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Volumn 7, Issue 21, 2016, Pages 30659-30677

Palmitoylated claudin7 captured in glycolipid-enriched membrane microdomains promotes metastasis via associated transmembrane and cytosolic molecules

Author keywords

Claudin7 palmitoylation; Complex dependent bioactivity; Glycolipid enriched membrane microdomains; Metastasis

Indexed keywords

ALPHA6BETA4 INTEGRIN; CISPLATIN; CLAUDIN 7; CYTOKERATIN 2; EZRIN; GLYCOGEN SYNTHASE KINASE 3BETA; GLYCOLIPID; MATRIX METALLOPROTEINASE 14; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PROTEIN KINASE B; UROKINASE RECEPTOR; CLAUDIN; CLDN7 PROTEIN, RAT; MEMBRANE PROTEIN; TRANSCRIPTION FACTOR;

EID: 84971578053     PISSN: None     EISSN: 19492553     Source Type: Journal    
DOI: 10.18632/oncotarget.8928     Document Type: Article
Times cited : (25)

References (100)
  • 2
    • 84872066969 scopus 로고    scopus 로고
    • Current concepts and novel targets in advanced pancreatic cancer
    • Michl P, Gress TM. Current concepts and novel targets in advanced pancreatic cancer. Gut. 2013; 62:317-326
    • (2013) Gut , vol.62 , pp. 317-326
    • Michl, P.1    Gress, T.M.2
  • 3
    • 84906962169 scopus 로고    scopus 로고
    • Altered gene products involved in the malignant reprogramming of cancer stem/progenitor cells and multitargeted therapies
    • Mimeault M, Batra SK. Altered gene products involved in the malignant reprogramming of cancer stem/progenitor cells and multitargeted therapies. Mol Aspects Med. 2014; 39:3-32
    • (2014) Mol Aspects Med , vol.39 , pp. 3-32
    • Mimeault, M.1    Batra, S.K.2
  • 5
    • 84892949820 scopus 로고    scopus 로고
    • Overview of current standpoints in profiling of circulating tumor cells
    • Kim K, Lee KH, Lee J, Choi J. Overview of current standpoints in profiling of circulating tumor cells. Arch Pharm Res. 2014; 37:88-95
    • (2014) Arch Pharm Res , vol.37 , pp. 88-95
    • Kim, K.1    Lee, K.H.2    Lee, J.3    Choi, J.4
  • 6
    • 79953042645 scopus 로고    scopus 로고
    • CD44: can a cancer-initiating cell profit from an abundantly expressed molecule?
    • Zöller M. CD44: can a cancer-initiating cell profit from an abundantly expressed molecule? Nat Rev Cancer. 2011; 11:254-267
    • (2011) Nat Rev Cancer , vol.11 , pp. 254-267
    • Zöller, M.1
  • 7
    • 84925031798 scopus 로고    scopus 로고
    • Cancer stem cells: perspectives for therapeutic targeting
    • Maccalli C, De Maria R. Cancer stem cells: perspectives for therapeutic targeting. Cancer Immunol Immunother. 2015; 64:91-97
    • (2015) Cancer Immunol Immunother , vol.64 , pp. 91-97
    • Maccalli, C.1    De Maria, R.2
  • 8
    • 82255175072 scopus 로고    scopus 로고
    • Lessons from common markers of tumor-initiating cells in solid cancers
    • Gires O. Lessons from common markers of tumor-initiating cells in solid cancers. Cell Mol Life Sci. 2011; 68:4009-4022
    • (2011) Cell Mol Life Sci , vol.68 , pp. 4009-4022
    • Gires, O.1
  • 9
    • 84878870719 scopus 로고    scopus 로고
    • EpCAM-associated claudin-7 supports lymphatic spread and drug resistance in rat pancreatic cancer
    • Thuma F, Zöller M. EpCAM-associated claudin-7 supports lymphatic spread and drug resistance in rat pancreatic cancer. Int J Cancer. 2013; 133:855-866
    • (2013) Int J Cancer , vol.133 , pp. 855-866
    • Thuma, F.1    Zöller, M.2
  • 10
    • 84922997111 scopus 로고    scopus 로고
    • Claudin-7 promotes the epithelial-mesenchymal transition in human colorectal cancer
    • Philip R, Heiler S, Mu W, Büchler MW, Zöller M, Thuma F. Claudin-7 promotes the epithelial-mesenchymal transition in human colorectal cancer. Oncotarget. 2015; 6:2046-2063. doi: 10.18632/oncotarget.2858
    • (2015) Oncotarget , vol.6 , pp. 2046-2063
    • Philip, R.1    Heiler, S.2    Mu, W.3    Büchler, M.W.4    Zöller, M.5    Thuma, F.6
  • 11
    • 0031741390 scopus 로고    scopus 로고
    • Overcoming barriers in the study of tight junction functions: from occludin to claudin
    • Tsukita S, Furuse M. Overcoming barriers in the study of tight junction functions: from occludin to claudin. Genes Cells. 1998; 3:569-573
