460406
  • Tuominen H, Kallioinen M. Increased tenascin expression in melanocytic tumors. J Cutan Pathol 1994; 21:424-9; PMID:7532653; http://dx.doi.org/10.1111/j.1600-0560.1994.tb00284.x
  • Sis B, Sagol O, Kupelioglu A, Sokmen S, Terzi C, Fuzun M, Ozer E, Bishop P. Prognostic significance of matrix metalloproteinase-2, cathepsin D, and tenascin-C expression in colorectal carcinoma. Pathol Res Pract 2004; 200:379-87; PMID:15239346; http://dx.doi.org/10.1016/j.prp.2004.02.012
  • Emoto K, Yamada Y, Sawada H, Fujimoto H, Ueno M, Takayama T, Kamada K, Naito A, Hirao S, Nakajima Y. Annexin II overexpression correlates with stromal tenascin-C overexpression: a prognostic marker in colorectal carcinoma. Cancer 2001; 92:1419-26; PMID:11745218; http://dx.doi.org/10.1002/1097-0142(20010915)92:6%3c1419::AID-CNCR1465%3e3.0.CO;2-J
  • Dueck M, Riedl S, Hinz U, Tandara A, Moller P, Herfarth C, Faissner A. Detection of tenascin-C isoforms in colorectal mucosa, ulcerative colitis, carcinomas and liver metastases. Int J Cancer 1999; 82:477-83; PMID:10404058; http://dx.doi.org/10.1002/(SICI)1097-0215(19990812)82:4%3c477::AID-IJC2%3e3.0.CO;2-5
  • Galler K, Junker K, Franz M, Hentschel J, Richter P, Gajda M, Göhlert A, von Eggeling F, Heller R, Giavazzi R, et al. Differential vascular expression and regulation of oncofetal tenascin-C and fibronectin variants in renal cell carcinoma (RCC): implications for an individualized angiogenesis-related targeted drug delivery. Histochem Cell Biol 2012; 137:195-204; PMID:22075565; http://dx.doi.org/10.1007/s00418-011-0886-z
  • Schwager K, Villa A, Rosli C, Neri D, Rosli-Khabas M, Moser G. A comparative immunofluorescence analysis of three clinical-stage antibodies in head and neck cancer. Head Neck Oncol 2011; 3:25; PMID:21548989; http://dx.doi.org/10.1186/1758-3284-3-25
  • Mighell AJ, Thompson J, Hume WJ, Markham AF, Robinson PA. Human tenascin-C: identification of a novel type III repeat in oral cancer and of novel splice variants in normal, malignant and reactive oral mucosae. Int J Cancer 1997; 72:236-40; PMID:9219826; http://dx.doi.org/10.1002/(SICI)1097-0215(19970717)72:2%3c236::AID-IJC6%3e3.0.CO;2-S
  • Derr LB, Chiquet-Ehrismann R, Gandour-Edwards R, Spence J, Tucker RP. The expression of tenascin-C with the AD1 variable repeat in embryonic tissues, cell lines and tumors in various vertebrate species. Differentiation 1997; 62:71-82; PMID:9404002; http://dx.doi.org/10.1046/j.1432-0436.1997.6220071.x
  • Frey K, Fiechter M, Schwager K, Belloni B, Barysch MJ, Neri D, Dummer R. Different patterns of fibronectin and tenascin-C splice variants expression in primary and metastatic melanoma lesions. Exp Dermatol 2011; 20:685-8; PMID:21649738; http://dx.doi.org/10.1111/j.1600-0625.2011.01314.x
  • Berndt A, Anger K, Richter P, Borsi L, Brack S, Silacci M, Franz M, Wunderlich H, Gajda M, Zardi L, et al. Differential expression of tenascin-C splicing domains in urothelial carcinomas of the urinary bladder. J Cancer Res Clin Oncol 2006; 132:537-46; PMID:16788848; http://dx.doi.org/10.1007/s00432-006-0106-8
  • Richter P, Tost M, Franz M, Altendorf-Hofmann A, Junker K, Borsi L, Neri D, Kosmehl H, Wunderlich H, Berndt A. B and C domain containing tenascin-C: urinary markers for invasiveness of urothelial carcinoma of the urinary bladder? J Cancer Res Clin Oncol 2009; 135:1351-8; PMID:19326143; http://dx.doi.org/10.1007/s00432-009-0576-6
  • Wilson KE, Langdon SP, Lessells AM, Miller WR. Expression of the extracellular matrix protein tenascin in malignant and benign ovarian tumours. Br J Cancer 1996; 74:999-1004; PMID:8855965; http://dx.doi.org/10.1038/bjc.1996.480
  • Adams M, Jones JL, Walker RA, Pringle JH, Bell SC. Changes in tenascin-C isoform expression in invasive and preinvasive breast disease. Cancer Res 2002; 62:3289-97; PMID:12036947
