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Volumn 80, Issue 12, 2010, Pages 1921-1929

Transglutaminase 2: A multi-tasking protein in the complex circuitry of inflammation and cancer

Author keywords

Cancer stem cell; Drug resistance; Epithelial to mesenchymal transition; Inflammation; Metastasis

Indexed keywords

ACYLTRANSFERASE INHIBITOR; ANTINEOPLASTIC AGENT; CARMUSTINE; CISPLATIN; DIETHYLCARBAMAZINE; DOXORUBICIN; GEMCITABINE; PACLITAXEL; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 2; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE INHIBITOR; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 78049427740     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2010.06.029     Document Type: Review
Times cited : (123)

References (91)
  • 1
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: crosslinking enzymes with pleiotropic functions
    • Lorand L., Graham R.M. Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat Rev Mol Cell Biol 2003, 4:140-156.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 2
    • 14544287324 scopus 로고    scopus 로고
    • Mammalian transglutaminases: a family portrait
    • Mehta K. Mammalian transglutaminases: a family portrait. Prog Exp Tumor Res 2005, 38:1-18.
    • (2005) Prog Exp Tumor Res , vol.38 , pp. 1-18
    • Mehta, K.1
  • 3
    • 0028176166 scopus 로고
    • Gh: a GTP-binding protein with transglutaminase activity and receptor signaling function
    • Nakaoka H., Perez D.M., Baek K.J., Das T., Husain A., Misono K., et al. Gh: a GTP-binding protein with transglutaminase activity and receptor signaling function. Science 1994, 264:1593-1596.
    • (1994) Science , vol.264 , pp. 1593-1596
    • Nakaoka, H.1    Perez, D.M.2    Baek, K.J.3    Das, T.4    Husain, A.5    Misono, K.6
  • 4
    • 0042068233 scopus 로고    scopus 로고
    • A novel function of tissue-type transglutaminase: protein disulphide isomerase
    • Hasegawa G., Suwa M., Ichikawa Y., Ohtsuka T., Kumagai S., Kikuchi M., et al. A novel function of tissue-type transglutaminase: protein disulphide isomerase. Biochem J 2003, 373:793-803.
    • (2003) Biochem J , vol.373 , pp. 793-803
    • Hasegawa, G.1    Suwa, M.2    Ichikawa, Y.3    Ohtsuka, T.4    Kumagai, S.5    Kikuchi, M.6
  • 5
    • 2642536093 scopus 로고    scopus 로고
    • Tissue transglutaminase has intrinsic kinase activity: identification of transglutaminase 2 as an insulin-like growth factor-binding protein-3 kinase
    • Mishra S., Murphy L.J. Tissue transglutaminase has intrinsic kinase activity: identification of transglutaminase 2 as an insulin-like growth factor-binding protein-3 kinase. J Biol Chem 2004, 279:23863-23868.
    • (2004) J Biol Chem , vol.279 , pp. 23863-23868
    • Mishra, S.1    Murphy, L.J.2
  • 6
    • 3042531037 scopus 로고    scopus 로고
    • Gha/tissue transglutaminase 2: an emerging G protein in signal transduction
    • Mhaouty-Kodja S. Gha/tissue transglutaminase 2: an emerging G protein in signal transduction. Biol Cell 2004, 96:363-367.
    • (2004) Biol Cell , vol.96 , pp. 363-367
    • Mhaouty-Kodja, S.1
  • 7
    • 0029862039 scopus 로고    scopus 로고
    • Transglutaminase induction by various cell death and apoptosis pathways
    • Fesus L., Madi A., Balajthy Z., Nemes Z., Szondy Z. Transglutaminase induction by various cell death and apoptosis pathways. Experientia 1996, 52:942-949.
    • (1996) Experientia , vol.52 , pp. 942-949
    • Fesus, L.1    Madi, A.2    Balajthy, Z.3    Nemes, Z.4    Szondy, Z.5
  • 8
    • 0038641718 scopus 로고    scopus 로고
    • Crosslinking of cellular proteins by tissue transglutaminase during nectrotic cell death: mechanism for maintaining tissue integrity
    • Nicholas B., Smerthurst P., Verderio E., Jones R., Griffin M. Crosslinking of cellular proteins by tissue transglutaminase during nectrotic cell death: mechanism for maintaining tissue integrity. Biochem J 2003, 371:413-422.
    • (2003) Biochem J , vol.371 , pp. 413-422
    • Nicholas, B.1    Smerthurst, P.2    Verderio, E.3    Jones, R.4    Griffin, M.5
  • 9
    • 67650928193 scopus 로고    scopus 로고
    • Tissue transglutaminase promotes or suppresses tumors depending on cell context
    • Chhabra A., Verma A., Mehta K. Tissue transglutaminase promotes or suppresses tumors depending on cell context. Anticancer Res 2009, 29:1909-1920.
    • (2009) Anticancer Res , vol.29 , pp. 1909-1920
    • Chhabra, A.1    Verma, A.2    Mehta, K.3
  • 10
    • 33845307265 scopus 로고    scopus 로고
    • Reversal of drug resistance in breast cancer cells by transglutaminase 2 inhibition and nuclear factor-kappaB inactivation
    • Kim D.S., Park S.S., Nam B.H., Kim I.H., Kim S.Y. Reversal of drug resistance in breast cancer cells by transglutaminase 2 inhibition and nuclear factor-kappaB inactivation. Cancer Res 2006, 66:10936-10943.
    • (2006) Cancer Res , vol.66 , pp. 10936-10943
    • Kim, D.S.1    Park, S.S.2    Nam, B.H.3    Kim, I.H.4    Kim, S.Y.5
  • 11
    • 34548399498 scopus 로고    scopus 로고
    • Transglutaminase-mediated activation of nuclear transcription factor-kappaB in cancer cells: a new therapeutic opportunity
    • Verma A., Mehta K. Transglutaminase-mediated activation of nuclear transcription factor-kappaB in cancer cells: a new therapeutic opportunity. Curr Cancer Drug Targets 2007, 7:559-565.