    • (1998) Genes Cells , vol.3 , pp. 569-573
    • Tsukita, S.1    Furuse, M.2
  • 14
    • 0037128938 scopus 로고    scopus 로고
    • Claudin-based tight junctions are crucial for the mammalian epidermal barrier: a lesson from claudin-1-deficient mice
    • Furuse M, Hata M, Furuse K, Yoshida Y, Haratake A, Sugitani Y, Noda T, Kubo A, Tsukita S. Claudin-based tight junctions are crucial for the mammalian epidermal barrier: a lesson from claudin-1-deficient mice. J Cell Biol. 2002; 156:1099-1111
    • (2002) J Cell Biol , vol.156 , pp. 1099-1111
    • Furuse, M.1    Hata, M.2    Furuse, K.3    Yoshida, Y.4    Haratake, A.5    Sugitani, Y.6    Noda, T.7    Kubo, A.8    Tsukita, S.9
  • 16
    • 84941349580 scopus 로고    scopus 로고
    • Intestinal deletion of Claudin-7 enhances paracellular organic solute flux and initiates colonic inflammation in mice
    • Tanaka H, Takechi M, Kiyonari H, Shioi G, Tamura A, Tsukita S. Intestinal deletion of Claudin-7 enhances paracellular organic solute flux and initiates colonic inflammation in mice. Gut. 2015; 64:1529-1538
    • (2015) Gut , vol.64 , pp. 1529-1538
    • Tanaka, H.1    Takechi, M.2    Kiyonari, H.3    Shioi, G.4    Tamura, A.5    Tsukita, S.6
  • 18
    • 84887393202 scopus 로고    scopus 로고
    • The claudin family of proteins in human malignancy: a clinical perspective
    • Ding L, Lu Z, Lu Q, Chen YH. The claudin family of proteins in human malignancy: a clinical perspective. Cancer Manag Res. 2013; 5:367-375
    • (2013) Cancer Manag Res , vol.5 , pp. 367-375
    • Ding, L.1    Lu, Z.2    Lu, Q.3    Chen, Y.H.4
  • 19
    • 84913551633 scopus 로고    scopus 로고
    • Claudin interactions in and out of the tight junction
    • Van Itallie CM, Anderson JM. Claudin interactions in and out of the tight junction. Tissue Barriers. 2013; 1: e25247
    • (2013) Tissue Barriers , vol.1
    • Van Itallie, C.M.1    Anderson, J.M.2
  • 20
    • 67650348496 scopus 로고    scopus 로고
    • Regulation and roles for claudin-family tight junction proteins
    • Findley MK, Koval M. Regulation and roles for claudin-family tight junction proteins. IUBMB Life. 2009; 61:431-437
    • (2009) IUBMB Life , vol.61 , pp. 431-437
    • Findley, M.K.1    Koval, M.2
  • 21
    • 33750142010 scopus 로고    scopus 로고
    • The tight junction proteins claudin-7 and-8 display a different subcellular localization at Henle's loops and collecting ducts of rabbit kidney
    • Gonzalez-Mariscal L, Namorado Mdel C, Martin D, Sierra G, Reyes JL. The tight junction proteins claudin-7 and-8 display a different subcellular localization at Henle's loops and collecting ducts of rabbit kidney. Nephrol Dial Transplant. 2006; 21:2391-2398
    • (2006) Nephrol Dial Transplant , vol.21 , pp. 2391-2398
    • Gonzalez-Mariscal, L.1    Namorado Mdel, C.2    Martin, D.3    Sierra, G.4    Reyes, J.L.5
  • 22
  • 23
    • 84935906852 scopus 로고    scopus 로고
    • A non-tight junction function of claudin-7-Interaction with integrin signaling in suppressing lung cancer cell proliferation and detachment
    • Lu Z, Kim do H, Fan J, Lu Q, Verbanac K, Ding L, Renegar R, Chen YH. A non-tight junction function of claudin-7-Interaction with integrin signaling in suppressing lung cancer cell proliferation and detachment. Mol Cancer. 2015; 14:120
    • (2015) Mol Cancer , vol.14 , pp. 120
    • Lu, Z.1    Kim do, H.2    Fan, J.3    Lu, Q.4    Verbanac, K.5    Ding, L.6    Renegar, R.7    Chen, Y.H.8
  • 24
    • 2442689137 scopus 로고    scopus 로고
    • Expression of claudin-7 and-8 along the mouse nephron
    • Li WY, Huey CL, Yu AS. Expression of claudin-7 and-8 along the mouse nephron. Am J Physiol Renal Physiol. 2004; 286:F1063-1071
    • (2004) Am J Physiol Renal Physiol , vol.286 , pp. F1063-F1071
    • Li, W.Y.1    Huey, C.L.2    Yu, A.S.3
  • 25
    • 22544434673 scopus 로고    scopus 로고
    • Phosphorylation of claudin-3 at threonine 192 by cAMP-dependent protein kinase regulates tight junction barrier function in ovarian cancer cells