  • Guttery DS, Hancox RA, Mulligan KT, Hughes S, Lambe SM, Pringle JH, Walker RA, Jones JL, Shaw JA. Association of invasion-promoting tenascin-C additional domains with breast cancers in young women. Breast Cancer Res 2010; 12:R57; PMID:20678196
  • Moritz S, Lehmann S, Faissner A, von Holst A. An induction gene trap screen in neural stem cells reveals an instructive function of the niche and identifies the splicing regulator sam68 as a tenascin-C-regulated target gene. Stem Cells 2008; 26:2321-31; PMID:18617690; http://dx.doi.org/10.1634/stemcells.2007-1095
  • Jensen MA, Wilkinson JE, Krainer AR. Splicing factor SRSF6 promotes hyperplasia of sensitized skin. Nat Struct Mol Biol 2014; 21:189-97; PMID:24440982; http://dx.doi.org/10.1038/nsmb.2756
  • Borsi L, Balza E, Castellani P, Carnemolla B, Ponassi M, Querze G, Zardi L. Cell-cycle dependent alternative splicing of the tenascin primary transcript. Cell Adhes Commun 1994; 1:307-17; PMID:7521758; http://dx.doi.org/10.3109/15419069409097262
  • Borsi L, Balza E, Gaggero B, Allemanni G, Zardi L. The alternative splicing pattern of the tenascin-C pre-mRNA is controlled by the extracellular pH. J Biol Chem 1995; 270:6243-5; PMID:7534307; http://dx.doi.org/10.1074/jbc.270.11.6243
  • Latijnhouwers MA, de Jongh GJ, Bergers M, de Rooij MJ, Schalkwijk J. Expression of tenascin-C splice variants by human skin cells. Arch Dermatol Res 2000; 292:446-54; PMID:11000288; http://dx.doi.org/10.1007/s004030000152
  • Zhao Y, Young SL. TGF-β regulates expression of tenascin alternative-splicing isoforms in fetal rat lung. Am J Physiol 1995; 268:L173-80; PMID:7532367
  • von Holst A, Egbers U, Prochiantz A, Faissner A. Neural stem/progenitor cells express 20 tenascin C isoforms that are differentially regulated by Pax6. J Biol Chem 2007; 282:9172-81; PMID:17264084; http://dx.doi.org/10.1074/jbc.M608067200
  • Imai K, Kusakabe M, Sakakura T, Nakanishi I, Okada Y. Susceptibility of tenascin to degradation by matrix metalloproteinases and serine proteinases. FEBS Lett 1994; 352:216-8; PMID:7523186; http://dx.doi.org/10.1016/0014-5793(94)00960-0
  • Siri A, Knauper V, Veirana N, Caocci F, Murphy G, Zardi L. Different susceptibility of small and large human tenascin-C isoforms to degradation by matrix metalloproteinases. J Biol Chem 1995; 270:8650-4; PMID:7536739; http://dx.doi.org/10.1074/jbc.270.15.8650
  • Bell SC, Pringle JH, Taylor DJ, Malak TM. Alternatively spliced tenascin-C mRNA isoforms in human fetal membranes. Mol Hum Reprod 1999; 5:1066-76; PMID:10541570; http://dx.doi.org/10.1093/molehr/5.11.1066
  • Tanaka R, Seki Y, Saito Y, Kamiya S, Fujita M, Okutsu H, Iyoda T, Takai T, Owaki T, Yajima H, et al. Tenascin-C-derived Peptide TNIIIA2 Highly Enhances Cell Survival and Platelet-derived Growth Factor (PDGF)-dependent Cell Proliferation through Potentiated and Sustained Activation of Integrin alpha5beta1. J Biol Chem 2014; 289:17699-708; PMID:24808173; http://dx.doi.org/10.1074/jbc.M113.546622
  • Kusagawa H, Onoda K, Namikawa S, Yada I, Okada A, Yoshida T, Sakakura T. Expression and degeneration of tenascin-C in human lung cancers. Br J Cancer 1998; 77:98-102; PMID:9459152; http://dx.doi.org/10.1038/bjc.1998.15
  • Cai M, Onoda K, Takao M, Kyoko IY, Shimpo H, Yoshida T, Yada I. Degradation of tenascin-C and activity of matrix metalloproteinase-2 are associated with tumor recurrence in early stage non-small cell lung cancer. Clin Cancer Res 2002; 8:1152-6; PMID:11948127
  • Jahkola T, Toivonen T, von Smitten K, Blomqvist C, Virtanen I. Expression of tenascin in invasion border of early breast cancer correlates with higher risk of distant metastasis. Int J Cancer 1996; 69:445-7; PMID:8980244; http://dx.doi.org/10.1002/(SICI)1097-0215(19961220)69:6%3c445::AID-IJC4%3e3.0.CO;2-4
