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Volumn 274, Issue 2, 2009, Pages 201-207

Depletion of nucleophosmin via transglutaminase 2 cross-linking increases drug resistance in cancer cells

Author keywords

B23; Drug resistance; Nucleophosmin; Polymerization; Transglutaminase

Indexed keywords

CYSTAMINE; DOXORUBICIN; NUCLEOPHOSMIN; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 2; UBIQUITIN;

EID: 58149463059     PISSN: 03043835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.canlet.2008.09.007     Document Type: Article
Times cited : (24)

References (35)
  • 2
    • 0034924217 scopus 로고    scopus 로고
    • Physiopathology and regulation of factor XIII
    • Ichinose A. Physiopathology and regulation of factor XIII. Thromb. Haemost. 86 (2001) 57-65
    • (2001) Thromb. Haemost. , vol.86 , pp. 57-65
    • Ichinose, A.1
  • 3
    • 0034093354 scopus 로고    scopus 로고
    • Protein crosslinking in assembly and remodelling of extracellular matrices: the role of transglutaminases
    • Aeschlimann D., and Thomazy V. Protein crosslinking in assembly and remodelling of extracellular matrices: the role of transglutaminases. Connect. Tissue Res. 41 (2000) 1-27
    • (2000) Connect. Tissue Res. , vol.41 , pp. 1-27
    • Aeschlimann, D.1    Thomazy, V.2
  • 4
    • 0035469864 scopus 로고    scopus 로고
    • Cell surface tissue transglutaminase is involved in adhesion and migration of monocytic cells on fibronectin
    • Akimov S.S., and Belkin A.M. Cell surface tissue transglutaminase is involved in adhesion and migration of monocytic cells on fibronectin. Blood 98 (2001) 1567-1576
    • (2001) Blood , vol.98 , pp. 1567-1576
    • Akimov, S.S.1    Belkin, A.M.2
  • 5
    • 0034675888 scopus 로고    scopus 로고
    • The complexity and redundancy of epithelial barrier function
    • Steinert P.M. The complexity and redundancy of epithelial barrier function. J. Cell Biol. 151 (2000) F5-F8
    • (2000) J. Cell Biol. , vol.151
    • Steinert, P.M.1
  • 6
    • 0023159034 scopus 로고
    • Induction and activation of tissue transglutaminase during programmed cell death
    • Fesus L., Thomazy V., and Falus A. Induction and activation of tissue transglutaminase during programmed cell death. FEBS Lett. 224 (1987) 104-108
    • (1987) FEBS Lett. , vol.224 , pp. 104-108
    • Fesus, L.1    Thomazy, V.2    Falus, A.3
  • 7
    • 0028108616 scopus 로고
    • High levels of transglutaminase expression in doxorubicin-resistant human breast carcinoma cells
    • Mehta K. High levels of transglutaminase expression in doxorubicin-resistant human breast carcinoma cells. Int. J. Cancer 58 (1994) 400-406
    • (1994) Int. J. Cancer , vol.58 , pp. 400-406
    • Mehta, K.1
  • 8
    • 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., and Sahin A.A. Prognostic significance of tissue transglutaminase in drug resistant and metastatic breast cancer. Clin. Cancer Res. 10 (2004) 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
  • 9
    • 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., Page R.L., and Cerione R.A. Augmentation of tissue transglutaminase expression and activation by epidermal growth factor inhibit doxorubicin-induced apoptosis in human breast cancer cells. J. Biol. Chem. 279 (2004) 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    Page, R.L.7    Cerione, R.A.8
  • 10
    • 11144233953 scopus 로고    scopus 로고
    • Transglutaminase 2 induces nuclear factor-kappaB activation via a novel pathway in BV-2 microglia
    • Lee J., Kim Y.S., Choi D.H., Bang M.S., Han T.R., Joh T.H., and Kim S.Y. Transglutaminase 2 induces nuclear factor-kappaB activation via a novel pathway in BV-2 microglia. J. Biol. Chem. 279 (2004) 53725-53735
    • (2004) J. Biol. Chem. , vol.279 , pp. 53725-53735
    • Lee, J.1    Kim, Y.S.2    Choi, D.H.3    Bang, M.S.4    Han, T.R.5    Joh, T.H.6    Kim, S.Y.7
  • 11
    • 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., and Kim S.Y. Reversal of drug resistance in breast cancer cells by transglutaminase 2 inhibition and nuclear factor-kappaB inactivation. Cancer Res. 66 (2006) 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
  • 12
    • 0023261706 scopus 로고
    • Identification of a prominent nuclear protein associated with proliferation of normal and malignant B cells
