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Volumn 9, Issue 1-2, 2015, Pages 96-104

Tenascin-C and integrins in cancer

Author keywords

Cancer cell; Integrins; Splice variant; Stromal cell; Tenascin C

Indexed keywords

EPIDERMAL GROWTH FACTOR; FIBRONECTIN; INTEGRIN; INTEGRIN RECEPTOR; PROTEIN TYROSINE PHOSPHATASE; SYNDECAN 4; TENASCIN; TOLL LIKE RECEPTOR 4;

EID: 84948747425     PISSN: 19336918     EISSN: 19336926     Source Type: Journal    
DOI: 10.1080/19336918.2015.1008332     Document Type: Review
Times cited : (135)

References (94)
  • 1
    • 33749452709 scopus 로고    scopus 로고
    • Tenascin-C induced signaling in cancer
    • Orend G, Chiquet-Ehrismann R. Tenascin-C induced signaling in cancer. Cancer Lett 2006; 244:143-63; http://dx.doi.org/10.1016/j.canlet.2006.02.017
    • (2006) Cancer Lett , vol.244 , pp. 143-163
    • Orend, G.1    Chiquet-Ehrismann, R.2
  • 3
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes RO. Integrins: bidirectional, allosteric signaling machines. Cell 2002; 110:673-87; http://dx.doi.org/10.1016/S0092-8674(02)00971-6
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 4
    • 33750453714 scopus 로고    scopus 로고
    • Integrin ligands at a glance
    • Humphries JD, Byron A, Humphries MJ. Integrin ligands at a glance. J Cell Sci 2006; 119:3901-3; http://dx.doi.org/10.1242/jcs.03098
    • (2006) J Cell Sci , vol.119 , pp. 3901-3903
    • Humphries, J.D.1    Byron, A.2    Humphries, M.J.3
  • 5
    • 65649146880 scopus 로고    scopus 로고
    • Integrin signalling at a glance
    • Harburger DS, Calderwood DA. Integrin signalling at a glance. J Cell Sci 2009; 122:159-63; http://dx.doi.org/10.1242/jcs.018093
    • (2009) J Cell Sci , vol.122 , pp. 159-163
    • Harburger, D.S.1    Calderwood, D.A.2
  • 6
    • 0036222549 scopus 로고    scopus 로고
    • Sensing the environment: A historical perspective on integrin signal transduction
    • Miranti CK, Brugge JS. Sensing the environment: a historical perspective on integrin signal transduction. Nat Cell Biol 2002; 4:E83-90; http://dx.doi.org/10.1038/ncb0402-e83
    • (2002) Nat Cell Biol , vol.4 , pp. E83-E90
    • Miranti, C.K.1    Brugge, J.S.2
  • 8
    • 0028305739 scopus 로고
    • Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C
    • Chung CY, Erickson HP. Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C. J Cell Biol 1994; 126:539-48;; http://dx.doi.org/10.1083/jcb.126.2.539
    • (1994) J Cell Biol , vol.126 , pp. 539-548
    • Chung, C.Y.1    Erickson, H.P.2
  • 9
    • 0030003154 scopus 로고    scopus 로고
    • Mitogenesis, cell migration, and loss of focal adhesions induced by tenascin-C interacting with its cell surface receptor, annexin II
    • 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
    • (1996) Mol Biol Cell , vol.7 , pp. 883-892
    • Chung, C.Y.1    Murphy-Ullrich, J.E.2    Erickson, H.P.3
  • 10
    • 0035252884 scopus 로고    scopus 로고
    • Glial tumor cell adhesion is mediated by binding of the FNIII domain of receptor protein tyrosine phosphatase b (RPTPbeta) to tenascin C
    • Adamsky K, Schilling J, Garwood J, Faissner A, Peles E. Glial tumor cell adhesion is mediated by binding of the FNIII domain of receptor protein tyrosine phosphatase b (RPTPbeta) to tenascin C. Oncogene 2001; 20:609-18; http://dx.doi.org/10.1038/sj.onc.1204119
    • (2001) Oncogene , vol.20 , pp. 609-618
    • Adamsky, K.1    Schilling, J.2    Garwood, J.3    Faissner, A.4    Peles, E.5
  • 11
    • 0030906999 scopus 로고    scopus 로고
    • The fibrinogen-like globe of tenascin-C mediates its interactions with neurocan and phosphacan/protein-tyrosine phosphatase-zeta/b
    • Milev P, Fischer D, Häring M, Schulthess T, Margolis RK, Chiquet-Ehrismann R, Margolis RU. The fibrinogen-like globe of tenascin-C mediates its interactions with neurocan and phosphacan/protein-tyrosine phosphatase-zeta/b. J Biol Chem 1997; 272:15501-9; http://dx.doi.org/10.1074/jbc.272.24.15501
    • (1997) J Biol Chem , vol.272 , pp. 15501-15509
    • Milev, P.1    Fischer, D.2    Häring, M.3    Schulthess, T.4    Margolis, R.K.5    Chiquet-Ehrismann, R.6    Margolis, R.U.7
  • 12
    • 0035939665 scopus 로고    scopus 로고
    • Epidermal growth factor (EGF)-like repeats of human tenascin-C as ligands for EGF receptor
    • 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; http://dx.doi.org/10.1083/jcb.200103103