  • Ilmonen S, Jahkola T, Turunen JP, Muhonen T, Asko-Seljavaara S. Tenascin-C in primary malignant melanoma of the skin. Histopathology 2004; 45:405-11; PMID:15469480; http://dx.doi.org/10.1111/j.1365-2559.2004.01976.x
  • Kaarteenaho-Wiik R, Soini Y, Pollanen R, Paakko P, Kinnula VL. Overexpression of tenascin-C in malignant pleural mesothelioma. Histopathology 2003; 42:280-91; PMID:12605648; http://dx.doi.org/10.1046/j.1365-2559.2003.01568.x
  • Aishima S, Taguchi K, Terashi T, Matsuura S, Shimada M, Tsuneyoshi M. Tenascin expression at the invasive front is associated with poor prognosis in intrahepatic cholangiocarcinoma. Mod Pathol 2003; 16:1019-27; PMID:14559985; http://dx.doi.org/10.1097/01.MP.0000086860.65672.73
  • Chiquet-Ehrismann R, Kalla P, Pearson CA. Participation of tenascin and transforming growth factor-β in reciprocal epithelial-mesenchymal interactions of MCF7 cells and fibroblasts. Cancer Res 1989; 49:4322-5; PMID:2472877
  • Seaman S, Stevens J, Yang MY, Logsdon D, Graff-Cherry C, St Croix B. Genes that distinguish physiological and pathological angiogenesis. Cancer cell 2007; 11:539-54; PMID:17560335; http://dx.doi.org/10.1016/j.ccr.2007.04.017
  • Chiquet M, Gelman L, Lutz R, Maier S. From mechanotransduction to extracellular matrix gene expression in fibroblasts. Biochim Biophys Acta 2009; 1793:911-20; PMID:19339214; http://dx.doi.org/10.1016/j.bbamcr.2009.01.012
  • Yoshida T, Matsumoto E, Hanamura N, Kalembeyi I, Katsuta K, Ishihara A, Sakakura T. Co-expression of tenascin and fibronectin in epithelial and stromal cells of benign lesions and ductal carcinomas in the human breast. J Pathol 1997; 182:421-8; PMID:9306963; http://dx.doi.org/10.1002/(SICI)1096-9896(199708)182:4%3c421::AID-PATH886%3e3.0.CO;2-U
  • Hanamura N, Yoshida T, Matsumoto E, Kawarada Y, Sakakura T. Expression of fibronectin and tenascin-C mRNA by myofibroblasts, vascular cells and epithelial cells in human colon adenomas and carcinomas. Int J Cancer 1997; 73:10-5; PMID:9334802; http://dx.doi.org/10.1002/(SICI)1097-0215(19970926)73:1%3c10::AID-IJC2%3e3.0.CO;2-4
  • Hindermann W, Berndt A, Borsi L, Luo X, Hyckel P, Katenkamp D, Kosmehl H. Synthesis and protein distribution of the unspliced large tenascin-C isoform in oral squamous cell carcinoma. J Pathol 1999; 189:475-80; PMID:10629546; http://dx.doi.org/10.1002/(SICI)1096-9896(199912)189:4%3c475::AID-PATH462%3e3.0.CO;2-V
  • Mori M, Muramatsu Y, Yamada K, Shrestha P, Takai Y. Intracellular localization of tenascin in squamous cell carcinoma of oral cavity: an immunohistochemical study. Anticancer Res 1996; 16:3075-9; PMID:8920770
  • Kawakatsu H, Shiurba R, Obara M, Hiraiwa H, Kusakabe M, Sakakura T. Human carcinoma cells synthesize and secrete tenascin in vitro. Jpn J Cancer Res 1992; 83:1073-80; PMID:1280634; http://dx.doi.org/10.1111/j.1349-7006.1992.tb02724.x
  • Herlyn M, Graeven U, Speicher D, Sela BA, Bennicelli JL, Kath R, Guerry D 4th. Characterization of tenascin secreted by human melanoma cells. Cancer Res 1991; 51:4853-8; PMID:1716515
  • Hiraiwa N, Kida H, Sakakura T, Kusakabe M. Induction of tenascin in cancer cells by interactions with embryonic mesenchyme mediated by a diffusible factor. J Cell Sci 1993; 104 ( Pt 2):289-96; PMID:7685035
  • Takahashi Y, Sawada G, Kurashige J, Matsumura T, Uchi R, Ueo H, Ishibashi M, Takano Y, Akiyoshi S, Iwaya T, et al. Tumor-derived tenascin-C promotes the epithelial-mesenchymal transition in colorectal cancer cells. Anticancer Res 2013; 33:1927-34; PMID:23645740
  • Saupe F, Schwenzer A, Jia Y, Gasser I, Spenle C, Langlois B, Kammerer M, Lefebvre O, Hlushchuk R, Rupp T, et al. Tenascin-C downregulates wnt inhibitor dickkopf-1, promoting tumorigenesis in a neuroendocrine tumor model. Cell Rep 2013; 5:482-92; PMID:24139798; http://dx.doi.org/10.1016/j.celrep.2013.09.014