    • D'Souza T, Agarwal R, Morin PJ. Phosphorylation of claudin-3 at threonine 192 by cAMP-dependent protein kinase regulates tight junction barrier function in ovarian cancer cells. J Biol Chem. 2005; 280:26233-26240
    • (2005) J Biol Chem , vol.280 , pp. 26233-26240
    • D'Souza, T.1    Agarwal, R.2    Morin, P.J.3
  • 27
    • 84859992839 scopus 로고    scopus 로고
    • Myosin light chain kinase mediates intestinal barrier disruption following burn injury
    • Chen C, Wang P, Su Q, Wang S, Wang F. Myosin light chain kinase mediates intestinal barrier disruption following burn injury. PLoS One. 2012; 7:e34946
    • (2012) PLoS One , vol.7
    • Chen, C.1    Wang, P.2    Su, Q.3    Wang, S.4    Wang, F.5
  • 28
    • 84879499448 scopus 로고    scopus 로고
    • Claudin-2 regulates colorectal inflammation via myosin light chain kinase-dependent signaling
    • Nishida M, Yoshida M, Nishiumi S, Furuse M, Azuma T. Claudin-2 regulates colorectal inflammation via myosin light chain kinase-dependent signaling. Dig Dis Sci. 2013; 58:1546-1559
    • (2013) Dig Dis Sci , vol.58 , pp. 1546-1559
    • Nishida, M.1    Yoshida, M.2    Nishiumi, S.3    Furuse, M.4    Azuma, T.5
  • 29
    • 36849032329 scopus 로고    scopus 로고
    • Claudin-16 is directly phosphorylated by protein kinase A independently of a vasodilator-stimulated phosphoprotein-mediated pathway
    • Ikari A, Ito M, Okude C, Sawada H, Harada H, Degawa M, Sakai H, Takahashi T, Sugatani J, Miwa M. Claudin-16 is directly phosphorylated by protein kinase A independently of a vasodilator-stimulated phosphoprotein-mediated pathway. J Cell Physiol. 2008; 214:221-229
    • (2008) J Cell Physiol , vol.214 , pp. 221-229
    • Ikari, A.1    Ito, M.2    Okude, C.3    Sawada, H.4    Harada, H.5    Degawa, M.6    Sakai, H.7    Takahashi, T.8    Sugatani, J.9    Miwa, M.10
  • 30
    • 83255189411 scopus 로고    scopus 로고
    • Alteration in intestine tight junction protein phosphorylation and apoptosis is associated with increase in IL-18 levels following alcohol intoxication and burn injury
    • Li X, Akhtar S, Choudhry MA. Alteration in intestine tight junction protein phosphorylation and apoptosis is associated with increase in IL-18 levels following alcohol intoxication and burn injury. Biochim Biophys Acta. 2012; 1822:196-203
    • (2012) Biochim Biophys Acta , vol.1822 , pp. 196-203
    • Li, X.1    Akhtar, S.2    Choudhry, M.A.3
  • 31
    • 84862834603 scopus 로고    scopus 로고
    • Tight junctions on the move: molecular mechanisms for epithelial barrier regulation
    • Shen L. Tight junctions on the move: molecular mechanisms for epithelial barrier regulation. Ann N Y Acad Sci. 2012; 1258:9-18
    • (2012) Ann N Y Acad Sci , vol.1258 , pp. 9-18
    • Shen, L.1
  • 32
    • 78650180636 scopus 로고    scopus 로고
    • Protein kinase C activation has distinct effects on the localization, phosphorylation and detergent solubility of the claudin protein family in tight and leaky epithelial cells
    • Sjö A, Magnusson KE, Peterson KH. Protein kinase C activation has distinct effects on the localization, phosphorylation and detergent solubility of the claudin protein family in tight and leaky epithelial cells. J Membr Biol. 2010; 236:181-189
    • (2010) J Membr Biol , vol.236 , pp. 181-189
    • Sjö, A.1    Magnusson, K.E.2    Peterson, K.H.3
  • 33
    • 84931081032 scopus 로고    scopus 로고
    • The importance of claudin-7 palmitoylation on membrane subdomain localization and metastasis-promoting activities
    • Heiler S, Mu W, Zöller M, Thuma F. The importance of claudin-7 palmitoylation on membrane subdomain localization and metastasis-promoting activities. Cell Commun Signal. 2015; 13:29
    • (2015) Cell Commun Signal , vol.13 , pp. 29
    • Heiler, S.1    Mu, W.2    Zöller, M.3    Thuma, F.4
  • 35
    • 77955033375 scopus 로고    scopus 로고
    • Greasing their way: lipid modifications determine protein association with membrane rafts
    • Levental I, Grzybek M, Simons K. Greasing their way: lipid modifications determine protein association with membrane rafts. Biochemistry. 2010; 49:6305-6316
    • (2010) Biochemistry , vol.49 , pp. 6305-6316