    • (2001) J Cell Biol , vol.154 , pp. 459-468
    • Swindle, C.S.1    Tran, K.T.2    Johnson, T.D.3    Banerjee, P.4    Mayes, A.M.5    Griffith, L.6    Wells, A.7
  • 13
    • 0028813381 scopus 로고
    • A single heparin binding region within the fibrinogen-like domain is functional in chick tenascin-C
    • Fischer D, Chiquet-Ehrismann R, Bernasconi C, Chiquet M. A single heparin binding region within the fibrinogen-like domain is functional in chick tenascin-C. J Biol Chem 1995; 270:3378-84; http://dx.doi.org/10.1074/jbc.270.27.16315
    • (1995) J Biol Chem , vol.270 , pp. 3378-3384
    • Fischer, D.1    Chiquet-Ehrismann, R.2    Bernasconi, C.3    Chiquet, M.4
  • 14
    • 0028924268 scopus 로고
    • Tenascin-C binds heparin by its fibronectin type III domain five
    • Weber P, Zimmermann DR, Winterhalter KH, Vaughan L. Tenascin-C binds heparin by its fibronectin type III domain five. J Biol Chem 1995; 270: 4619-23; http://dx.doi.org/10.1074/jbc.270.9.4619
    • (1995) J Biol Chem , vol.270 , pp. 4619-4623
    • Weber, P.1    Zimmermann, D.R.2    Winterhalter, K.H.3    Vaughan, L.4
  • 16
    • 70249086983 scopus 로고    scopus 로고
    • Defining the role of integrin alphavbeta6 in cancer
    • Bandyopadhyay A, Raghavan S. Defining the role of integrin alphavbeta6 in cancer. Curr Drug Targets 2009; 10:645-52; http://dx.doi.org/10.2174/138945009788680374
    • (2009) Curr Drug Targets , vol.10 , pp. 645-652
    • Bandyopadhyay, A.1    Raghavan, S.2
  • 17
    • 0029796370 scopus 로고    scopus 로고
    • Differential effects of the integrins alpha9beta1, alphavbeta3, and alphavbeta6 on cell proliferative responses to tenascin. Roles of the b subunit extracellular and cytoplasmic domains
    • Yokosaki Y, Monis H, Chen J, Sheppard D. Differential effects of the integrins alpha9beta1, alphavbeta3, and alphavbeta6 on cell proliferative responses to tenascin. Roles of the b subunit extracellular and cytoplasmic domains. J Biol Chem 1996; 271:24144-50; http://dx.doi.org/10.1074/jbc.271.39.24144
    • (1996) J Biol Chem , vol.271 , pp. 24144-24150
    • Yokosaki, Y.1    Monis, H.2    Chen, J.3    Sheppard, D.4
  • 18
    • 14944348752 scopus 로고    scopus 로고
    • Transcriptional activation of integrin beta6 during the epithelial-mesenchymal transition defines a novel prognostic indicator of aggressive colon carcinoma
    • Bates RC, Bellovin DI, Brown C, Maynard E, Wu B, Kawakatsu H, Sheppard D, Oettgen P, Mercurio AM. Transcriptional activation of integrin beta6 during the epithelial-mesenchymal transition defines a novel prognostic indicator of aggressive colon carcinoma. J Clin Invest 2005; 115:339-47; http://dx.doi.org/10.1172/JCI200523183
    • (2005) J Clin Invest , vol.115 , pp. 339-347
    • Bates, R.C.1    Bellovin, D.I.2    Brown, C.3    Maynard, E.4    Wu, B.5    Kawakatsu, H.6    Sheppard, D.7    Oettgen, P.8    Mercurio, A.M.9
  • 19
    • 84883188295 scopus 로고    scopus 로고
    • Binding of avb1 and avb6 integrins to tenascin-C induces epithelial-mesenchymal transition-like change of breast cancer cells
    • Katoh D, Nagaharu K, Shimojo N, Hanamura N, Yamashita M, Kozuka Y, Imanaka-Yoshida K, Yoshida T. Binding of avb1 and avb6 integrins to tenascin-C induces epithelial-mesenchymal transition-like change of breast cancer cells. Oncogenesis 2013; 2:e65; http://dx.doi.org/10.1038/oncsis.2013.27
    • (2013) Oncogenesis , pp. 2
    • Katoh, D.1    Nagaharu, K.2    Shimojo, N.3    Hanamura, N.4    Yamashita, M.5    Kozuka, Y.6    Imanaka-Yoshida, K.7    Yoshida, T.8
  • 20
    • 61449094945 scopus 로고    scopus 로고
    • The role of the integrin a v beta6 in regulating the epithelial to mesenchymal transition in oral cancer
    • Ramos DM, Dang D, Sadler S. The role of the integrin a v beta6 in regulating the epithelial to mesenchymal transition in oral cancer. Anticancer Res 2009; 29: 125-30
    • (2009) Anticancer Res , vol.29 , pp. 125-130
    • Ramos, D.M.1    Dang, D.2    Sadler, S.3
  • 21
    • 27644538315 scopus 로고    scopus 로고
    • Integrin-mediated activation of latent transforming growth factor b
    • Sheppard D. Integrin-mediated activation of latent transforming growth factor b. Cancer Metastasis Rev 2005; 24:395-402; http://dx.doi.org/10.1007/s10555-005-5131-6
    • (2005) Cancer Metastasis Rev , vol.24 , pp. 395-402