  • Talts JF, Wirl G, Dictor M, Muller WJ, Fassler R. Tenascin-C modulates tumor stroma and monocyte/macrophage recruitment but not tumor growth or metastasis in a mouse strain with spontaneous mammary cancer. J Cell Sci 1999; 112 (Pt 12):1855-64; PMID:10341205
  • O'Connell JT, Sugimoto H, Cooke VG, MacDonald BA, Mehta AI, LeBleu VS, Dewar R, Rocha RM, Brentani RR, Resnick MB, et al. VEGF-A and Tenascin-C produced by S100A4+ stromal cells are important for metastatic colonization. Proc Natl Acad Sci U S A 2011; 108:16002-7; PMID:21911392; http://dx.doi.org/10.1073/pnas.1109493108
  • Fukunaga-Kalabis M, Martinez G, Nguyen TK, Kim D, Santiago-Walker A, Roesch A, Herlyn M. Tenascin-C promotes melanoma progression by maintaining the ABCB5-positive side population. Oncogene 2010; 29:6115-24; PMID:20729912; http://dx.doi.org/10.1038/onc.2010.350
  • Tanaka K, Hiraiwa N, Hashimoto H, Yamazaki Y, Kusakabe M. Tenascin-C regulates angiogenesis in tumor through the regulation of vascular endothelial growth factor expression. Int J Cancer 2004; 108:31-40; PMID:14618612; http://dx.doi.org/10.1002/ijc.11509
  • Chiquet-Ehrismann R, Kalla P, Pearson CA, Beck K, Chiquet M. Tenascin interferes with fibronectin action. Cell 1988; 53:383-90; PMID:2452695; http://dx.doi.org/10.1016/0092-8674(88)90158-4
  • Chiquet-Ehrismann R, Matsuoka Y, Hofer U, Spring J, Bernasconi C, Chiquet M. Tenascin variants: differential binding to fibronectin and distinct distribution in cell cultures and tissues. Cell Regul 1991; 2:927-38; PMID:1725601
  • Huang W, Chiquet-Ehrismann R, Moyano JV, Garcia-Pardo A, Orend G. Interference of tenascin-C with syndecan-4 binding to fibronectin blocks cell adhesion and stimulates tumor cell proliferation. Cancer Res 2001; 61:8586-94; PMID:11731446
  • Wenk MB, Midwood KS, Schwarzbauer JE. Tenascin-C suppresses Rho activation. J Cell Biol 2000; 150:913-20; PMID:10953015; http://dx.doi.org/10.1083/jcb.150.4.913
  • Grahovac J, Becker D, Wells A. Melanoma cell invasiveness is promoted at least in part by the epidermal growth factor-like repeats of tenascin-C. J Invest Dermatol 2013; 133:210-20; PMID:22951722; http://dx.doi.org/10.1038/jid.2012.263
  • Hashimoto Y, Kim DJ, Adams JC. The roles of fascins in health and disease. J Pathol 2011; 224:289-300; PMID:21618240; http://dx.doi.org/10.1002/path.2894
  • Li A, Dawson JC, Forero-Vargas M, Spence HJ, Yu X, Konig I, Anderson K, Machesky LM. The actin-bundling protein fascin stabilizes actin in invadopodia and potentiates protrusive invasion. Curr Biol 2010; 20:339-45; PMID:20137952; http://dx.doi.org/10.1016/j.cub.2009.12.035
  • Vignjevic D, Kojima S, Aratyn Y, Danciu O, Svitkina T, Borisy GG. Role of fascin in filopodial protrusion. J Cell Biol 2006; 174:863-75; PMID:16966425; http://dx.doi.org/10.1083/jcb.200603013
  • Tan VY, Lewis SJ, Adams JC, Martin RM. Association of fascin-1 with mortality, disease progression and metastasis in carcinomas: a systematic review and meta-analysis. BMC Med 2013; 11:52; PMID:23442983; http://dx.doi.org/10.1186/1741-7015-11-52
  • Kim MY, Oskarsson T, Acharyya S, Nguyen DX, Zhang XH, Norton L, Massagué J. Tumor self-seeding by circulating cancer cells. Cell 2009; 139:1315-26; PMID:20064377; http://dx.doi.org/10.1016/j.cell.2009.11.025
  • Fischer D, Tucker RP, Chiquet-Ehrismann R, Adams JC. Cell-adhesive responses to tenascin-C splice variants involve formation of fascin microspikes. Mol Biol Cell 1997; 8:2055-75; PMID:9348542; http://dx.doi.org/10.1091/mbc.8.10.2055
  • Chaffer CL, Weinberg RA. A perspective on cancer cell metastasis. Science 2011; 331:1559-64; PMID:21436443; http://dx.doi.org/10.1126/science.1203543
  • Thiery JP, Acloque H, Huang RY, Nieto MA. Epithelial-mesenchymal transitions in development and disease. Cell 2009; 139:871-90; PMID:19945376; http://dx.doi.org/10.1016/j.cell.2009.11.007