    • Levental, I.1    Grzybek, M.2    Simons, K.3
  • 36
    • 84893612959 scopus 로고    scopus 로고
    • Palmitoylated transmembrane adaptor proteins in leukocyte signaling
    • Stepanek O, Draber P, Horejsi V. Palmitoylated transmembrane adaptor proteins in leukocyte signaling. Cell Signal. 2014; 26:895-902
    • (2014) Cell Signal , vol.26 , pp. 895-902
    • Stepanek, O.1    Draber, P.2    Horejsi, V.3
  • 37
    • 84892178225 scopus 로고    scopus 로고
    • Interaction of membrane/lipid rafts with the cytoskeleton: impact on signaling and function: membrane/lipid rafts, mediators of cytoskeletal arrangement and cell signaling
    • Head BP, Patel HH, Insel PA. Interaction of membrane/lipid rafts with the cytoskeleton: impact on signaling and function: membrane/lipid rafts, mediators of cytoskeletal arrangement and cell signaling. Biochim Biophys Acta. 2014; 1838:532-545
    • (2014) Biochim Biophys Acta , vol.1838 , pp. 532-545
    • Head, B.P.1    Patel, H.H.2    Insel, P.A.3
  • 38
    • 84920916855 scopus 로고    scopus 로고
    • Lipid rafts as major platforms for signaling regulation in cancer
    • Mollinedo F, Gajate C. Lipid rafts as major platforms for signaling regulation in cancer. Adv Biol Regul. 2015 ; 57:130-146
    • (2015) Adv Biol Regul , vol.57 , pp. 130-146
    • Mollinedo, F.1    Gajate, C.2
  • 39
    • 77957895194 scopus 로고    scopus 로고
    • Lipid rafts, caveolae, and their endocytosis
    • Lajoie P, Nabi IR. Lipid rafts, caveolae, and their endocytosis. Int Rev Cell Mol Biol. 2010; 282:135-163
    • (2010) Int Rev Cell Mol Biol , vol.282 , pp. 135-163
    • Lajoie, P.1    Nabi, I.R.2
  • 41
    • 57749169272 scopus 로고    scopus 로고
    • Tetraspanins: push and pull in suppressing and promoting metastasis
    • Zöller M. Tetraspanins: push and pull in suppressing and promoting metastasis. Nat Rev Cancer. 2009; 9:40-55
    • (2009) Nat Rev Cancer , vol.9 , pp. 40-55
    • Zöller, M.1
  • 42
    • 84941710002 scopus 로고    scopus 로고
    • Cell membrane fluid-mosaic structure and cancer metastasis
    • Nicolson GL. Cell membrane fluid-mosaic structure and cancer metastasis. Cancer Res. 2015; 75:1169-1176
    • (2015) Cancer Res , vol.75 , pp. 1169-1176
    • Nicolson, G.L.1
  • 43
    • 84919468543 scopus 로고    scopus 로고
    • Tetraspanins in extracellular vesicle formation and function
    • Andreu Z, Yáñez-Mó M. Tetraspanins in extracellular vesicle formation and function. Front Immunol. 2014; 5:442
    • (2014) Front Immunol , vol.5 , pp. 442
    • Andreu, Z.1    Yáñez-Mó, M.2
  • 44
    • 77955349312 scopus 로고    scopus 로고
    • Claudin family of proteins and cancer: an overview
    • Singh AB, Sharma A, Dhawan P. Claudin family of proteins and cancer: an overview. J Oncol. 2010; 2010:541957
    • (2010) J Oncol , vol.2010
    • Singh, A.B.1    Sharma, A.2    Dhawan, P.3
  • 45
    • 84884240720 scopus 로고    scopus 로고
    • Emerging roles of claudins in human cancer
    • Kwon MJ. Emerging roles of claudins in human cancer. Int J Mol Sci. 2013; 14:18148-18180
    • (2013) Int J Mol Sci , vol.14 , pp. 18148-18180
    • Kwon, M.J.1
  • 46
    • 79955009775 scopus 로고    scopus 로고
    • The Claudin family and its role in cancer and metastasis
    • Escudero-Esparza A, Jiang WG, Martin TA. The Claudin family and its role in cancer and metastasis. Front Biosci. 2011; 16:1069-1083
    • (2011) Front Biosci , vol.16 , pp. 1069-1083
    • Escudero-Esparza, A.1    Jiang, W.G.2    Martin, T.A.3
  • 48
    • 84860367617 scopus 로고    scopus 로고
    • EpCAM and its potential role in tumor-initiating cells
    • Imrich S, Hachmeister M, Gires O. EpCAM and its potential role in tumor-initiating cells. Cell Adh Migr. 2012; 6:30-38
    • (2012) Cell Adh Migr , vol.6 , pp. 30-38
    • Imrich, S.1    Hachmeister, M.2    Gires, O.3
  • 51
    • 84876914835 scopus 로고    scopus 로고
    • Epithelial cell adhesion molecule (EpCAM) regulates claudin dynamics and tight junctions
    • Wu CJ, Mannan P, Lu M, Udey MC. Epithelial cell adhesion molecule (EpCAM) regulates claudin dynamics and tight junctions. J Biol Chem. 2013; 288:12253-12268