    • Sheppard, D.1
  • 22
    • 0037457668 scopus 로고    scopus 로고
    • Tenascin-C upregulates matrix metalloproteinase-9 in breast cancer cells: Direct and synergistic effects with transforming growth factor b 1
    • Kalembeyi I, Inada H, Nishiura R, Imanaka-Yoshida K, Sakakura T, Yoshida T. Tenascin-C upregulates matrix metalloproteinase-9 in breast cancer cells: Direct and synergistic effects with transforming growth factor b 1. Int J Cancer 2003; 105:53-60; http://dx.doi.org/10.1002/ijc.11037
    • (2003) Int J Cancer , vol.105 , pp. 53-60
    • Kalembeyi, I.1    Inada, H.2    Nishiura, R.3    Imanaka-Yoshida, K.4    Sakakura, T.5    Yoshida, T.6
  • 23
    • 84865642922 scopus 로고    scopus 로고
    • The newcomer in the integrin family: Integrin a9 in biology and cancer
    • Høye AM, Couchman JR, Wewer UM, Fukami K, Yoneda A. The newcomer in the integrin family: integrin a9 in biology and cancer. Adv Biol Regul 2012; 52:326-39; http://dx.doi.org/10.1016/j.jbior.2012.03.004
    • (2012) Adv Biol Regul , vol.52 , pp. 326-339
    • Høye, A.M.1    Couchman, J.R.2    Wewer, U.M.3    Fukami, K.4    Yoneda, A.5
  • 24
    • 0032496223 scopus 로고    scopus 로고
    • Identification of the ligand binding site for the integrin alpha9 beta1 in the third fibronectin type III repeat of tenascin-C
    • Yokosaki Y, Matsuura N, Higashiyama S, Murakami I, Obara M, Yamakido M, Shigeto N, Chen J, Sheppard D. Identification of the ligand binding site for the integrin alpha9 beta1 in the third fibronectin type III repeat of tenascin-C. J Biol Chem 1998; 273:11423-8; http://dx.doi.org/10.1074/jbc.273.19.11423
    • (1998) J Biol Chem , vol.273 , pp. 11423-11428
    • Yokosaki, Y.1    Matsuura, N.2    Higashiyama, S.3    Murakami, I.4    Obara, M.5    Yamakido, M.6    Shigeto, N.7    Chen, J.8    Sheppard, D.9
  • 25
    • 33646065641 scopus 로고    scopus 로고
    • Immunohistochemical assessment of fibronectin and tenascin and their integrin receptors alpha5beta1 and alpha9beta1 in gastric and colorectal cancers with lymph node and liver metastases
    • Gulubova M, Vlaykova T. Immunohistochemical assessment of fibronectin and tenascin and their integrin receptors alpha5beta1 and alpha9beta1 in gastric and colorectal cancers with lymph node and liver metastases. Acta Histochem 2006; 108:25-35; http://dx.doi.org/10.1016/j.acthis.2005.12.001
    • (2006) Acta Histochem , vol.108 , pp. 25-35
    • Gulubova, M.1    Vlaykova, T.2
  • 26
    • 79952558693 scopus 로고    scopus 로고
    • Clinical and functional significance of a9b1 integrin expression in breast cancer: A novel cell-surface marker of the basal phenotype that promotes tumour cell invasion
    • Allen MD, Vaziri R, Green M, Chelala C, Brentnall AR, Dreger S, Vallath S, Nitch-Smith H, Hayward J, Carpenter R, et al. Clinical and functional significance of a9b1 integrin expression in breast cancer: a novel cell-surface marker of the basal phenotype that promotes tumour cell invasion. J Pathol 2011; 223: 646-58; http://dx.doi.org/10.1002/path.2833
    • (2011) J Pathol , vol.223 , pp. 646-658
    • Allen, M.D.1    Vaziri, R.2    Green, M.3    Chelala, C.4    Brentnall, A.R.5    Dreger, S.6    Vallath, S.7    Nitch-Smith, H.8    Hayward, J.9    Carpenter, R.10
  • 27
    • 84914146487 scopus 로고    scopus 로고
    • Tumor-a9b1 integrin-mediated signaling induces breast cancer growth and lymphatic metastasis via the recruitment of cancer-associated fibroblasts
    • Ota D, Kanayama M, Matsui Y, Ito K, Maeda N, Kutomi G, Hirata K, Torigoe T, Sato N, Takaoka A, et al. Tumor-a9b1 integrin-mediated signaling induces breast cancer growth and lymphatic metastasis via the recruitment of cancer-associated fibroblasts. J Mol Med (Berl) 2014; 92(12):1271-81
    • (2014) J Mol Med (Berl) , vol.92 , Issue.12 , pp. 1271-1281
    • Ota, D.1    Kanayama, M.2    Matsui, Y.3    Ito, K.4    Maeda, N.5    Kutomi, G.6    Hirata, K.7    Torigoe, T.8    Sato, N.9    Takaoka, A.10
  • 28
    • 84903952426 scopus 로고    scopus 로고
    • Endothelial cell-derived fibronectin extra domain A promotes colorectal cancer metastasis via inducing epithelial-mesenchymal transition
    • Ou J, Peng Y, Deng J, Miao H, Zhou J, Zha L, Zhou R, Yu L, Shi H, Liang H. Endothelial cell-derived fibronectin extra domain A promotes colorectal cancer metastasis via inducing epithelial-mesenchymal transition. Carcinogenesis 2014; 35:1661-70