    • (2007) Curr Cancer Drug Targets , vol.7 , pp. 559-565
    • Verma, A.1    Mehta, K.2
  • 12
    • 0035827627 scopus 로고    scopus 로고
    • Graham RM targeted inactivation of Gh/tissue transglutaminase II
    • Nanda N., Iismaa S.E., Dagger, Owens W.A., Husain A., Mackay F. Graham RM targeted inactivation of Gh/tissue transglutaminase II. J Biol Chem 2001, 276:20673-20678.
    • (2001) J Biol Chem , vol.276 , pp. 20673-20678
    • Nanda, N.1    Iismaa, S.E.2    Dagger3    Owens, W.A.4    Husain, A.5    Mackay, F.6
  • 14
    • 67651071286 scopus 로고    scopus 로고
    • Transglutaminases and disease: lessons from genetically engineered mouse models and inherited disorders
    • Iismaa S.E., Mearns B.M., Lorand L., Graham R.M. Transglutaminases and disease: lessons from genetically engineered mouse models and inherited disorders. Physiol Rev 2009, 89:991-1023.
    • (2009) Physiol Rev , vol.89 , pp. 991-1023
    • Iismaa, S.E.1    Mearns, B.M.2    Lorand, L.3    Graham, R.M.4
  • 15
    • 4143089161 scopus 로고    scopus 로고
    • Tissue transglutaminase in normal and abnormal wound healing: review article
    • Verderio E.A.M., Johnson T., Griffin M. Tissue transglutaminase in normal and abnormal wound healing: review article. Amino Acids 2004, 26:387-404.
    • (2004) Amino Acids , vol.26 , pp. 387-404
    • Verderio, E.A.M.1    Johnson, T.2    Griffin, M.3
  • 16
    • 26444591889 scopus 로고    scopus 로고
    • TGF-beta1 upregulates transglutaminase 2 and fibronectin in dermal fibroblasts: a possible mechanism for the stabilization of tissue inflammation
    • Quan G., Choi J.Y., Lee D.S., Lee S.C. TGF-beta1 upregulates transglutaminase 2 and fibronectin in dermal fibroblasts: a possible mechanism for the stabilization of tissue inflammation. Arch Dermatol Res 2005, 297:84-90.
    • (2005) Arch Dermatol Res , vol.297 , pp. 84-90
    • Quan, G.1    Choi, J.Y.2    Lee, D.S.3    Lee, S.C.4
  • 17
    • 0031885898 scopus 로고    scopus 로고
    • TNF-alpha modulates expression of the tissue transglutaminase gene in liver cells
    • Kuncio G.S., Tsyganskaya M., Zhu J., Liu S.-L., Nagy L., Thomazy V., et al. TNF-alpha modulates expression of the tissue transglutaminase gene in liver cells. Am J Physiol 1998, 274:G240-G245.
    • (1998) Am J Physiol , vol.274
    • Kuncio, G.S.1    Tsyganskaya, M.2    Zhu, J.3    Liu, S.-L.4    Nagy, L.5    Thomazy, V.6
  • 18
    • 33744496065 scopus 로고    scopus 로고
    • Transglutaminase 2 in inflammation
    • Kim S.Y. Transglutaminase 2 in inflammation. Front Biosci 2006, 11:3026-3035.
    • (2006) Front Biosci , vol.11 , pp. 3026-3035
    • Kim, S.Y.1
  • 19
    • 0035403504 scopus 로고    scopus 로고
    • Interleukin-1 induces pro-mineralizing activity of cartilage tissue transglutaminase and factor XIIIa
    • Johnson K., Hashimoto S., Lotz M., Pritzker K., Terkeltaub R. Interleukin-1 induces pro-mineralizing activity of cartilage tissue transglutaminase and factor XIIIa. Am J Pathol 2001, 159:149-163.
    • (2001) Am J Pathol , vol.159 , pp. 149-163
    • Johnson, K.1    Hashimoto, S.2    Lotz, M.3    Pritzker, K.4    Terkeltaub, R.5
  • 20
    • 0027405028 scopus 로고
    • Expression induced by interleukin-6 of tissue-type transglutaminase in human hepatoblastoma HepG2 cells
    • Suto N., Ikura K., Sasaki R. Expression induced by interleukin-6 of tissue-type transglutaminase in human hepatoblastoma HepG2 cells. J Biol Chem 1993, 268(10):7469-7473.
    • (1993) J Biol Chem , vol.268 , Issue.10 , pp. 7469-7473
    • Suto, N.1    Ikura, K.2    Sasaki, R.3
  • 21
    • 0032824155 scopus 로고    scopus 로고
    • Tissue transglutaminase is expressed, active, and directly involved in rat dermal wound healing and angiogenesis
    • Haroon Z.A., Hettasch J.M., Lai TSDewhirst M.W., Greenberg C.S. Tissue transglutaminase is expressed, active, and directly involved in rat dermal wound healing and angiogenesis. FASEB J 1999, 13(13):1787-1795.
    • (1999) FASEB J , vol.13 , Issue.13 , pp. 1787-1795
    • Haroon, Z.A.1    Hettasch, J.M.2    Lai TSDewhirst, M.W.3    Greenberg, C.S.4
  • 24
    • 77952495149 scopus 로고    scopus 로고
    • Recent advances in understanding the roles of transglutaminase 2 in alcoholic steatohepatitis
    • Tatsukawa H., Kojima S. Recent advances in understanding the roles of transglutaminase 2 in alcoholic steatohepatitis. Cell Biol Int 2010, 34:325-334.
    • (2010) Cell Biol Int , vol.34 , pp. 325-334
    • Tatsukawa, H.1    Kojima, S.2
  • 25
    • 51349086373 scopus 로고    scopus 로고
    • Tissue transglutaminase contributes to interstitial renal fibrosis by favoring accumulation of fibrillar collagen through TGF-beta activation and cell infiltration
    • Shweke N., Boulos N., Jouanneau C., Vandermeersch S., Melino G., Dussaule J.C., et al. Tissue transglutaminase contributes to interstitial renal fibrosis by favoring accumulation of fibrillar collagen through TGF-beta activation and cell infiltration. Am J Pathol 2008, 173:631-642.