    • Feuerstein N., and Mond J.J. Identification of a prominent nuclear protein associated with proliferation of normal and malignant B cells. J. Immunol. 139 (1987) 1818-1822
    • (1987) J. Immunol. , vol.139 , pp. 1818-1822
    • Feuerstein, N.1    Mond, J.J.2
  • 13
    • 0023369370 scopus 로고
    • A constitutive nucleolar protein identified as a member of the nucleoplasmin family
    • Schmidt-Zachmann M.S., Hügle-Dörr B., and Franke W.W. A constitutive nucleolar protein identified as a member of the nucleoplasmin family. EMBO J. 6 (1987) 1881-1890
    • (1987) EMBO J. , vol.6 , pp. 1881-1890
    • Schmidt-Zachmann, M.S.1    Hügle-Dörr, B.2    Franke, W.W.3
  • 14
    • 0023764934 scopus 로고
    • DNA cloning and amino acid sequence determination of a major constituent protein of mammalian nucleoli correspondence of the nucleoplasmin-related protein NO38 to mammalian protein B23
    • Schmidt-Zachmann M.S., and Franke W.W. DNA cloning and amino acid sequence determination of a major constituent protein of mammalian nucleoli correspondence of the nucleoplasmin-related protein NO38 to mammalian protein B23. Chromosoma 96 (1988) 417-426
    • (1988) Chromosoma , vol.96 , pp. 417-426
    • Schmidt-Zachmann, M.S.1    Franke, W.W.2
  • 15
    • 0024595908 scopus 로고
    • Characterization of the cDNA encoding human nucleophosmin and studies of its role in normal and abnormal growth
    • Chan W.Y., Liu Q.R., Borjigin J., Busch H., Rennert O.M., Tease L.A., and Chan P.K. Characterization of the cDNA encoding human nucleophosmin and studies of its role in normal and abnormal growth. Biochemistry 28 (1989) 1033-1039
    • (1989) Biochemistry , vol.28 , pp. 1033-1039
    • Chan, W.Y.1    Liu, Q.R.2    Borjigin, J.3    Busch, H.4    Rennert, O.M.5    Tease, L.A.6    Chan, P.K.7
  • 16
    • 0036302062 scopus 로고    scopus 로고
    • Nucleophosmin regulates the stability and transcriptional activity of p53
    • Colombo E., Marine J.C., Danovi D., Falini B., and Pelicci P.G. Nucleophosmin regulates the stability and transcriptional activity of p53. Nat. Cell Biol. 4 (2002) 529-533
    • (2002) Nat. Cell Biol. , vol.4 , pp. 529-533
    • Colombo, E.1    Marine, J.C.2    Danovi, D.3    Falini, B.4    Pelicci, P.G.5
  • 17
    • 0036198225 scopus 로고    scopus 로고
    • Resistance to UV-induced cell-killing in nucleophosmin/B23 over-expressed NIH 3T3 fibroblasts: enhancement of DNA repair and up-regulation of PCNA in association with nucleophosmin/B23 over-expression
    • Wu M.H., Chang J.H., and Yung B.Y. Resistance to UV-induced cell-killing in nucleophosmin/B23 over-expressed NIH 3T3 fibroblasts: enhancement of DNA repair and up-regulation of PCNA in association with nucleophosmin/B23 over-expression. Carcinogenesis 23 (2002) 93-100
    • (2002) Carcinogenesis , vol.23 , pp. 93-100
    • Wu, M.H.1    Chang, J.H.2    Yung, B.Y.3
  • 21
    • 0030022316 scopus 로고    scopus 로고
    • The t(5;17) variant of acute promyelocytic leukemia expresses a nucleophosmin-retinoic acid receptor fusion
    • Redner R.L., Rush E.A., Faas S., Rudert W.A., and Corey S.J. The t(5;17) variant of acute promyelocytic leukemia expresses a nucleophosmin-retinoic acid receptor fusion. Blood 87 (1996) 882-886
    • (1996) Blood , vol.87 , pp. 882-886
    • Redner, R.L.1    Rush, E.A.2    Faas, S.3    Rudert, W.A.4    Corey, S.J.5
  • 24
    • 38149137370 scopus 로고    scopus 로고
    • Proteomic analysis of high-molecular-weight protein polymers in a doxorubicin-resistant breast-cancer cell line
    • Park S.S., Kim D.S., Park K.S., Song H.J., and Kim S.Y. Proteomic analysis of high-molecular-weight protein polymers in a doxorubicin-resistant breast-cancer cell line. Proteomics Clin. Appl. 1 (2007) 555-560
    • (2007) Proteomics Clin. Appl. , vol.1 , pp. 555-560
    • Park, S.S.1    Kim, D.S.2    Park, K.S.3    Song, H.J.4    Kim, S.Y.5
  • 25
    • 0032917157 scopus 로고    scopus 로고
    • Nucleolar protein B23 has molecular chaperone active ties
    • Szebeni A., and Olson M.O. Nucleolar protein B23 has molecular chaperone active ties. Protein Sci. 8 (1999) 905-912
    • (1999) Protein Sci. , vol.8 , pp. 905-912
    • Szebeni, A.1    Olson, M.O.2
  • 26
    • 33744496065 scopus 로고    scopus 로고
    • Transglutaminase 2 in inflammation
    • Kim S.Y. Transglutaminase 2 in inflammation. Front Biosci. 11 (2006) 3026-3035