    • (2014) Carcinogenesis , vol.35 , pp. 1661-1670
    • Ou, J.1    Peng, Y.2    Deng, J.3    Miao, H.4    Zhou, J.5    Zha, L.6    Zhou, R.7    Yu, L.8    Shi, H.9    Liang, H.10
  • 29
    • 0343090477 scopus 로고    scopus 로고
    • Immunolocalization of tenascin-C, alpha9 integrin subunit, and alphavbeta6 integrin during wound healing in human oral mucosa
    • Häkkinen L, Hildebrand HC, Berndt A, Kosmehl H, Larjava H. Immunolocalization of tenascin-C, alpha9 integrin subunit, and alphavbeta6 integrin during wound healing in human oral mucosa. J Histochem Cytochem 2000; 48:985-98; http://dx.doi.org/10.1177/002215540004800712
    • (2000) J Histochem Cytochem , vol.48 , pp. 985-998
    • Häkkinen, L.1    Hildebrand, H.C.2    Berndt, A.3    Kosmehl, H.4    Larjava, H.5
  • 30
    • 0032917295 scopus 로고    scopus 로고
    • Expression of tenascin-C and the integrin a 9 subunit in regeneration of rat nasal mucosa after chemical injury: Involvement in migration and proliferation of epithelial cells
    • Yoshimura E, Majima A, Sakakura Y, Sakakura T, Yoshida T. Expression of tenascin-C and the integrin a 9 subunit in regeneration of rat nasal mucosa after chemical injury: involvement in migration and proliferation of epithelial cells. Histochem Cell Biol 1999; 111:259-64; http://dx.doi.org/10.1007/s004180050356
    • (1999) Histochem Cell Biol , vol.111 , pp. 259-264
    • Yoshimura, E.1    Majima, A.2    Sakakura, Y.3    Sakakura, T.4    Yoshida, T.5
  • 31
    • 1542269303 scopus 로고    scopus 로고
    • Integrins: Roles in cancer development and as treatment targets
    • Jin H, Varner J. Integrins: roles in cancer development and as treatment targets. Br J Cancer 2004; 90:561-5; http://dx.doi.org/10.1038/sj.bjc.6601576
    • (2004) Br J Cancer , vol.90 , pp. 561-565
    • Jin, H.1    Varner, J.2
  • 32
    • 84868143439 scopus 로고    scopus 로고
    • Cheresh DA. AV integrins in angiogenesis and cancer
    • Weis SM, Cheresh DA. aV integrins in angiogenesis and cancer. Cold Spring Harb Perspect Med 2011; 1: a006478; http://dx.doi.org/10.1101/cshperspect.a006478
    • (2011) Cold Spring Harb Perspect Med , vol.1
    • Weis, S.M.1
  • 33
    • 0027364324 scopus 로고
    • Multiple integrins mediate cell attachment to cytotactin/tenascin
    • Prieto AL, Edelman GM, Crossin KL. Multiple integrins mediate cell attachment to cytotactin/tenascin. Proc Natl Acad Sci U S A 1993; 90:10154-8; http://dx.doi.org/10.1073/pnas.90.21.10154
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 10154-10158
    • Prieto, A.L.1    Edelman, G.M.2    Crossin, K.L.3
  • 34
    • 0034595969 scopus 로고    scopus 로고
    • Identification of amino acid sequences in fibrinogen gamma -chain and tenascin C C-terminal domains critical for binding to integrin a vbeta 3
    • Yokoyama K, Erickson HP, Ikeda Y, Takada Y. Identification of amino acid sequences in fibrinogen gamma -chain and tenascin C C-terminal domains critical for binding to integrin a vbeta 3. J Biol Chem 2000; 275:16891-8; http://dx.doi.org/10.1074/jbc.M000610200
    • (2000) J Biol Chem , vol.275 , pp. 16891-16898
    • Yokoyama, K.1    Erickson, H.P.2    Ikeda, Y.3    Takada, Y.4
  • 35
    • 79960675151 scopus 로고    scopus 로고
    • Tenascin-C Enhances Crosstalk Signaling of Integrin a v b 3/PDGFR-b Complex by SRC Recruitment Promoting PDGFInduced Proliferation and Migration in Smooth Muscle Cells
    • Ishigaki T, Imanaka-Yoshida K, Shimojo N, Matsushima S, Taki W, Yoshida T. Tenascin-C Enhances Crosstalk Signaling of Integrin a v b 3/PDGFR-b Complex by SRC Recruitment Promoting PDGFInduced Proliferation and Migration in Smooth Muscle Cells. J Cell Physiol 2011; 226:2617-24; http://dx.doi.org/10.1002/jcp.22614
    • (2011) J Cell Physiol , vol.226 , pp. 2617-2624
    • Ishigaki, T.1    Imanaka-Yoshida, K.2    Shimojo, N.3    Matsushima, S.4    Taki, W.5    Yoshida, T.6
  • 37
    • 0035984171 scopus 로고    scopus 로고
    • Lessons from the alpha2 integrin knockout mouse
    • Mercurio AM. Lessons from the alpha2 integrin knockout mouse. Am J Pathol 2002; 161:3-6; http://dx.doi.org/10.1016/S0002-9440(10)64149-1
    • (2002) Am J Pathol , vol.161 , pp. 3-6
    • Mercurio, A.M.1
  • 38
    • 0030007495 scopus 로고    scopus 로고
    • Tenascin mediates human glioma cell migration and modulates cell migration on fibronectin