    • (2008) Am J Pathol , vol.173 , pp. 631-642
    • Shweke, N.1    Boulos, N.2    Jouanneau, C.3    Vandermeersch, S.4    Melino, G.5    Dussaule, J.C.6
  • 26
    • 0025756890 scopus 로고
    • Transglutaminase differentiation during maturation of human blood monocytes to macrophages
    • Seiving B., Ohlsson K., Linder C., Stenberg P. Transglutaminase differentiation during maturation of human blood monocytes to macrophages. Eur J Haematol 1991, 46:263-271.
    • (1991) Eur J Haematol , vol.46 , pp. 263-271
    • Seiving, B.1    Ohlsson, K.2    Linder, C.3    Stenberg, P.4
  • 27
    • 61449162968 scopus 로고    scopus 로고
    • Transglutaminase 2 is needed for the formation of an efficient phagocyte portal in macrophages engulfing apoptotic cells
    • Garabuczi E., Sarang Z., Vereb G., Vámosi G., Aeschlimann D., Blaskó B., et al. Transglutaminase 2 is needed for the formation of an efficient phagocyte portal in macrophages engulfing apoptotic cells. J Immunol 2009, 182:2084-2092.
    • (2009) J Immunol , vol.182 , pp. 2084-2092
    • Garabuczi, E.1    Sarang, Z.2    Vereb, G.3    Vámosi, G.4    Aeschlimann, D.5    Blaskó, B.6
  • 28
    • 0035469864 scopus 로고    scopus 로고
    • Cell surface tissue transglutaminase is involved in adhesion and migration of monocytic cells on fibronectin
    • Akimov S.S., Belkin A.M. Cell surface tissue transglutaminase is involved in adhesion and migration of monocytic cells on fibronectin. Blood 2001, 98(5):1567-1576.
    • (2001) Blood , vol.98 , Issue.5 , pp. 1567-1576
    • Akimov, S.S.1    Belkin, A.M.2
  • 29
    • 0043124302 scopus 로고    scopus 로고
    • Importance of tissue transglutaminase in repair of extracellular matrices and cell death of dermal fibroblasts after exposure to a solarium ultraviolet A source
    • Gross S.R., Balklava Z., Griffin M. Importance of tissue transglutaminase in repair of extracellular matrices and cell death of dermal fibroblasts after exposure to a solarium ultraviolet A source. J Invest Dermatol 2003, 121:412-423.
    • (2003) J Invest Dermatol , vol.121 , pp. 412-423
    • Gross, S.R.1    Balklava, Z.2    Griffin, M.3
  • 30
    • 0034695929 scopus 로고    scopus 로고
    • Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin
    • Akimov S.S., Krylov D., Fleischman L.F., Belkin A.M. Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin. J Cell Biol 2000, 148:825-838.
    • (2000) J Cell Biol , vol.148 , pp. 825-838
    • Akimov, S.S.1    Krylov, D.2    Fleischman, L.F.3    Belkin, A.M.4
  • 31
    • 51049089580 scopus 로고    scopus 로고
    • Fibronectin-tissue transglutaminase matrix rescues RGD-impaired cell adhesion through syndecan-4 and beta1 integrin co-signaling
    • Telci D., Wang Z., Li X., Verderio E.A., Humphries M.J., Baccarini M., et al. Fibronectin-tissue transglutaminase matrix rescues RGD-impaired cell adhesion through syndecan-4 and beta1 integrin co-signaling. J Biol Chem 2008, 283:20937-20947.
    • (2008) J Biol Chem , vol.283 , pp. 20937-20947
    • Telci, D.1    Wang, Z.2    Li, X.3    Verderio, E.A.4    Humphries, M.J.5    Baccarini, M.6
  • 32
    • 33745138517 scopus 로고    scopus 로고
    • GPR56, an atypical G protein-coupled receptor, binds tissue transglutaminase, TG2, and inhibits melanoma tumor growth and metastasis
    • Xu L., Begum S., Hearn J.D., Hynes R.O. GPR56, an atypical G protein-coupled receptor, binds tissue transglutaminase, TG2, and inhibits melanoma tumor growth and metastasis. Proc Natl Acad Sci USA 2006, 103:9023-9028.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 9023-9028
    • Xu, L.1    Begum, S.2    Hearn, J.D.3    Hynes, R.O.4
  • 33
    • 77950346282 scopus 로고    scopus 로고
    • Immunity, inflammation, and cancer
    • Grivennikov S., Greten F.R., Karin M. Immunity, inflammation, and cancer. Cell 2010, 140:883-899.
    • (2010) Cell , vol.140 , pp. 883-899
    • Grivennikov, S.1    Greten, F.R.2    Karin, M.3
  • 35
    • 34548848815 scopus 로고    scopus 로고
    • Tissue transglutaminase-mediated chemoresistance in cancer cells
    • Verma A., Mehta K. Tissue transglutaminase-mediated chemoresistance in cancer cells. Drug Resist Updat 2007, 10:144-151.
    • (2007) Drug Resist Updat , vol.10 , pp. 144-151
    • Verma, A.1    Mehta, K.2
  • 36
    • 34247153086 scopus 로고    scopus 로고
    • Tissue transglutaminase expression promotes cell attachment, invasion and survival in breast cancer cells
    • Mangala L.S., Fok J.Y., Zorrilla-Calancha I.R., Verma A., Mehta K. Tissue transglutaminase expression promotes cell attachment, invasion and survival in breast cancer cells. Oncogene 2007, 26:2459-2470.
    • (2007) Oncogene , vol.26 , pp. 2459-2470
    • Mangala, L.S.1    Fok, J.Y.2    Zorrilla-Calancha, I.R.3    Verma, A.4    Mehta, K.5
  • 37
    • 40949114150 scopus 로고    scopus 로고
    • The transglutaminase 2 gene (TGM2), a potential molecular marker for chemotherapeutic drug sensitivity, is epigenetically silenced in breast cancer
    • Ai L., Kim W.J., Demircan B., Dyer L.M., Bray K.J., Skehan R.R., et al. The transglutaminase 2 gene (TGM2), a potential molecular marker for chemotherapeutic drug sensitivity, is epigenetically silenced in breast cancer. Carcinogenesis 2008, 29:510-518.