    • (2013) J Biol Chem , vol.288 , pp. 12253-12268
    • Wu, C.J.1    Mannan, P.2    Lu, M.3    Udey, M.C.4
  • 52
    • 84899622480 scopus 로고    scopus 로고
    • Coexpression of EpCAM, CD44 variant isoforms and claudin-7 in anaplastic thyroid carcinoma
    • Okada T, Nakamura T, Watanabe T, Onoda N, Ashida A, Okuyama R, Ito K. Coexpression of EpCAM, CD44 variant isoforms and claudin-7 in anaplastic thyroid carcinoma. PLoS One. 2014; 9:e94487
    • (2014) PLoS One , vol.9
    • Okada, T.1    Nakamura, T.2    Watanabe, T.3    Onoda, N.4    Ashida, A.5    Okuyama, R.6    Ito, K.7
  • 54
    • 36348991571 scopus 로고    scopus 로고
    • Activation of hepatic stem cell marker EpCAM by Wnt-beta-catenin signaling in hepatocellular carcinoma
    • Yamashita T, Budhu A, Forgues M, Wang XW. Activation of hepatic stem cell marker EpCAM by Wnt-beta-catenin signaling in hepatocellular carcinoma. Cancer Res. 2007; 67:10831-10839
    • (2007) Cancer Res , vol.67 , pp. 10831-10839
    • Yamashita, T.1    Budhu, A.2    Forgues, M.3    Wang, X.W.4
  • 55
    • 78049514693 scopus 로고    scopus 로고
    • The tumor-associated EpCAM regulates morphogenetic movements through intracellular signaling
    • Maghzal N, Vogt E, Reintsch W, Fraser JS, Fagotto F. The tumor-associated EpCAM regulates morphogenetic movements through intracellular signaling. J Cell Biol. 2010; 191:645-659
    • (2010) J Cell Biol , vol.191 , pp. 645-659
    • Maghzal, N.1    Vogt, E.2    Reintsch, W.3    Fraser, J.S.4    Fagotto, F.5
  • 57
    • 59149084182 scopus 로고    scopus 로고
    • Transcriptional repression of epithelial cell adhesion molecule contributes to p53 control of breast cancer invasion
    • Sankpal NV, Willman MW, Fleming TP, Mayfield JD, Gillanders WE. Transcriptional repression of epithelial cell adhesion molecule contributes to p53 control of breast cancer invasion. Cancer Res. 2009; 69:753-757
    • (2009) Cancer Res , vol.69 , pp. 753-757
    • Sankpal, N.V.1    Willman, M.W.2    Fleming, T.P.3    Mayfield, J.D.4    Gillanders, W.E.5
  • 59
    • 84869225084 scopus 로고    scopus 로고
    • Epithelial Cell Adhesion Molecule Regulates Tumor Initiation and Tumorigenesis via Activating Reprogramming Factors and Epithelial-Mesenchymal Transition Genes Expression in Colon Cancer
    • Lin CW, Liao MY, Lin WW, Wang YP, Lu TY, Wu HC. Epithelial Cell Adhesion Molecule Regulates Tumor Initiation and Tumorigenesis via Activating Reprogramming Factors and Epithelial-Mesenchymal Transition Genes Expression in Colon Cancer. J Biol Chem. 2012; 287: 39449-39459
    • (2012) J Biol Chem , vol.287 , pp. 39449-39459
    • Lin, C.W.1    Liao, M.Y.2    Lin, W.W.3    Wang, Y.P.4    Lu, T.Y.5    Wu, H.C.6
  • 60
    • 39549111466 scopus 로고    scopus 로고
    • Identification of adult hepatic progenitor cells capable of repopulating injured rat liver
    • Yovchev MI, Grozdanov PN, Zhou H, Racherla H, Guha C, Dabeva MD. Identification of adult hepatic progenitor cells capable of repopulating injured rat liver. Hepatology. 2008; 47:636-647
    • (2008) Hepatology , vol.47 , pp. 636-647
    • Yovchev, M.I.1    Grozdanov, P.N.2    Zhou, H.3    Racherla, H.4    Guha, C.5    Dabeva, M.D.6
  • 61
    • 84867142054 scopus 로고    scopus 로고
    • EpCAM contributes to formation of functional tight junction in the intestinal epithelium by recruiting claudin proteins
    • Lei Z, Maeda T, Tamura A, Nakamura T, Yamazaki Y, Shiratori H, Yashiro K, Tsukita S, Hamada H. EpCAM contributes to formation of functional tight junction in the intestinal epithelium by recruiting claudin proteins. Dev Biol. 2012; 371:136-145
    • (2012) Dev Biol , vol.371 , pp. 136-145
    • Lei, Z.1    Maeda, T.2    Tamura, A.3    Nakamura, T.4    Yamazaki, Y.5    Shiratori, H.6    Yashiro, K.7    Tsukita, S.8    Hamada, H.9
  • 62
    • 0020521439 scopus 로고
    • Characterization of BSp73, a spontaneous rat tumor and its in vivo selected variants showing different metastasizing capacities
    • Matzku S, Komitowski D, Mildenberger M, Zöller M. Characterization of BSp73, a spontaneous rat tumor and its in vivo selected variants showing different metastasizing capacities. Invasion Metastasis. 1983; 3:109-123