    • Deryugina EI, Bourdon MA. Tenascin mediates human glioma cell migration and modulates cell migration on fibronectin. J Cell Sci 1996; 109 (Pt 3):643-52
    • (1996) J Cell Sci , vol.109 , pp. 643-652
    • Deryugina, E.I.1    Bourdon, M.A.2
  • 39
    • 0027303968 scopus 로고
    • Endothelial cell attachment and spreading on human tenascin is mediated by a 2 b 1 and a v b 3 integrins
    • Sriramarao P, Mendler M, Bourdon MA. Endothelial cell attachment and spreading on human tenascin is mediated by a 2 b 1 and a v b 3 integrins. J Cell Sci 1993; 105 (Pt 4):1001-12
    • (1993) J Cell Sci , vol.105 , pp. 1001-1012
    • Sriramarao, P.1    Mendler, M.2    Bourdon, M.A.3
  • 40
    • 41549155540 scopus 로고    scopus 로고
    • Collagen I-mediated upregulation of N-cadherin requires cooperative signals from integrins and discoidin domain receptor 1
    • Shintani Y, Fukumoto Y, Chaika N, Svoboda R, Wheelock MJ, Johnson KR. Collagen I-mediated upregulation of N-cadherin requires cooperative signals from integrins and discoidin domain receptor 1. J Cell Biol 2008; 180:1277-89; http://dx.doi.org/10.1083/jcb.200708137
    • (2008) J Cell Biol , vol.180 , pp. 1277-1289
    • Shintani, Y.1    Fukumoto, Y.2    Chaika, N.3    Svoboda, R.4    Wheelock, M.J.5    Johnson, K.R.6
  • 41
    • 77953064012 scopus 로고    scopus 로고
    • Laminin-binding integrins and their tetraspanin partners as potential antimetastatic targets
    • Stipp CS. Laminin-binding integrins and their tetraspanin partners as potential antimetastatic targets. Expert Rev Mol Med 2010; 12:e3; http://dx.doi.org/10.1017/S1462399409001355
    • (2010) Expert Rev Mol Med , vol.12
    • Stipp, C.S.1
  • 42
    • 0842279598 scopus 로고    scopus 로고
    • Neurite outgrowth by the alternatively spliced region of human tenascin-C is mediated by neuronal alpha7beta1 integrin
    • Mercado ML, Nur-e-Kamal A, Liu HY, Gross SR, Movahed R, Meiners S. Neurite outgrowth by the alternatively spliced region of human tenascin-C is mediated by neuronal alpha7beta1 integrin. J Neurosci 2004; 24:238-47; http://dx.doi.org/10.1523/JNEUROSCI.4519-03.2004
    • (2004) J Neurosci , vol.24 , pp. 238-247
    • Mercado, M.L.1    Nur-E-Kamal, A.2    Liu, H.Y.3    Gross, S.R.4    Movahed, R.5    Meiners, S.6
  • 43
    • 34347385686 scopus 로고    scopus 로고
    • Analysis of integrin alpha7 mutations in prostate cancer, liver cancer, glioblastoma multiforme, and leiomyosarcoma
    • Ren B, Yu YP, Tseng GC, Wu C, Chen K, Rao UN, Nelson J, Michalopoulos GK, Luo JH. Analysis of integrin alpha7 mutations in prostate cancer, liver cancer, glioblastoma multiforme, and leiomyosarcoma. J Natl Cancer Inst 2007; 99:868-80; http://dx.doi.org/10.1093/jnci/djk199
    • (2007) J Natl Cancer Inst , vol.99 , pp. 868-880
    • Ren, B.1    Yu, Y.P.2    Tseng, G.C.3    Wu, C.4    Chen, K.5    Rao, U.N.6    Nelson, J.7    Michalopoulos, G.K.8    Luo, J.H.9
  • 44
    • 0036947610 scopus 로고    scopus 로고
    • Lessons in congenital and acquired renal disease from alpha8 integrin mutant mice
    • Hartner A, Dötsch J. Lessons in congenital and acquired renal disease from alpha8 integrin mutant mice. Pediatr Nephrol 2002; 17:882-8; http://dx.doi.org/10.1007/s00467-002-0950-y
    • (2002) Pediatr Nephrol , vol.17 , pp. 882-888
    • Hartner, A.1    Dötsch, J.2
  • 45
    • 0028981367 scopus 로고
    • The human integrin a 8 b 1 functions as a receptor for tenascin, fibronectin, and vitronectin
    • Schnapp LM, Hatch N, Ramos DM, Klimanskaya IV, Sheppard D, Pytela R. The human integrin a 8 b 1 functions as a receptor for tenascin, fibronectin, and vitronectin. J Biol Chem 1995; 270:23196-202; http://dx.doi.org/10.1074/jbc.270.39.23196
    • (1995) J Biol Chem , vol.270 , pp. 23196-23202
    • Schnapp, L.M.1    Hatch, N.2    Ramos, D.M.3    Klimanskaya, I.V.4    Sheppard, D.5    Pytela, R.6
  • 46
    • 0345215170 scopus 로고    scopus 로고
    • Utilization of a soluble integrin-alkaline phosphatase chimera to characterize integrin a 8 b 1 receptor interactions with tenascin: Murine a 8 b 1 binds to the RGD site in tenascin-C fragments, but not to native tenascin-C
    • Denda S, Müller U, Crossin KL, Erickson HP, Reichardt LF. Utilization of a soluble integrin-alkaline phosphatase chimera to characterize integrin a 8 b 1 receptor interactions with tenascin: murine a 8 b 1 binds to the RGD site in tenascin-C fragments, but not to native tenascin-C. Biochemistry 1998; 37:5464-74; http://dx.doi.org/10.1021/bi9727489