    • (2008) Carcinogenesis , vol.29 , pp. 510-518
    • Ai, L.1    Kim, W.J.2    Demircan, B.3    Dyer, L.M.4    Bray, K.J.5    Skehan, R.R.6
  • 38
    • 33751285778 scopus 로고    scopus 로고
    • Increased expression of tissue transglutaminase in pancreatic ductal adenocarcinoma and its implications in drug resistance and metastasis
    • Verma A., Wang H., Manavathi B., Fok J.Y., Mann A.P., Kumar R., et al. Increased expression of tissue transglutaminase in pancreatic ductal adenocarcinoma and its implications in drug resistance and metastasis. Cancer Res 2006, 66:10525-10533.
    • (2006) Cancer Res , vol.66 , pp. 10525-10533
    • Verma, A.1    Wang, H.2    Manavathi, B.3    Fok, J.Y.4    Mann, A.P.5    Kumar, R.6
  • 39
    • 9744274000 scopus 로고    scopus 로고
    • Prognostic significance of tissue transglutaminase in drug resistant and metastatic breast cancer
    • Mehta K., Fok J., Miller F.R., Koul D., Sahin A.A. Prognostic significance of tissue transglutaminase in drug resistant and metastatic breast cancer. Clin Cancer Res 2004, 10:8068-8076.
    • (2004) Clin Cancer Res , vol.10 , pp. 8068-8076
    • Mehta, K.1    Fok, J.2    Miller, F.R.3    Koul, D.4    Sahin, A.A.5
  • 40
    • 33746041843 scopus 로고    scopus 로고
    • Implications of tissue transglutaminase expression in malignant melanoma
    • Fok J.Y., Ekmekcioglu S., Mehta K. Implications of tissue transglutaminase expression in malignant melanoma. Mol Cancer Ther 2006, 5:1493-1503.
    • (2006) Mol Cancer Ther , vol.5 , pp. 1493-1503
    • Fok, J.Y.1    Ekmekcioglu, S.2    Mehta, K.3
  • 41
    • 48649099197 scopus 로고    scopus 로고
    • Clinical and biological significance of tissue transglutaminase in ovarian carcinoma
    • Hwang J.Y., Mangala L.S., Fok J.Y., Lin Y.G., Merritt W.M., Spannuth W.A., et al. Clinical and biological significance of tissue transglutaminase in ovarian carcinoma. Cancer Res 2008, 68:5849-5858.
    • (2008) Cancer Res , vol.68 , pp. 5849-5858
    • Hwang, J.Y.1    Mangala, L.S.2    Fok, J.Y.3    Lin, Y.G.4    Merritt, W.M.5    Spannuth, W.A.6
  • 42
    • 34547639164 scopus 로고    scopus 로고
    • Enhanced peritoneal ovarian tumor dissemination by tissue transglutaminase
    • Satpathy M., Cao L., Pincheira R., Emerson R., Bigsby R., Nakshatri H., et al. Enhanced peritoneal ovarian tumor dissemination by tissue transglutaminase. Cancer Res 2007, 67:7194-7202.
    • (2007) Cancer Res , vol.67 , pp. 7194-7202
    • Satpathy, M.1    Cao, L.2    Pincheira, R.3    Emerson, R.4    Bigsby, R.5    Nakshatri, H.6
  • 43
    • 77949261587 scopus 로고    scopus 로고
    • Transglutaminase 2 as a cisplatin resistance marker in non-small cell lung cancer
    • Park K.S., Kim H.K., Lee J.H., Choi Y.B., Park S.Y., Yang S.H., et al. Transglutaminase 2 as a cisplatin resistance marker in non-small cell lung cancer. J Cancer Res Clin Oncol 2010, 136:493-502.
    • (2010) J Cancer Res Clin Oncol , vol.136 , pp. 493-502
    • Park, K.S.1    Kim, H.K.2    Lee, J.H.3    Choi, Y.B.4    Park, S.Y.5    Yang, S.H.6
  • 44
    • 34247349128 scopus 로고    scopus 로고
    • Transglutaminase 2 inhibitor, KCC009, disrupts fibronectin assembly in the extracellular matrix and sensitizes orthotopic glioblastomas to chemotherapy
    • Yuan L., Siegel M., Choi K., Khosla C., Miller C.R., Jackson E.N., et al. Transglutaminase 2 inhibitor, KCC009, disrupts fibronectin assembly in the extracellular matrix and sensitizes orthotopic glioblastomas to chemotherapy. Oncogene 2007, 26:2563-2573.
    • (2007) Oncogene , vol.26 , pp. 2563-2573
    • Yuan, L.1    Siegel, M.2    Choi, K.3    Khosla, C.4    Miller, C.R.5    Jackson, E.N.6
  • 45
    • 9144241047 scopus 로고    scopus 로고
    • Highly expressed genes in pancreatic ductal adenocarcinomas: a comprehensive characterization and comparison of the transcription profiles obtained from three major technologies
    • Iacobuzio-Donahue C.A., Ashfaq R., Maitra A., Adsay N.V., Shen-Ong G.L., Berg K., et al. Highly expressed genes in pancreatic ductal adenocarcinomas: a comprehensive characterization and comparison of the transcription profiles obtained from three major technologies. Cancer Res 2003, 63:8614-8622.
    • (2003) Cancer Res , vol.63 , pp. 8614-8622
    • Iacobuzio-Donahue, C.A.1    Ashfaq, R.2    Maitra, A.3    Adsay, N.V.4    Shen-Ong, G.L.5    Berg, K.6
  • 46
    • 0037879089 scopus 로고    scopus 로고
    • Identification of metastasis-associated proteins by proteomic analysis and functional exploration of interleukin-18 in metastasis
    • Jiang D., Ying W., Lu Y., Wan J., Zhai Y., Liu W., et al. Identification of metastasis-associated proteins by proteomic analysis and functional exploration of interleukin-18 in metastasis. Proteomics 2003, 3:724-737.