  • Tanaka S, Sumioka T, Fujita N, Kitano A, Okada Y, Yamanaka O, Flanders KC, Miyajima M, Saika S. Suppression of injury-induced epithelial-mesenchymal transition in a mouse lens epithelium lacking tenascin-C. Mol Vis 2010; 16:1194-205; PMID:20664686
  • Katoh D, Nagaharu K, Shimojo N, Hanamura N, Yamashita M, Kozuka Y, Imanaka-Yoshida K, Yoshida T. Binding of alphavbeta1 and alphavbeta6 integrins to tenascin-C induces epithelial-mesenchymal transition-like change of breast cancer cells. Oncogenesis 2013; 2:e65
  • Nagaharu K, Zhang X, Yoshida T, Katoh D, Hanamura N, Kozuka Y, Ogawa T, Shiraishi T, Imanaka-Yoshida K. Tenascin C induces epithelial-mesenchymal transition-like change accompanied by SRC activation and focal adhesion kinase phosphorylation in human breast cancer cells. Am J Pathol 2011; 178:754-63; PMID:21281808; http://dx.doi.org/10.1016/j.ajpath.2010.10.015
  • Luzzi KJ, MacDonald IC, Schmidt EE, Kerkvliet N, Morris VL, Chambers AF, Groom AC. Multistep nature of metastatic inefficiency: dormancy of solitary cells after successful extravasation and limited survival of early micrometastases. Am J Pathol 1998; 153:865-73; http://dx.doi.org/10.1016/S0002-9440(10)65628-3
  • Sivasankaran B, Degen M, Ghaffari A, Hegi ME, Hamou MF, Ionescu MC, Zweifel C, Tolnay M, Wasner M, Mergenthaler S, et al. Tenascin-C is a novel RBPJkappa-induced target gene for Notch signaling in gliomas. Cancer Res 2009; 69:458-65; PMID:19147558; http://dx.doi.org/10.1158/0008-5472.CAN-08-2610
  • Beiter K, Hiendlmeyer E, Brabletz T, Hlubek F, Haynl A, Knoll C, Kirchner T, Jung A. β-Catenin regulates the expression of tenascin-C in human colorectal tumors. Oncogene 2005; 24:8200-4; PMID:16091738
  • Tsunoda T, Inada H, Kalembeyi I, Imanaka-Yoshida K, Sakakibara M, Okada R, Katsuta K, Sakakura T, Majima Y, Yoshida T. Involvement of large tenascin-C splice variants in breast cancer progression. Am J Pathol 2003; 162:1857-67; PMID:12759243; http://dx.doi.org/10.1016/S0002-9440(10)64320-9
  • Yoshida T, Yoshimura E, Numata H, Sakakura Y, Sakakura T. Involvement of tenascin-C in proliferation and migration of laryngeal carcinoma cells. Virchows Arch 1999; 435:496-500; PMID:10592053; http://dx.doi.org/10.1007/s004280050433
  • Orend G, Huang W, Olayioye MA, Hynes NE, Chiquet-Ehrismann R. Tenascin-C blocks cell-cycle progression of anchorage-dependent fibroblasts on fibronectin through inhibition of syndecan-4. Oncogene 2003; 22:3917-26; PMID:12813465; http://dx.doi.org/10.1038/sj.onc.1206618
  • Swindle CS, Tran KT, Johnson TD, Banerjee P, Mayes AM, Griffith L, Wells A. Epidermal growth factor (EGF)-like repeats of human tenascin-C as ligands for EGF receptor. J Cell Biol 2001; 154:459-68; PMID:11470832; http://dx.doi.org/10.1083/jcb.200103103
  • Van Obberghen-Schilling E, Tucker RP, Saupe F, Gasser I, Cseh B, Orend G. Fibronectin and tenascin-C: accomplices in vascular morphogenesis during development and tumor growth. Int J Dev Biol 2011; 55:511-25; PMID:21769776; http://dx.doi.org/10.1387/ijdb.103243eo
  • Sriramarao P, Mendler M, Bourdon MA. Endothelial cell attachment and spreading on human tenascin is mediated by α 2 β 1 and α v β 3 integrins. J Cell Sci 1993; 105 (Pt 4):1001-12; PMID:7693733
  • Canfield AE, Schor AM. Evidence that tenascin and thrombospondin-1 modulate sprouting of endothelial cells. J Cell Sci 1995; 108 (Pt 2):797-809; PMID:7539439
  • Chung CY, Murphy-Ullrich JE, Erickson HP. Mitogenesis, cell migration, and loss of focal adhesions induced by tenascin-C interacting with its cell surface receptor, annexin II. Mol Biol Cell 1996; 7:883-92; PMID:8816995; http://dx.doi.org/10.1091/mbc.7.6.883
  • Lopez-Novoa JM, Nieto MA. Inflammation and EMT: an alliance towards organ fibrosis and cancer progression. EMBO Mol Med 2009; 1:303-14; PMID:20049734; http://dx.doi.org/10.1002/emmm.200900043