    • (1998) Biochemistry , vol.37 , pp. 5464-5474
    • Denda, S.1    Müller, U.2    Crossin, K.L.3    Erickson, H.P.4    Reichardt, L.F.5
  • 47
    • 14944345010 scopus 로고    scopus 로고
    • Tenascin-W is found in malignant mammary tumors, promotes alpha8 integrin-dependent motility and requires p38MAPK activity for BMP-2 and TNF-a induced expression in vitro
    • Scherberich A, Tucker RP, Degen M, Brown-Luedi M, Andres AC, Chiquet-Ehrismann R. Tenascin-W is found in malignant mammary tumors, promotes alpha8 integrin-dependent motility and requires p38MAPK activity for BMP-2 and TNF-a induced expression in vitro. Oncogene 2005; 24:1525-32; http://dx.doi.org/10.1038/sj.onc.1208342
    • (2005) Oncogene , vol.24 , pp. 1525-1532
    • Scherberich, A.1    Tucker, R.P.2    Degen, M.3    Brown-Luedi, M.4    Andres, A.C.5    Chiquet-Ehrismann, R.6
  • 49
    • 0035576810 scopus 로고    scopus 로고
    • Interference of tenascin-C with syndecan-4 binding to fibronectin blocks cell adhesion and stimulates tumor cell proliferation
    • 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
    • (2001) Cancer Res , vol.61 , pp. 8586-8594
    • Huang, W.1    Chiquet-Ehrismann, R.2    Moyano, J.V.3    Garcia-Pardo, A.4    Orend, G.5
  • 50
    • 0038339013 scopus 로고    scopus 로고
    • Tenascin-C blocks cell-cycle progression of anchorage-dependent fibroblasts on fibronectin through inhibition of syndecan-4
    • 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; http://dx.doi.org/10.1038/sj.onc.1206618
    • (2003) Oncogene , vol.22 , pp. 3917-3926
    • Orend, G.1    Huang, W.2    Olayioye, M.A.3    Hynes, N.E.4    Chiquet-Ehrismann, R.5
  • 51
    • 9444297917 scopus 로고    scopus 로고
    • Coregulation of fibronectin signaling and matrix contraction by tenascin-C and syndecan-4
    • Midwood KS, Valenick LV, Hsia HC, Schwarzbauer JE. Coregulation of fibronectin signaling and matrix contraction by tenascin-C and syndecan-4. Mol Biol Cell 2004; 15:5670-7; http://dx.doi.org/10.1091/mbc.E04-08-0759
    • (2004) Mol Biol Cell , vol.15 , pp. 5670-5677
    • Midwood, K.S.1    Valenick, L.V.2    Hsia, H.C.3    Schwarzbauer, J.E.4
  • 52
    • 84903467700 scopus 로고    scopus 로고
    • 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 a5b1
    • 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 a5b1. J Biol Chem 2014; 289:17699-708; http://dx.doi.org/10.1074/jbc.M113.546622
    • (2014) J Biol Chem , vol.289 , pp. 17699-17708
    • Tanaka, R.1    Seki, Y.2    Saito, Y.3    Kamiya, S.4    Fujita, M.5    Okutsu, H.6    Iyoda, T.7    Takai, T.8    Owaki, T.9    Yajima, H.10
  • 53
    • 0036606644 scopus 로고    scopus 로고
    • Changes in tenascin-C isoform expression in invasive and preinvasive breast disease
    • 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
    • (2002) Cancer Res , vol.62 , pp. 3289-3297
    • Adams, M.1    Jones, J.L.2    Walker, R.A.3    Pringle, J.H.4    Bell, S.C.5
  • 54
    • 0030876608 scopus 로고    scopus 로고
    • Co-expression of tenascin and fibronectin in epithelial and stromal cells of benign lesions and ductal carcinomas in the human breast
    • Yoshida T, Matsumoto EI, 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; http://dx.doi.org/10.1002/(SICI)1096-9896(199708)182:4%3c421::AID-PATH886%3e3.0.CO;2-U
    • (1997) J Pathol , vol.182 , pp. 421-428
    • Yoshida, T.1    Matsumoto, E.I.2    Hanamura, N.3    Kalembeyi, I.4    Katsuta, K.5    Ishihara, A.6    Sakakura, T.7
  • 55
    • 0029112799 scopus 로고
    • Tenascin expression in cancer cells and stroma of human breast cancer and its prognostic significance
    • 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
    • (1995) Clin Cancer Res , vol.1 , pp. 1035-1041
    • Ishihara, A.1    Yoshida, T.2    Tamaki, H.3    Sakakura, T.4
  • 56
    • 0030820152 scopus 로고    scopus 로고
    • Analysis of tenascin mRNA expression in the murine mammary gland from embryogenesis to carcinogenesis: An in situ hybridization study
    • Kalembeyi I, Yoshida T, Iriyama K, Sakakura T. Analysis of tenascin mRNA expression in the murine mammary gland from embryogenesis to carcinogenesis: an in situ hybridization study. Int J Dev Biol 1997; 41:569-73