    • (2006) Front Biosci. , vol.11 , pp. 3026-3035
    • Kim, S.Y.1
  • 27
    • 0034637578 scopus 로고    scopus 로고
    • Mapping the functional domains of nucleolar protein B23
    • Hingorani K., Szebeni A., and Olson M.O. Mapping the functional domains of nucleolar protein B23. J. Biol. Chem. 275 (2000) 24451-24457
    • (2000) J. Biol. Chem. , vol.275 , pp. 24451-24457
    • Hingorani, K.1    Szebeni, A.2    Olson, M.O.3
  • 28
    • 14844340165 scopus 로고    scopus 로고
    • N-terminal control of small heat shock protein oligomerization: changes in aggregate size and chaperone-like function
    • Eifert C., Burgio M.R., Bennett P.M., Salerno J.C., and Koretz J.F. N-terminal control of small heat shock protein oligomerization: changes in aggregate size and chaperone-like function. Biochim. Biophys. Acta 1748 (2005) 146-156
    • (2005) Biochim. Biophys. Acta , vol.1748 , pp. 146-156
    • Eifert, C.1    Burgio, M.R.2    Bennett, P.M.3    Salerno, J.C.4    Koretz, J.F.5
  • 29
    • 33646858986 scopus 로고    scopus 로고
    • Implications of increased tissue transglutaminase (TG2) expression in drug-resistant breast cancer (MCF-7) cells
    • Herman J.F., Mangala L.S., and Mehta K. Implications of increased tissue transglutaminase (TG2) expression in drug-resistant breast cancer (MCF-7) cells. Oncogene 25 (2006) 3049-3058
    • (2006) Oncogene , vol.25 , pp. 3049-3058
    • Herman, J.F.1    Mangala, L.S.2    Mehta, K.3
  • 30
    • 11844299691 scopus 로고    scopus 로고
    • Release of nucleophosmin from the nucleus: involvement in aloe-emodin-induced human lung non small carcinoma cell apoptosis
    • Lee H.Z., Wu C.H., and Chang S.P. Release of nucleophosmin from the nucleus: involvement in aloe-emodin-induced human lung non small carcinoma cell apoptosis. Int. J. Cancer 113 (2005) 971-976
    • (2005) Int. J. Cancer , vol.113 , pp. 971-976
    • Lee, H.Z.1    Wu, C.H.2    Chang, S.P.3
  • 31
    • 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., and Mehta K. Tissue transglutaminase regulates focal adhesion kinase/AKT activation by modulating PTEN expression in pancreatic cancer cells. Clin. Cancer Res. 14 (2008) 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    Mehta, K.7
  • 32
    • 35748929414 scopus 로고    scopus 로고
    • Cytosolic accumulation of HSP60 during apoptosis with or without apparent mitochondrial release: evidence that its pro-apoptotic or pro-survival functions involve differential interactions with caspase-3
    • Chandra D., Choy G., and Tang D.G. Cytosolic accumulation of HSP60 during apoptosis with or without apparent mitochondrial release: evidence that its pro-apoptotic or pro-survival functions involve differential interactions with caspase-3. J. Biol. Chem. 282 (2007) 31289-31301
    • (2007) J. Biol. Chem. , vol.282 , pp. 31289-31301
    • Chandra, D.1    Choy, G.2    Tang, D.G.3
  • 33
    • 0041355325 scopus 로고    scopus 로고
    • Proteomics identification of acyl-acceptor and acyl-donor substrates for transglutaminase in a human intestinal epithelial cell line implications for celiac disease
    • Orrù S., Caputo I., D'Amato A., Ruoppolo M., and Esposito C. Proteomics identification of acyl-acceptor and acyl-donor substrates for transglutaminase in a human intestinal epithelial cell line implications for celiac disease. J. Biol. Chem. 278 (2003) 31766-31773
    • (2003) J. Biol. Chem. , vol.278 , pp. 31766-31773
    • Orrù, S.1    Caputo, I.2    D'Amato, A.3    Ruoppolo, M.4    Esposito, C.5
  • 34
    • 0032929487 scopus 로고    scopus 로고
    • Reduction of transglutaminase 2 expression is associated with an induction of drug sensitivity in the PC-14 human lung cancer cell line
    • Han J.A., and Park S.C. Reduction of transglutaminase 2 expression is associated with an induction of drug sensitivity in the PC-14 human lung cancer cell line. J. Cancer Res. Clin. Oncol. 125 (1999) 89-95
    • (1999) J. Cancer Res. Clin. Oncol. , vol.125 , pp. 89-95
    • Han, J.A.1    Park, S.C.2
  • 35
    • 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., and Mehta K. Increased expression of tissue transglutaminase in pancreatic ductal adenocarcinoma and its implications in drug resistance and metastasis. Cancer Res. 66 (2006) 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    Mehta, K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.