  • Sottile J, Hocking DC. Fibronectin polymerization regulates the composition and stability of extracellular matrix fibrils and cell-matrix adhesions. Mol Biol Cell 2002; 13:3546-59; PMID:12388756; http://dx.doi.org/10.1091/mbc.E02-01-0048
  • Kaariainen E, Nummela P, Soikkeli J, Yin M, Lukk M, Jahkola T, Virolainen S, Ora A, Ukkonen E, Saksela O, et al. Switch to an invasive growth phase in melanoma is associated with tenascin-C, fibronectin, and procollagen-I forming specific channel structures for invasion. J Pathol 2006; 210:181-91; PMID:16924594; http://dx.doi.org/10.1002/path.2045
  • Wight TN, Potter-Perigo S. The extracellular matrix: an active or passive player in fibrosis? Am J Physiol Gastrointest Liver Physiol 2011; 301:G950-5; PMID:21512158; http://dx.doi.org/10.1152/ajpgi.00132.2011
  • Blaauboer ME, Boeijen FR, Emson CL, Turner SM, Zandieh-Doulabi B, Hanemaaijer R, Smit TH, Stoop R, Everts V. Extracellular matrix proteins: a positive feedback loop in lung fibrosis? Matrix Biol 2014; 34:170-8; PMID:24291458; http://dx.doi.org/10.1016/j.matbio.2013.11.002
  • Imanaka-Yoshida K, Hiroe M, Nishikawa T, Ishiyama S, Shimojo T, Ohta Y, Sakakura T, Yoshida T. Tenascin-C modulates adhesion of cardiomyocytes to extracellular matrix during tissue remodeling after myocardial infarction. Lab Invest 2001; 81:1015-24; PMID:11454990; http://dx.doi.org/10.1038/labinvest.3780313
  • Hardie WD, Korfhagen TR, Sartor MA, Prestridge A, Medvedovic M, Le Cras TD, Ikegami M, Wesselkamper SC, Davidson C, Dietsch M, et al. Genomic profile of matrix and vasculature remodeling in TGF-α induced pulmonary fibrosis. Am J Respir Cell Mol Biol 2007; 37:309-21; PMID:17496152; http://dx.doi.org/10.1165/rcmb.2006-0455OC
  • Carey WA, Taylor GD, Dean WB, Bristow JD. Tenascin-C deficiency attenuates TGF-ss-mediated fibrosis following murine lung injury. Am J Physiol Lung Cell Mol Physiol 2010; 299:L785-93; PMID:20833777; http://dx.doi.org/10.1152/ajplung.00385.2009
  • El-Karef A, Yoshida T, Gabazza EC, Nishioka T, Inada H, Sakakura T, Imanaka-Yoshida K. Deficiency of tenascin-C attenuates liver fibrosis in immune-mediated chronic hepatitis in mice. J Pathol 2007; 211:86-94; PMID:17121418; http://dx.doi.org/10.1002/path.2099
  • De Wever O, Nguyen QD, Van Hoorde L, Bracke M, Bruyneel E, Gespach C, Mareel M. Tenascin-C and SF/HGF produced by myofibroblasts in vitro provide convergent pro-invasive signals to human colon cancer cells through RhoA and Rac. FASEB J 2004; 18:1016-8; PMID:15059978
  • Islam MS, Kusakabe M, Horiguchi K, Iino S, Nakamura T, Iwanaga K, Hashimoto H, Matsumoto S, Murata T, Hori M, et al. PDGF and TGF-β promote tenascin-C expression in subepithelial myofibroblasts and contribute to intestinal mucosal protection in mice. Br J Pharmacol 2014; 171:375-88; PMID:24116743; http://dx.doi.org/10.1111/bph.12452
  • Tamaoki M, Imanaka-Yoshida K, Yokoyama K, Nishioka T, Inada H, Hiroe M, Sakakura T, Yoshida T. Tenascin-C regulates recruitment of myofibroblasts during tissue repair after myocardial injury. Am J Pathol 2005; 167:71-80; PMID:15972953; http://dx.doi.org/10.1016/S0002-9440(10)62954-9
  • Jacobs TW, Byrne C, Colditz G, Connolly JL, Schnitt SJ. Radial scars in benign breast-biopsy specimens and the risk of breast cancer. New Engl J Med 1999; 340:430-6; PMID:9971867; http://dx.doi.org/10.1056/NEJM199902113400604
  • Mossman BT, Churg A. Mechanisms in the pathogenesis of asbestosis and silicosis. Am J Respir Crit Care Med 1998; 157:1666-80; PMID:9603153; http://dx.doi.org/10.1164/ajrccm.157.5.9707141
  • Oberhauser AF, Marszalek PE, Erickson HP, Fernandez JM. The molecular elasticity of the extracellular matrix protein tenascin. Nat 1998; 393:181-5; PMID:9603523; http://dx.doi.org/10.1038/30270
  • Midwood K, Sacre S, Piccinini AM, Inglis J, Trebaul A, Chan E, Drexler S, Sofat N, Kashiwagi M, Orend G, et al. Tenascin-C is an endogenous activator of Toll-like receptor 4 that is essential for maintaining inflammation in arthritic joint disease. Nat Med 2009; 15:774-80; PMID:19561617; http://dx.doi.org/10.1038/nm.1987