    • (1997) Int J Dev Biol , vol.41 , pp. 569-573
    • Kalembeyi, I.1    Yoshida, T.2    Iriyama, K.3    Sakakura, T.4
  • 58
    • 0030879730 scopus 로고    scopus 로고
    • Expression of fibronectin and tenascin-C mRNA by myofibroblasts, vascular cells and epithelial cells in human colon adenomas and carcinomas
    • 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; http://dx.doi.org/10.1002/(SICI)1097-0215(19970926)73:1% 3c10::AID-IJC2%3e3.0.CO;2-4
    • (1997) Int J Cancer , vol.73 , pp. 10-15
    • Hanamura, N.1    Yoshida, T.2    Matsumoto, E.3    Kawarada, Y.4    Sakakura, T.5
  • 59
    • 3242664404 scopus 로고    scopus 로고
    • Kosmehl H. MRNA expression and protein distribution of the unspliced tenascin-C isoform in prostatic adenocarcinoma
    • Katenkamp K, Berndt A, Hindermann W, Wunderlich H, Haas KM, Borsi L, Zardi L, Kosmehl H. mRNA expression and protein distribution of the unspliced tenascin-C isoform in prostatic adenocarcinoma. J Pathol 2004; 203:771-9; http://dx.doi.org/10.1002/path.1589
    • (2004) J Pathol , vol.203 , pp. 771-779
    • Katenkamp, K.1    Berndt, A.2    Hindermann, W.3    Wunderlich, H.4    Haas, K.M.5    Borsi, L.6    Zardi, L.7
  • 60
    • 84867855446 scopus 로고    scopus 로고
    • Parenchymal-stromal switching for extracellular matrix production on invasion of oral squamous cell carcinoma
    • Metwaly H, Maruyama S, Yamazaki M, Tsuneki M, Abe T, Jen KY, Cheng J, Saku T. Parenchymal-stromal switching for extracellular matrix production on invasion of oral squamous cell carcinoma. Hum Pathol 2012; 43:1973-81; http://dx.doi.org/10.1016/j.humpath.2012.02.006
    • (2012) Hum Pathol , vol.43 , pp. 1973-1981
    • Metwaly, H.1    Maruyama, S.2    Yamazaki, M.3    Tsuneki, M.4    Abe, T.5    Jen, K.Y.6    Cheng, J.7    Saku, T.8
  • 61
    • 0032693911 scopus 로고    scopus 로고
    • Synthesis and protein distribution of the unspliced large tenascin-C isoform in oral squamous cell carcinoma
    • Hindermann W, Berndt A, Borsi L, Luo XM, 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; http://dx.doi.org/10.1002/(SICI)1096-9896(199912)189:4%3c475:: AID-PATH462%3e3.0.CO;2-V
    • (1999) J Pathol , vol.189 , pp. 475-480
    • Hindermann, W.1    Berndt, A.2    Borsi, L.3    Luo, X.M.4    Hyckel, P.5    Katenkamp, D.6    Kosmehl, H.7
  • 63
    • 0032725357 scopus 로고    scopus 로고
    • Involvement of tenascin-C in proliferation and migration of laryngeal carcinoma cells
    • 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; http://dx.doi.org/10.1007/s004280050433
    • (1999) Virchows Arch , vol.435 , pp. 496-500
    • Yoshida, T.1    Yoshimura, E.2    Numata, H.3    Sakakura, Y.4    Sakakura, T.5
  • 64
    • 0029886136 scopus 로고    scopus 로고
    • Tenascin in human papillomavirus associated lesions of the uterine cervix
    • Pollanen R, Soini Y, Vuopala S, Laara E, Lehto VP. Tenascin in human papillomavirus associated lesions of the uterine cervix. J Clin Pathol 1996; 49:521-3; http://dx.doi.org/10.1136/jcp.49.6.521
    • (1996) J Clin Pathol , vol.49 , pp. 521-523
    • Pollanen, R.1    Soini, Y.2    Vuopala, S.3    Laara, E.4    Lehto, V.P.5
  • 66
    • 0030087965 scopus 로고    scopus 로고
    • Basal layer of epithelium expresses tenascin mRNA during healing of incisional skin wounds
    • Aukhil I, Sahlberg C, Thesleff I. Basal layer of epithelium expresses tenascin mRNA during healing of incisional skin wounds. J Periodontal Res 1996; 31:105-12; http://dx.doi.org/10.1111/j.1600-0765.1996.tb00471.x
    • (1996) J Periodontal Res , vol.31 , pp. 105-112
    • Aukhil, I.1    Sahlberg, C.2    Thesleff, I.3
  • 67
    • 0024382080 scopus 로고
    • Participation of tenascin and transforming growth factor-b in reciprocal epithelial-mesenchymal interactions of MCF7 cells and fibroblasts
    • Chiquet-Ehrismann R, Kalla P, Pearson CA. Participation of tenascin and transforming growth factor-b in reciprocal epithelial-mesenchymal interactions of MCF7 cells and fibroblasts. Cancer Res 1989; 49:4322-5
    • (1989) Cancer Res , vol.49 , pp. 4322-4325
    • Chiquet-Ehrismann, R.1    Kalla, P.2    Pearson, C.A.3
  • 69
    • 0027516317 scopus 로고
    • Induction of tenascin in cancer-cells by interactions with embryonic mesenchyme mediated by a diffusible factor
    • 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; 104:289-96