    • (2003) Proteomics , vol.3 , pp. 724-737
    • Jiang, D.1    Ying, W.2    Lu, Y.3    Wan, J.4    Zhai, Y.5    Liu, W.6
  • 47
    • 4744351463 scopus 로고    scopus 로고
    • Augmentation of tissue transglutaminase expression and activation by epidermal growth factor inhibit doxorubicin-induced apoptosis in human breast cancer cells
    • Antonyak M.A., Miller A.M., Jansen J.M., Boehm J.E., Balkman C.E., Wakshlag J.J., et al. Augmentation of tissue transglutaminase expression and activation by epidermal growth factor inhibit doxorubicin-induced apoptosis in human breast cancer cells. J Biol Chem 2004, 279:41461-41467.
    • (2004) J Biol Chem , vol.279 , pp. 41461-41467
    • Antonyak, M.A.1    Miller, A.M.2    Jansen, J.M.3    Boehm, J.E.4    Balkman, C.E.5    Wakshlag, J.J.6
  • 49
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D., Weinberg R.A. The hallmarks of cancer. Cell 2000, 100:57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 50
    • 0024379282 scopus 로고
    • Transglutaminase levels and immunologic functions of BCG-elicited mouse peritoneal macrophages isolated by centrifugal elutriation
    • Khera V., Mehta K. Transglutaminase levels and immunologic functions of BCG-elicited mouse peritoneal macrophages isolated by centrifugal elutriation. J Leukoc Biol 1989, 45:434-443.
    • (1989) J Leukoc Biol , vol.45 , pp. 434-443
    • Khera, V.1    Mehta, K.2
  • 51
    • 0042834268 scopus 로고    scopus 로고
    • Identification of tissue transglutaminase as a novel molecule involved in human CD8+ T cell transendothelial migration
    • Mohan K., Pinto D., Issekutz T.B. Identification of tissue transglutaminase as a novel molecule involved in human CD8+ T cell transendothelial migration. J Immunol 2003, 171:3179-3186.
    • (2003) J Immunol , vol.171 , pp. 3179-3186
    • Mohan, K.1    Pinto, D.2    Issekutz, T.B.3
  • 52
    • 1542742158 scopus 로고    scopus 로고
    • TGFb-induced cell surface tissue transglutaminase increases adhesion and migration of RPE cells on fibronectin through the gelatin-binding domain
    • Priglinger S.G., Alge C.S., Neubauer A.S., Kristin N., Hirneiss C., Eibl K., et al. TGFb-induced cell surface tissue transglutaminase increases adhesion and migration of RPE cells on fibronectin through the gelatin-binding domain. Invest Ophthal Visual Sci 2004, 45:955-963.
    • (2004) Invest Ophthal Visual Sci , vol.45 , pp. 955-963
    • Priglinger, S.G.1    Alge, C.S.2    Neubauer, A.S.3    Kristin, N.4    Hirneiss, C.5    Eibl, K.6
  • 53
    • 30544434283 scopus 로고    scopus 로고
    • Retinoic acid receptors and tissue-transglutaminase mediate short-term effect of retinoic acid on migration and invasion of neuroblastoma SH-SY5Y cells
    • Joshi S., Guleria R., Pan J., DiPette D., Singh U.S. Retinoic acid receptors and tissue-transglutaminase mediate short-term effect of retinoic acid on migration and invasion of neuroblastoma SH-SY5Y cells. Oncogene 2006, 25:240-247.
    • (2006) Oncogene , vol.25 , pp. 240-247
    • Joshi, S.1    Guleria, R.2    Pan, J.3    DiPette, D.4    Singh, U.S.5
  • 54
    • 34547104819 scopus 로고    scopus 로고
    • Tissue transglutaminase is essential for integrin-mediated survival of bone marrow-derived mesenchymal stem cells
    • Song H., Chang W., Lim S., Seo H.S., Shim C.Y., Park S., et al. Tissue transglutaminase is essential for integrin-mediated survival of bone marrow-derived mesenchymal stem cells. Stem Cells 2007, 25:1431-1438.
    • (2007) Stem Cells , vol.25 , pp. 1431-1438
    • Song, H.1    Chang, W.2    Lim, S.3    Seo, H.S.4    Shim, C.Y.5    Park, S.6
  • 55
    • 63049090100 scopus 로고    scopus 로고
    • Metastasis: from dissemination to organ-specific colonization
    • Nguyen D.X., Bos P.D., Massagué J. Metastasis: from dissemination to organ-specific colonization. Nat Rev Cancer 2009, 9:274-284.
    • (2009) Nat Rev Cancer , vol.9 , pp. 274-284
    • Nguyen, D.X.1    Bos, P.D.2    Massagué, J.3
  • 56
    • 0035992398 scopus 로고    scopus 로고
    • Proteomic analysis of lung adenocarcinoma: identification of a highly expressed set of proteins in tumors
    • Chen G., Gharib T.G., Huang C.C., Thomas D.G., Shedden K.A., Taylor J.M., et al. Proteomic analysis of lung adenocarcinoma: identification of a highly expressed set of proteins in tumors. Clin Cancer Res 2002, 8:2298-2305.
    • (2002) Clin Cancer Res , vol.8 , pp. 2298-2305
    • Chen, G.1    Gharib, T.G.2    Huang, C.C.3    Thomas, D.G.4    Shedden, K.A.5    Taylor, J.M.6
  • 57
    • 0030871969 scopus 로고    scopus 로고
    • Melanoma cell adhesion to injured arterioles: mechanisms of stabilized tethering
    • Kong L., Korthuis R.J. Melanoma cell adhesion to injured arterioles: mechanisms of stabilized tethering. Clin Exp Metastasis 1997, 15:426-431.
    • (1997) Clin Exp Metastasis , vol.15 , pp. 426-431
    • Kong, L.1    Korthuis, R.J.2
  • 58
    • 33846895222 scopus 로고    scopus 로고
    • GPR56 and TG2: possible roles in suppression of tumor growth by the microenvironment
    • Xu L., Hynes R.O. GPR56 and TG2: possible roles in suppression of tumor growth by the microenvironment. Cell Cycle 2007, 6:160-165.