    • (1983) Invasion Metastasis , vol.3 , pp. 109-123
    • Matzku, S.1    Komitowski, D.2    Mildenberger, M.3    Zöller, M.4
  • 63
    • 79955541291 scopus 로고    scopus 로고
    • CD44v6 coordinates tumor matrix-triggered motility and apoptosis resistance
    • Jung T, Gross W, Zöller M. CD44v6 coordinates tumor matrix-triggered motility and apoptosis resistance. J Biol Chem. 2011; 286:15862-15874
    • (2011) J Biol Chem , vol.286 , pp. 15862-15874
    • Jung, T.1    Gross, W.2    Zöller, M.3
  • 64
    • 84881105192 scopus 로고    scopus 로고
    • Tspan8 and CD151 promote metastasis by distinct mechanisms
    • Yue S, Mu W, Zöller M. Tspan8 and CD151 promote metastasis by distinct mechanisms. Eur J Cancer. 2013; 49:2934-2948
    • (2013) Eur J Cancer , vol.49 , pp. 2934-2948
    • Yue, S.1    Mu, W.2    Zöller, M.3
  • 65
    • 84963937412 scopus 로고    scopus 로고
    • Kinases, tails and more: regulation of PTEN function by phosphorylation
    • Fragoso R, Barata JT. Kinases, tails and more: regulation of PTEN function by phosphorylation. Methods. 2015; 77-78:75-81
    • (2015) Methods , vol.77-78 , pp. 75-81
    • Fragoso, R.1    Barata, J.T.2
  • 66
    • 84926251200 scopus 로고    scopus 로고
    • Outsmart tumor exosomes to steal the cancer initiating cell its niche
    • Thuma F, Zöller M. Outsmart tumor exosomes to steal the cancer initiating cell its niche. Semin Cancer Biol. 2014; 28:39-50
    • (2014) Semin Cancer Biol , vol.28 , pp. 39-50
    • Thuma, F.1    Zöller, M.2
  • 67
    • 84863439963 scopus 로고    scopus 로고
    • Toward tailored exosomes: the exosomal tetraspanin web contributes to target cell selection
    • Rana S, Yue S, Stadel D, Zöller M. Toward tailored exosomes: the exosomal tetraspanin web contributes to target cell selection. Int J Biochem Cell Biol. 2012; 44:1574-1584
    • (2012) Int J Biochem Cell Biol , vol.44 , pp. 1574-1584
    • Rana, S.1    Yue, S.2    Stadel, D.3    Zöller, M.4
  • 68
    • 84912105184 scopus 로고    scopus 로고
    • Tight junction, selective permeability, and related diseases
    • Krug SM, Schulzke JD, Fromm M. Tight junction, selective permeability, and related diseases. Semin Cell Dev Biol. 2014; 36:166-176
    • (2014) Semin Cell Dev Biol , vol.36 , pp. 166-176
    • Krug, S.M.1    Schulzke, J.D.2    Fromm, M.3
  • 70
    • 84906317288 scopus 로고    scopus 로고
    • The role of claudin-1 and claudin-7 in cervical tumorigenesis
    • Cunniffe C, Brankin B, Lambkin H, Ryan F. The role of claudin-1 and claudin-7 in cervical tumorigenesis. Anticancer Res. 2014; 34:2851-2857
    • (2014) Anticancer Res , vol.34 , pp. 2851-2857
    • Cunniffe, C.1    Brankin, B.2    Lambkin, H.3    Ryan, F.4
  • 71
    • 84994106751 scopus 로고    scopus 로고
    • Computational analysis identifies invasion-associated genes in pituitary adenomas
    • Cao C, Wang W, Ma C, Jiang P. Computational analysis identifies invasion-associated genes in pituitary adenomas. Mol Med Rep. 2015; 12:1977-1982
    • (2015) Mol Med Rep , vol.12 , pp. 1977-1982
    • Cao, C.1    Wang, W.2    Ma, C.3    Jiang, P.4
  • 73
    • 84899622480 scopus 로고    scopus 로고
    • Coexpression of EpCAM, CD44 variant isoforms and claudin-7 in anaplastic thyroid carcinoma
    • Okada T, Nakamura T, Watanabe T, Onoda N, Ashida A, Okuyama R, Ito K. Coexpression of EpCAM, CD44 variant isoforms and claudin-7 in anaplastic thyroid carcinoma. PLoS One. 2014; 9:e94487
    • (2014) PLoS One , vol.9
    • Okada, T.1    Nakamura, T.2    Watanabe, T.3    Onoda, N.4    Ashida, A.5    Okuyama, R.6    Ito, K.7
  • 75
    • 84893973181 scopus 로고    scopus 로고
    • Expression of claudin-7 and loss of claudin-18 correlate with poor prognosis in gastric cancer
    • Jun KH, Kim JH, Jung JH, Choi HJ, Chin HM. Expression of claudin-7 and loss of claudin-18 correlate with poor prognosis in gastric cancer. Int J Surg. 2014; 12:156-162
    • (2014) Int J Surg , vol.12 , pp. 156-162
    • Jun, K.H.1    Kim, J.H.2    Jung, J.H.3    Choi, H.J.4    Chin, H.M.5