    • (1993) J Cell Sci , vol.104 , pp. 289-296
    • Hiraiwa, N.1    Kida, H.2    Sakakura, T.3    Kusakabe, M.4
  • 71
    • 0026457220 scopus 로고
    • Expression of different tenascin isoforms in normal, hyperplastic and neoplastic human breast tissues
    • Borsi L, Carnemolla B, Nicolo G, Spina B, Tanara G, Zardi L. Expression of different tenascin isoforms in normal, hyperplastic and neoplastic human breast tissues. Int J Cancer 1992; 52:688-92; http://dx.doi.org/10.1002/ijc.2910520504
    • (1992) Int J Cancer , vol.52 , pp. 688-692
    • Borsi, L.1    Carnemolla, B.2    Nicolo, G.3    Spina, B.4    Tanara, G.5    Zardi, L.6
  • 78
    • 79959659734 scopus 로고    scopus 로고
    • Tenascin-C enhances pancreatic cancer cell growth and motility and affects cell adhesion through activation of the integrin pathway
    • Paron I, Berchtold S, Vörös J, Shamarla M, Erkan M, Höfler H, Esposito I. Tenascin-C enhances pancreatic cancer cell growth and motility and affects cell adhesion through activation of the integrin pathway. PLoS One 2011; 6:e21684
    • (2011) Plos One , vol.6
    • Paron, I.1    Berchtold, S.2    Vörös, J.3    Shamarla, M.4    Erkan, M.5    Höfler, H.6    Esposito, I.7
  • 79
    • 0028908403 scopus 로고
    • Different susceptibility of small and large human tenascin-c isoforms to degradation by matrix metalloproteinases
    • 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
    • (1995) J Biol Chem , vol.270 , pp. 8650-8654
    • Siri, A.1    Knauper, V.2    Veirana, N.3    Caocci, F.4    Murphy, G.5    Zardi, L.6
  • 83
    • 70450198396 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transitions in development and disease
    • Thiery JP, Acloque H, Huang RY, Nieto MA. Epithelial-mesenchymal transitions in development and disease. Cell 2009; 139:871-90
    • (2009) Cell , vol.139 , pp. 871-890
    • Thiery, J.P.1    Acloque, H.2    Huang, R.Y.3    Nieto, M.A.4
  • 84
    • 79951841887 scopus 로고    scopus 로고
    • Tenascin C induces epithelial-mesenchymal transition-like change accompanied by SRC activation and focal adhesion kinase phosphorylation in human breast cancer cells
    • 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
    • (2011) Am J Pathol , vol.178 , pp. 754-763
    • Nagaharu, K.1    Zhang, X.2    Yoshida, T.3    Katoh, D.4    Hanamura, N.5    Kozuka, Y.6    Ogawa, T.7    Shiraishi, T.8    Imanaka-Yoshida, K.9
  • 87
    • 0035058769 scopus 로고    scopus 로고
    • The de-adhesive activity of matricellular proteins: Is intermediate cell adhesion an adaptive state?
    • Murphy-Ullrich JE. The de-adhesive activity of matricellular proteins: is intermediate cell adhesion an adaptive state? J Clin Invest 2001; 107:785-90
    • (2001) J Clin Invest , vol.107 , pp. 785-790
    • Murphy-Ullrich, J.E.1
  • 88
    • 33748476449 scopus 로고    scopus 로고
    • Glioma-produced extracellular matrix influences brain tumor tropism of human neural stem cells
    • Ziu M, Schmidt NO, Cargioli TG, Aboody KS, Black PM, Carroll RS. Glioma-produced extracellular matrix influences brain tumor tropism of human neural stem cells. J Neurooncol 2006; 79:125-33
    • (2006) J Neurooncol , vol.79 , pp. 125-133
    • Ziu, M.1    Schmidt, N.O.2    Cargioli, T.G.3    Aboody, K.S.4    Black, P.M.5    Carroll, R.S.6
  • 91
    • 67650502739 scopus 로고    scopus 로고
    • Tenascin-C is an endogenous activator of Tolllike receptor 4 that is essential for maintaining inflammation in arthritic joint disease
    • 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 Tolllike receptor 4 that is essential for maintaining inflammation in arthritic joint disease. Nat Med 2009; 15:774-80; http://dx.doi.org/10.1038/nm.1987
    • (2009) Nat Med , vol.15 , pp. 774-780
    • Midwood, K.1    Sacre, S.2    Piccinini, A.M.3    Inglis, J.4    Trebaul, A.5    Chan, E.6    Drexler, S.7    Sofat, N.8    Kashiwagi, M.9    Orend, G.10
  • 92
    • 84868202071 scopus 로고    scopus 로고
    • Stromal biomarkers in breast cancer development and progression
    • Rudnick JA, Kuperwasser C. Stromal biomarkers in breast cancer development and progression. Clin Exp Metastasis 2012; 29:663-72; http://dx.doi.org/10.1007/s10585-012-9499-8
    • (2012) Clin Exp Metastasis , vol.29 , pp. 663-672
    • Rudnick, J.A.1    Kuperwasser, C.2


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