    • (2007) Cell Cycle , vol.6 , pp. 160-165
    • Xu, L.1    Hynes, R.O.2
  • 59
    • 0035901090 scopus 로고    scopus 로고
    • Inflammation and cancer: back to Virchow?
    • Balkwill F., Mantovani A. Inflammation and cancer: back to Virchow?. Lancet 2001, 357:539-545.
    • (2001) Lancet , vol.357 , pp. 539-545
    • Balkwill, F.1    Mantovani, A.2
  • 60
    • 33645952640 scopus 로고    scopus 로고
    • Infection & neoplastic growth 101: the required reading for microbial pathogens aspiring to cause cancer
    • Bertout J., Thomas-Tikhonenko A. Infection & neoplastic growth 101: the required reading for microbial pathogens aspiring to cause cancer. Cancer Treat Res 2006, 130:167-197.
    • (2006) Cancer Treat Res , vol.130 , pp. 167-197
    • Bertout, J.1    Thomas-Tikhonenko, A.2
  • 61
    • 70450198396 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transitions in development and disease
    • Thiery P.J., Acloque H., Huang R.Y.J., Nieto M.A. Epithelial-mesenchymal transitions in development and disease. Cell 2009, 139:871-887.
    • (2009) Cell , vol.139 , pp. 871-887
    • Thiery, P.J.1    Acloque, H.2    Huang, R.Y.J.3    Nieto, M.A.4
  • 62
    • 70450142560 scopus 로고    scopus 로고
    • Inflammation and EMT: an alliance towards organ fibrosis and cancer progression
    • López-Novoa J.M., Nieto M.A. Inflammation and EMT: an alliance towards organ fibrosis and cancer progression. EMBO Mol Med 2009, 1:303-314.
    • (2009) EMBO Mol Med , vol.1 , pp. 303-314
    • López-Novoa, J.M.1    Nieto, M.A.2
  • 63
    • 56749176437 scopus 로고    scopus 로고
    • Cadherins and cancer: how does cadherin dysfunction promote tumor progression?
    • Jeanes A., Gottardi C.J., Yap A.S. Cadherins and cancer: how does cadherin dysfunction promote tumor progression?. Oncogene 2008, 27:6920-6929.
    • (2008) Oncogene , vol.27 , pp. 6920-6929
    • Jeanes, A.1    Gottardi, C.J.2    Yap, A.S.3
  • 64
    • 67650996754 scopus 로고    scopus 로고
    • Biomarkers for epithelial-mesechymal transitions
    • Zeisberg M., Neilson E.G. Biomarkers for epithelial-mesechymal transitions. J Clin Invest 2009, 119:1429-1437.
    • (2009) J Clin Invest , vol.119 , pp. 1429-1437
    • Zeisberg, M.1    Neilson, E.G.2
  • 65
    • 0033230475 scopus 로고    scopus 로고
    • N-cadherin promotes motility in human breast cancer cells regardless of their E-cadherin expression
    • Nieman M.T., Prudoff R.S., Johnson K.R., Wheelock M.J. N-cadherin promotes motility in human breast cancer cells regardless of their E-cadherin expression. J Cell Biol 1999, 147:631-644.
    • (1999) J Cell Biol , vol.147 , pp. 631-644
    • Nieman, M.T.1    Prudoff, R.S.2    Johnson, K.R.3    Wheelock, M.J.4
  • 66
    • 67651005404 scopus 로고    scopus 로고
    • EMT: when epithelial cells decide to become mesenchymal-like cells
    • Kalluri R. EMT: when epithelial cells decide to become mesenchymal-like cells. J Clin Invest 2009, 119:1417-1419.
    • (2009) J Clin Invest , vol.119 , pp. 1417-1419
    • Kalluri, R.1
  • 67
    • 59449090107 scopus 로고    scopus 로고
    • Derynck R.TGF-beta-induced epithelial to mesenchymal transition
    • Xu J., Lamouille S. Derynck R.TGF-beta-induced epithelial to mesenchymal transition. Cell Res 2009, 19:156-172.
    • (2009) Cell Res , vol.19 , pp. 156-172
    • Xu, J.1    Lamouille, S.2
  • 68
    • 75649088874 scopus 로고    scopus 로고
    • Mechanisms of the epithelial-mesenchymal transition by TGF-beta
    • Wendt M.K., Allington T.M., Schiemann W.P. Mechanisms of the epithelial-mesenchymal transition by TGF-beta. Future Oncol 2009, 5:1145-1168.
    • (2009) Future Oncol , vol.5 , pp. 1145-1168
    • Wendt, M.K.1    Allington, T.M.2    Schiemann, W.P.3
  • 69
    • 74949093198 scopus 로고    scopus 로고
    • Transforming growth factor-beta signaling in epithelial-mesenchymal transition and progression of cancer
    • Miyazono K. Transforming growth factor-beta signaling in epithelial-mesenchymal transition and progression of cancer. Proc Jpn Acad Ser B: Phys Biol Sci 2009, 85:314-323.
    • (2009) Proc Jpn Acad Ser B: Phys Biol Sci , vol.85 , pp. 314-323
    • Miyazono, K.1
  • 70
    • 77249117415 scopus 로고    scopus 로고
    • Pancreatic cancer stem cell and EMT in drug resistance and metastasis
    • Sarkar F.H., Li Y., Wang Z., Kong D. Pancreatic cancer stem cell and EMT in drug resistance and metastasis. Minerva Chir 2009, 64:489-500.
    • (2009) Minerva Chir , vol.64 , pp. 489-500
    • Sarkar, F.H.1    Li, Y.2    Wang, Z.3    Kong, D.4
  • 71
    • 33751582928 scopus 로고    scopus 로고
    • Snail activation disrupts tissue homeostasis and induces fibrosis in the adult kidney
    • Boutet A., De Frutos C.A., Maxwell P.H., Mayol M.J., Romero J., Nieto M.A. Snail activation disrupts tissue homeostasis and induces fibrosis in the adult kidney. EMBO J 2006, 25:5603-5613.