  • 76
    • 84862834603 scopus 로고    scopus 로고
    • Tight junctions on the move: molecular mechanisms for epithelial barrier regulation
    • Shen L. Tight junctions on the move: molecular mechanisms for epithelial barrier regulation. Ann N Y Acad Sci. 2012; 1258:9-18
    • (2012) Ann N Y Acad Sci , vol.1258 , pp. 9-18
    • Shen, L.1
  • 77
    • 84935906852 scopus 로고    scopus 로고
    • A non-tight junction function of claudin-7-Interaction with integrin signaling in suppressing lung cancer cell proliferation and detachment
    • Lu Z, Kim do H, Fan J, Lu Q, Verbanac K, Ding L, Renegar R, Chen YH. A non-tight junction function of claudin-7-Interaction with integrin signaling in suppressing lung cancer cell proliferation and detachment. Mol Cancer. 2015; 14:120
    • (2015) Mol Cancer , vol.14 , pp. 120
    • Lu, Z.1    Kim do, H.2    Fan, J.3    Lu, Q.4    Verbanac, K.5    Ding, L.6    Renegar, R.7    Chen, Y.H.8
  • 79
    • 84929143197 scopus 로고    scopus 로고
    • Downregulation of 5-HT1B and 5-HT1D receptors inhibits proliferation, clonogenicity and invasion of human pancreatic cancer cells
    • Gurbuz N, Ashour AA, Alpay SN, Ozpolat B. Downregulation of 5-HT1B and 5-HT1D receptors inhibits proliferation, clonogenicity and invasion of human pancreatic cancer cells. PLoS One. 2014; 9: e110067
    • (2014) PLoS One , vol.9
    • Gurbuz, N.1    Ashour, A.A.2    Alpay, S.N.3    Ozpolat, B.4
  • 80
    • 84878880586 scopus 로고    scopus 로고
    • The Extracellular Matrix Metalloproteinase Inducer (EMMPRIN, CD147)-a potential novel target in atherothrombosis prevention?
    • Joghetaei N, Stein A, Byrne RA, Schulz C, King L, May AE, Schmidt R. The Extracellular Matrix Metalloproteinase Inducer (EMMPRIN, CD147)-a potential novel target in atherothrombosis prevention? Thromb Res. 2013; 131:474-480
    • (2013) Thromb Res , vol.131 , pp. 474-480
    • Joghetaei, N.1    Stein, A.2    Byrne, R.A.3    Schulz, C.4    King, L.5    May, A.E.6    Schmidt, R.7
  • 82
    • 84907501988 scopus 로고    scopus 로고
    • Signaling mechanisms of the epithelial-mesenchymal transition
    • Gonzalez DM, Medici D. Signaling mechanisms of the epithelial-mesenchymal transition. Sci Signal. 2014; 7:re8
    • (2014) Sci Signal , vol.7
    • Gonzalez, D.M.1    Medici, D.2
  • 83
    • 68549106083 scopus 로고    scopus 로고
    • E-cadherin, betacatenin, and ZEB1 in malignant progression of cancer
    • Schmalhofer O, Brabletz S, Brabletz T. E-cadherin, betacatenin, and ZEB1 in malignant progression of cancer. Cancer Metastasis Rev. 2009; 28:151-166
    • (2009) Cancer Metastasis Rev , vol.28 , pp. 151-166
    • Schmalhofer, O.1    Brabletz, S.2    Brabletz, T.3
  • 85
    • 84903710528 scopus 로고    scopus 로고
    • Emerging role of nanog in tumorigenesis and cancer stem cells
    • IV Santaliz-Ruiz LE, Xie X, Old M, Teknos TN, Pan Q. Emerging role of nanog in tumorigenesis and cancer stem cells. Int J Cancer. 2014; 135:2741-2748
    • (2014) Int J Cancer , vol.135 , pp. 2741-2748
    • Santaliz-Ruiz, L.E.1    Xie, X.2    Old, M.3    Teknos, T.N.4    Pan, Q.5
  • 86
    • 47749087950 scopus 로고    scopus 로고
    • Integrin-linked kinase-essential roles in physiology and cancer biology
    • McDonald PC, Fielding AB, Dedhar S. Integrin-linked kinase-essential roles in physiology and cancer biology. J Cell Sci. 2008; 121:3121-3132
    • (2008) J Cell Sci , vol.121 , pp. 3121-3132
    • McDonald, P.C.1    Fielding, A.B.2    Dedhar, S.3
  • 87
    • 79960901978 scopus 로고    scopus 로고
    • The role of the p38 MAPK signaling pathway in high glucose-induced epithelial-mesenchymal transition of cultured human renal tubular epithelial cells
    • Lv ZM, Wang Q, Wan Q, Lin JG, Hu MS, Liu YX, Wang R. The role of the p38 MAPK signaling pathway in high glucose-induced epithelial-mesenchymal transition of cultured human renal tubular epithelial cells. PLoS One. 2011; 6:e22806
    • (2011) PLoS One , vol.6
    • Lv, Z.M.1    Wang, Q.2    Wan, Q.3    Lin, J.G.4    Hu, M.S.5    Liu, Y.X.6    Wang, R.7
  • 88
    • 84880914022 scopus 로고    scopus 로고