  • Patel L, Sun W, Glasson SS, Morris EA, Flannery CR, Chockalingam PS. Tenascin-C induces inflammatory mediators and matrix degradation in osteoarthritic cartilage. BMC Musculoskelet Disord 2011; 12:164; PMID:21762512; http://dx.doi.org/10.1186/1471-2474-12-164
  • Puente Navazo MD, Valmori D, Ruegg C. The alternatively spliced domain TnFnIII A1A2 of the extracellular matrix protein tenascin-C suppresses activation-induced T lymphocyte proliferation and cytokine production. J Immunol 2001; 167:6431-40; PMID:11714809; http://dx.doi.org/10.4049/jimmunol.167.11.6431
  • Hauzenberger D, Olivier P, Gundersen D, Ruegg C. Tenascin-C inhibits beta1 integrin-dependent T lymphocyte adhesion to fibronectin through the binding of its fnIII 1-5 repeats to fibronectin. Eur J Immunol 1999; 29:1435-47; PMID:10359097; http://dx.doi.org/10.1002/(SICI)1521-4141(199905)29:05%3c1435::AID-IMMU1435%3e3.0.CO;2-N
  • Garcion E, Halilagic A, Faissner A, ffrench-Constant C. Generation of an environmental niche for neural stem cell development by the extracellular matrix molecule tenascin C. Development 2004; 131:3423-32; PMID:15226258; http://dx.doi.org/10.1242/dev.01202
  • Garcion E, Faissner A, ffrench-Constant C. Knockout mice reveal a contribution of the extracellular matrix molecule tenascin-C to neural precursor proliferation and migration. Development 2001; 128:2485-96; PMID:11493565
  • Klein G, Beck S, Muller CA. Tenascin is a cytoadhesive extracellular matrix component of the human hematopoietic microenvironment. J Cell Biol 1993; 123:1027-35; PMID:7693718; http://dx.doi.org/10.1083/jcb.123.4.1027
  • Seiffert M, Beck SC, Schermutzki F, Muller CA, Erickson HP, Klein G. Mitogenic and adhesive effects of tenascin-C on human hematopoietic cells are mediated by various functional domains. Matrix Biol 1998; 17:47-63; PMID:9628252; http://dx.doi.org/10.1016/S0945-053X(98)90124-X
  • Yokosaki Y, Palmer EL, Prieto AL, Crossin KL, Bourdon MA, Pytela R, Sheppard D. The integrin α 9 β 1 mediates cell attachment to a non-RGD site in the third fibronectin type III repeat of tenascin. J Biol Chem 1994; 269:26691-6; PMID:7523411
  • Nakamura-Ishizu A, Okuno Y, Omatsu Y, Okabe K, Morimoto J, Uede T, Nagasawa T, Suda T, Kubota Y. Extracellular matrix protein tenascin-C is required in the bone marrow microenvironment primed for hematopoietic regeneration. Blood 2012; 119:5429-37; PMID:22553313; http://dx.doi.org/10.1182/blood-2011-11-393645
  • Tucker RP, Ferralli J, Schittny JC, Chiquet-Ehrismann R. Tenascin-C and tenascin-W in whisker follicle stem cell niches: possible roles in regulating stem cell proliferation and migration. J Cell Sci 2013; 126:5111-5; PMID:24101721; http://dx.doi.org/10.1242/jcs.134650
  • Ellis SL, Heazlewood SY, Williams B, Reitsma AJ, Grassinger J, Borg J, Heazlewood CK, Chidgey AP, Nilsson SK. The role of Tenascin C in the lymphoid progenitor cell niche. Exp Hematol 2013; 41:1050-61; PMID:24084079; http://dx.doi.org/10.1016/j.exphem.2013.09.009
  • Flenkenthaler F, Windschuttl S, Frohlich T, Schwarzer JU, Mayerhofer A, Arnold GJ. Secretome analysis of testicular peritubular cells: a window into the human testicular microenvironment and the spermatogonial stem cell niche in man. J Proteome Res 2014; 13:1259-69; PMID:24422521; http://dx.doi.org/10.1021/pr400769z
  • Nakatsu MN, Vartanyan L, Vu DM, Ng MY, Li X, Deng SX. Preferential biological processes in the human limbus by differential gene profiling. PloS one 2013; 8:e61833; PMID:23630617; http://dx.doi.org/10.1371/journal.pone.0061833
  • Descot A, Oskarsson T. The molecular composition of the metastatic niche. Exp Cell Res 2013; 319:1679-86; PMID:23707205