    • (2006) EMBO J , vol.25 , pp. 5603-5613
    • Boutet, A.1    De Frutos, C.A.2    Maxwell, P.H.3    Mayol, M.J.4    Romero, J.5    Nieto, M.A.6
  • 72
    • 0346724511 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transition and its implications for fibrosis
    • Kalluri R., Neilson E.G. Epithelial-mesenchymal transition and its implications for fibrosis. J Clin Invest 2003, 112:1776-1784.
    • (2003) J Clin Invest , vol.112 , pp. 1776-1784
    • Kalluri, R.1    Neilson, E.G.2
  • 73
    • 73649115337 scopus 로고    scopus 로고
    • Epithelial-to-mesenchymal transition and ovarian tumor progression induced by tissue transglutaminase
    • Shao M., Cao L., Shen C., Satpathy M., Chelladurai B., Bigsby R.M., et al. Epithelial-to-mesenchymal transition and ovarian tumor progression induced by tissue transglutaminase. Cancer Res 2009, 69:9192-9201.
    • (2009) Cancer Res , vol.69 , pp. 9192-9201
    • Shao, M.1    Cao, L.2    Shen, C.3    Satpathy, M.4    Chelladurai, B.5    Bigsby, R.M.6
  • 74
    • 43049165453 scopus 로고    scopus 로고
    • The epithelial-mesenchymal transition generates cells with properties of stem cells
    • Mani S.A., Guo W., Liao M.J., Eaton E.N., Ayyanan A., Zhou A.Y., et al. The epithelial-mesenchymal transition generates cells with properties of stem cells. Cell 2008, 133:704-715.
    • (2008) Cell , vol.133 , pp. 704-715
    • Mani, S.A.1    Guo, W.2    Liao, M.J.3    Eaton, E.N.4    Ayyanan, A.5    Zhou, A.Y.6
  • 75
    • 0142242157 scopus 로고    scopus 로고
    • A novel RGD-independent cel adhesion pathway mediated by fibronectin-bound tissue transglutaminase rescues cells from anoikis
    • Verderio E.A., Telci D., Okoye A., Melino G., Griffin M. A novel RGD-independent cel adhesion pathway mediated by fibronectin-bound tissue transglutaminase rescues cells from anoikis. J Biol Chem 2003, 278:42604-42614.
    • (2003) J Biol Chem , vol.278 , pp. 42604-42614
    • Verderio, E.A.1    Telci, D.2    Okoye, A.3    Melino, G.4    Griffin, M.5
  • 76
    • 42249085070 scopus 로고    scopus 로고
    • Tissue transglutaminase regulates focal adhesion kinase/AKT activation by modulating PTEN expression in pancreatic cancer cells
    • Verma A., Guha S., Wang H., Fok J.Y., Koul D., Abbruzzese J., et al. Tissue transglutaminase regulates focal adhesion kinase/AKT activation by modulating PTEN expression in pancreatic cancer cells. Clin Cancer Res 2008, 14:1997-2005.
    • (2008) Clin Cancer Res , vol.14 , pp. 1997-2005
    • Verma, A.1    Guha, S.2    Wang, H.3    Fok, J.Y.4    Koul, D.5    Abbruzzese, J.6
  • 77
    • 33646858986 scopus 로고    scopus 로고
    • Implications of increased tissue transglutaminase expression in drug-resistant breast cancer (MCF-7) cells
    • Herman J.F., Mehta K. Implications of increased tissue transglutaminase expression in drug-resistant breast cancer (MCF-7) cells. Oncogene 2006, 25:3049-3058.
    • (2006) Oncogene , vol.25 , pp. 3049-3058
    • Herman, J.F.1    Mehta, K.2
  • 78
    • 67650999875 scopus 로고    scopus 로고
    • The basics of epithelial-mesenchymal transition
    • Kalluri R., Weinberg R.A. The basics of epithelial-mesenchymal transition. J Clin Invest 2009, 119:1420-1428.
    • (2009) J Clin Invest , vol.119 , pp. 1420-1428
    • Kalluri, R.1    Weinberg, R.A.2
  • 79
    • 4344612243 scopus 로고    scopus 로고
    • NF-κB is essential for epithelial-mesenchymal transition and metastasis in a model of breast cancer progression
    • Margit D., Huber A., Azoitei N., Baumann B., Grunert S., et al. NF-κB is essential for epithelial-mesenchymal transition and metastasis in a model of breast cancer progression. J Clin Invest 2004, 114:5669-5681.
    • (2004) J Clin Invest , vol.114 , pp. 5669-5681
    • Margit, D.1    Huber, A.2    Azoitei, N.3    Baumann, B.4    Grunert, S.5
  • 80
    • 0036546501 scopus 로고    scopus 로고
    • NF-κB in cancer: from innocent bystander to major culprit
    • Karin M., Cao Y., Greten F.R., Li Z.W. NF-κB in cancer: from innocent bystander to major culprit. Nat Rev Cancer 2002, 2:301-310.
    • (2002) Nat Rev Cancer , vol.2 , pp. 301-310
    • Karin, M.1    Cao, Y.2    Greten, F.R.3    Li, Z.W.4
  • 81
    • 0036020941 scopus 로고    scopus 로고
    • NF-κB as a therapeutic target in cancer
    • Orlowski R.Z., Baldwin A.S. NF-κB as a therapeutic target in cancer. Trends Mol Med 2002, 8:385-389.
    • (2002) Trends Mol Med , vol.8 , pp. 385-389
    • Orlowski, R.Z.1    Baldwin, A.S.2
  • 82
    • 65349092794 scopus 로고    scopus 로고
    • Stabilization of Sanil by NF-kB is required for inflammation-induced cell migration and invasion
    • Wu Y., Deng J., Rychahou P.G., Qui S., Evers B.M., Zhou B.P. Stabilization of Sanil by NF-kB is required for inflammation-induced cell migration and invasion. Cell 2009, 15:416-428.