    • An MAPK-dependent pathway induces epithelialmesenchymal transition via Twist activation in human breast cancer cell lines
    • Li NY, Weber CE, Wai PY, Cuevas BD, Zhang J, Kuo PC, Mi Z. An MAPK-dependent pathway induces epithelialmesenchymal transition via Twist activation in human breast cancer cell lines. Surgery. 2013; 154:404-410
    • (2013) Surgery , vol.154 , pp. 404-410
    • Li, N.Y.1    Weber, C.E.2    Wai, P.Y.3    Cuevas, B.D.4    Zhang, J.5    Kuo, P.C.6    Mi, Z.7
  • 89
    • 69249111313 scopus 로고    scopus 로고
    • Reversibility of epithelial-mesenchymal transition (EMT) induced in breast cancer cells by activation of urokinase receptor-dependent cell signaling
    • Jo M, Lester RD, Montel V, Eastman B, Takimoto S, Gonias SL. Reversibility of epithelial-mesenchymal transition (EMT) induced in breast cancer cells by activation of urokinase receptor-dependent cell signaling. J Biol Chem. 2009; 284:22825-22833
    • (2009) J Biol Chem , vol.284 , pp. 22825-22833
    • Jo, M.1    Lester, R.D.2    Montel, V.3    Eastman, B.4    Takimoto, S.5    Gonias, S.L.6
  • 91
    • 84881308659 scopus 로고    scopus 로고
    • PD-1 increases PTEN phosphatase activity while decreasing PTEN protein stability by inhibiting casein kinase 2
    • Patsoukis N, Li L, Sari D, Petkova V, Boussiotis VA. PD-1 increases PTEN phosphatase activity while decreasing PTEN protein stability by inhibiting casein kinase 2. Mol Cell Biol. 2013; 33:3091-3098
    • (2013) Mol Cell Biol , vol.33 , pp. 3091-3098
    • Patsoukis, N.1    Li, L.2    Sari, D.3    Petkova, V.4    Boussiotis, V.A.5
  • 95
    • 79958748545 scopus 로고    scopus 로고
    • Extracellular heat shock proteins, cellular export vesicles, and the Stress Observation System: a form of communication during injury, infection, and cell damage. It is never known how far a controversial finding will go! Dedicated to Ferruccio Ritossa
    • De Maio A. Extracellular heat shock proteins, cellular export vesicles, and the Stress Observation System: a form of communication during injury, infection, and cell damage. It is never known how far a controversial finding will go! Dedicated to Ferruccio Ritossa. Cell Stress Chaperones. 2011; 16:235-249
    • (2011) Cell Stress Chaperones , vol.16 , pp. 235-249
    • De Maio, A.1
  • 96
    • 84865305431 scopus 로고    scopus 로고
    • Structures and mechanisms of vesicle coat components and multisubunit tethering complexes
    • Jackson LP, Kümmel D, Reinisch KM, Owen DJ. Structures and mechanisms of vesicle coat components and multisubunit tethering complexes. Curr Opin Cell Biol. 2012; 24:475-483
    • (2012) Curr Opin Cell Biol , vol.24 , pp. 475-483
    • Jackson, L.P.1    Kümmel, D.2    Reinisch, K.M.3    Owen, D.J.4
  • 97
    • 84896689164 scopus 로고    scopus 로고
    • Oligomerization of rab/effector complexes in the regulation of vesicle trafficking
    • Khan AR. Oligomerization of rab/effector complexes in the regulation of vesicle trafficking. Prog Mol Biol Transl Sci. 2013; 117:579-614
    • (2013) Prog Mol Biol Transl Sci , vol.117 , pp. 579-614
    • Khan, A.R.1
  • 98
    • 84878905805 scopus 로고    scopus 로고
    • Detection of protein palmitoylation in cultured Hippocampal neurons by immunoprecipitation and acyl-biotin exchange (ABE)
    • Brigidi GS, Bamji SX. Detection of protein palmitoylation in cultured Hippocampal neurons by immunoprecipitation and acyl-biotin exchange (ABE). J Vis Exp. 2013; 72:e50031
    • (2013) J Vis Exp , vol.72
    • Brigidi, G.S.1    Bamji, S.X.2
  • 100
    • 0027104001 scopus 로고
    • Dynamics of three-dimensional replication patterns during the S-phase, analysed by double labelling of DNA and confocal microscopy
    • Manders EM, Stap J, Brakenhoff GJ, van Driel R, Aten JA. Dynamics of three-dimensional replication patterns during the S-phase, analysed by double labelling of DNA and confocal microscopy. J Cell Sci. 1992; 103:857-862
    • (1992) J Cell Sci , vol.103 , pp. 857-862
    • Manders, E.M.1    Stap, J.2    Brakenhoff, G.J.3    van Driel, R.4    Aten, J.A.5


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