  • Barcellos-Hoff MH, Lyden D, Wang TC. The evolution of the cancer niche during multistage carcinogenesis. Nat Rev Cancer 2013; 13:511-8; PMID:23760023; http://dx.doi.org/10.1038/nrc3536
  • Dontu G, Abdallah WM, Foley JM, Jackson KW, Clarke MF, Kawamura MJ, Wicha MS. In vitro propagation and transcriptional profiling of human mammary stem/progenitor cells. Genes Dev 2003; 17:1253-70; PMID:12756227; http://dx.doi.org/10.1101/gad.1061803
  • Oskarsson T, Massague J. Extracellular matrix players in metastatic niches. EMBO J 2012; 31:254-6; PMID:22179697; http://dx.doi.org/10.1038/emboj.2011.469
  • Wagner KU, Rui H. Jak2/Stat5 signaling in mammogenesis, breast cancer initiation and progression. J Mammary Gland Biol Neoplasia 2008; 13:93-103; PMID:18228120; http://dx.doi.org/10.1007/s10911-008-9062-z
  • Ruiz C, Huang W, Hegi ME, Lange K, Hamou MF, Fluri E, Oakeley EJ, Chiquet-Ehrismann R, Orend G. Growth promoting signaling by tenascin-C [corrected]. Cancer Res 2004; 64:7377-85; PMID:15492259; http://dx.doi.org/10.1158/0008-5472.CAN-04-1234
  • Hermann PC, Huber SL, Herrler T, Aicher A, Ellwart JW, Guba M, Bruns CJ, Heeschen C. Distinct populations of cancer stem cells determine tumor growth and metastatic activity in human pancreatic cancer. Cell Stem Cell 2007; 1:313-23; PMID:18371365; http://dx.doi.org/10.1016/j.stem.2007.06.002
  • Mani SA, Guo W, Liao MJ, Eaton EN, Ayyanan A, Zhou AY, Brooks M, Reinhard F, Zhang CC, Shipitsin M, et al. The epithelial-mesenchymal transition generates cells with properties of stem cells. Cell 2008; 133:704-15; PMID:18485877; http://dx.doi.org/10.1016/j.cell.2008.03.027
  • Malanchi I, Santamaria-Martinez A, Susanto E, Peng H, Lehr HA, Delaloye JF, Huelsken J. Interactions between cancer stem cells and their niche govern metastatic colonization. Nature 2012; 481:85-9; http://dx.doi.org/10.1038/nature10694
  • Kii I, Nishiyama T, Li M, Matsumoto K, Saito M, Amizuka N, Kudo A. Incorporation of tenascin-C into the extracellular matrix by periostin underlies an extracellular meshwork architecture. J Biol Chem 2010; 285:2028-39; PMID:19887451; http://dx.doi.org/10.1074/jbc.M109.051961
  • Acharyya S, Oskarsson T, Vanharanta S, Malladi S, Kim J, Morris PG, Manova-Todorova K, Leversha M, Hogg N, Seshan VE, et al. A CXCL1 paracrine network links cancer chemoresistance and metastasis. Cell 2012; 150:165-78; PMID:22770218; http://dx.doi.org/10.1016/j.cell.2012.04.042
  • Schafer ZT, Grassian AR, Song L, Jiang Z, Gerhart-Hines Z, Irie HY, Gao S, Puigserver P, Brugge JS. Antioxidant and oncogene rescue of metabolic defects caused by loss of matrix attachment. Nature 2009; 461:109-13; PMID:19693011; http://dx.doi.org/10.1038/nature08268
  • Farmer P, Bonnefoi H, Anderle P, Cameron D, Wirapati P, Becette V, André S, Piccart M, Campone M, Brain E, et al. A stroma-related gene signature predicts resistance to neoadjuvant chemotherapy in breast cancer. Nat Med 2009; 15:68-74; http://dx.doi.org/10.1038/nm.1908
  • Gong XG, Lv YF, Li XQ, Xu FG, Ma QY. Gemcitabine resistance induced by interaction between alternatively spliced segment of tenascin-C and annexin A2 in pancreatic cancer cells. Biol Pharm Bull 2010; 33:1261-7; PMID:20686216; http://dx.doi.org/10.1248/bpb.33.1261
  • Wang B, Liu K, Lin HY, Bellam N, Ling S, Lin WC. Fourteen-3-3Tau regulates ubiquitin-independent proteasomal degradation of p21, a novel mechanism of p21 downregulation in breast cancer. Mol Cell Biol 2010; 30:1508-27; PMID:20086099; http://dx.doi.org/10.1128/MCB.01335-09
  • Helleman J, Jansen MP, Ruigrok-Ritstier K, van Staveren IL, Look MP, Meijer-van Gelder ME, Sieuwerts AM, Klijn JG, Sleijfer S, Foekens JA, et al. Association of an extracellular matrix gene cluster with breast cancer prognosis and endocrine therapy response. Clin Cancer Res 2008; 14:5555-64; PMID:18765548; http://dx.doi.org/10.1158/1078-0432.CCR-08-0555