    • (2009) Cell , vol.15 , pp. 416-428
    • Wu, Y.1    Deng, J.2    Rychahou, P.G.3    Qui, S.4    Evers, B.M.5    Zhou, B.P.6
  • 83
    • 33846828787 scopus 로고    scopus 로고
    • Nakshat NF-kappaB represses E-cadherin expression and enhances epithelial to mesenchymal transition of mammary epithelial cells: potential involvement of ZEB-1 and ZEB-2
    • Chua H.L., Bhat-Nakshatri P., Clare S.E., Morimiya A., Badve S., Nakshat NF-kappaB represses E-cadherin expression and enhances epithelial to mesenchymal transition of mammary epithelial cells: potential involvement of ZEB-1 and ZEB-2. Oncogene 2007, 26:711-724.
    • (2007) Oncogene , vol.26 , pp. 711-724
    • Chua, H.L.1    Bhat-Nakshatri, P.2    Clare, S.E.3    Morimiya, A.4    Badve, S.5
  • 84
    • 74449086363 scopus 로고    scopus 로고
    • Transglutaminase II interacts with rac1, regulates production of reactive oxygen species, expression of snail, secretion of Th2 cytokines and mediates in vitro and in vivo allergic inflammation
    • Kim Y., Eom S., Kim K., Lee Y.S., Choe J., et al. Transglutaminase II interacts with rac1, regulates production of reactive oxygen species, expression of snail, secretion of Th2 cytokines and mediates in vitro and in vivo allergic inflammation. Mol Immunol 2010, 47:1010-1022.
    • (2010) Mol Immunol , vol.47 , pp. 1010-1022
    • Kim, Y.1    Eom, S.2    Kim, K.3    Lee, Y.S.4    Choe, J.5
  • 85
    • 0032557461 scopus 로고    scopus 로고
    • Identification of a transforming growth factor-beta1/bone morphogenetic protein 4 (TGF-beta1/BMP4) response element within the mouse tissue transglutaminase gene promoter
    • Ritter S.J., Davies P.J. Identification of a transforming growth factor-beta1/bone morphogenetic protein 4 (TGF-beta1/BMP4) response element within the mouse tissue transglutaminase gene promoter. J Biol Chem 1998, 273:12798-12806.
    • (1998) J Biol Chem , vol.273 , pp. 12798-12806
    • Ritter, S.J.1    Davies, P.J.2
  • 86
    • 0030974902 scopus 로고    scopus 로고
    • Latent transforming growth factor-beta binding protein domains involved in activation and transglutaminase-dependent cross-linking of latent transforming growth factor-beta
    • Nunes I., Gleizes P.E., Metz C.N., Rifkin D.B. Latent transforming growth factor-beta binding protein domains involved in activation and transglutaminase-dependent cross-linking of latent transforming growth factor-beta. J Cell Biol 1997, 136:1151-1163.
    • (1997) J Cell Biol , vol.136 , pp. 1151-1163
    • Nunes, I.1    Gleizes, P.E.2    Metz, C.N.3    Rifkin, D.B.4
  • 87
    • 70350380992 scopus 로고    scopus 로고
    • Increased TG2 expression can result in induction of transforming growth factor beta1, causing increased synthesis and deposition of matrix proteins, which can be regulated by nitric oxide
    • Telci D., Collighan R.J., Basaga H., Griffin M. Increased TG2 expression can result in induction of transforming growth factor beta1, causing increased synthesis and deposition of matrix proteins, which can be regulated by nitric oxide. J Biol Chem 2009, 284:29547-29558.
    • (2009) J Biol Chem , vol.284 , pp. 29547-29558
    • Telci, D.1    Collighan, R.J.2    Basaga, H.3    Griffin, M.4
  • 88
    • 70450222098 scopus 로고    scopus 로고
    • Matrix crosslinking forces tumor progression by enhancing integrin signaling
    • Levental K.R., Yu H., Kass L., Lakins J.N., Egeblad M., Erler J.T., et al. Matrix crosslinking forces tumor progression by enhancing integrin signaling. Cell 2009, 139:891-906.
    • (2009) Cell , vol.139 , pp. 891-906
    • Levental, K.R.1    Yu, H.2    Kass, L.3    Lakins, J.N.4    Egeblad, M.5    Erler, J.T.6
  • 89
    • 53349143213 scopus 로고    scopus 로고
    • Tissue transglutaminase protects epithelial ovarian cancer cells from cisplatin-induced apoptosis by promoting cell survival signaling
    • Cao L., Petrusca D.N., Satpathy M., Nakshatri H., Petrache I., Matei D. Tissue transglutaminase protects epithelial ovarian cancer cells from cisplatin-induced apoptosis by promoting cell survival signaling. Carcinogenesis 2008, 29:1893-1900.
    • (2008) Carcinogenesis , vol.29 , pp. 1893-1900
    • Cao, L.1    Petrusca, D.N.2    Satpathy, M.3    Nakshatri, H.4    Petrache, I.5    Matei, D.6
  • 90
    • 33644668017 scopus 로고    scopus 로고
    • Tissue transglutaminase 2 inhibition promotes cell death and chemosensitivity in glioblastomas
    • Yuan L., Choi K., Khosla C., Zheng X., Higashikubo R., Chicoine M.R., et al. Tissue transglutaminase 2 inhibition promotes cell death and chemosensitivity in glioblastomas. Mol Cancer Ther 2005, 4:1293-1302.
    • (2005) Mol Cancer Ther , vol.4 , pp. 1293-1302
    • Yuan, L.1    Choi, K.2    Khosla, C.3    Zheng, X.4    Higashikubo, R.5    Chicoine, M.R.6
  • 91
    • 67650221578 scopus 로고    scopus 로고
    • Regulation of platelet-derived growth factor receptor function by integrin-associated cell surface transglutaminase
    • Zemskov E.A., Loukinova E., Mikhailenko I., Coleman R.A., Strickland D.K., Belkin A.M. Regulation of platelet-derived growth factor receptor function by integrin-associated cell surface transglutaminase. J Biol Chem 2009, 284:16693-16703.
    • (2009) J Biol Chem , vol.284 , pp. 16693-16703
    • Zemskov, E.A.1    Loukinova, E.2    Mikhailenko, I.3    Coleman, R.A.4    Strickland, D.K.5    Belkin, A.M.6


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