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Volumn 319, Issue 10, 2013, Pages 1482-1490

A correlation between altered O-GlcNAcylation, migration and with changes in E-cadherin levels in ovarian cancer cells

Author keywords

Cell migration; E cadherin; O GlcNAcylation; O linked N acetylglucosamine transferase; Ovarian cancer

Indexed keywords

SMALL INTERFERING RNA; UVOMORULIN;

EID: 84877921283     PISSN: 00144827     EISSN: 10902422     Source Type: Journal    
DOI: 10.1016/j.yexcr.2013.03.013     Document Type: Article
Times cited : (40)

References (44)
  • 2
    • 0037300799 scopus 로고    scopus 로고
    • A role for N-acetylglucosamine as a nutrient sensor and mediator of insulin resistance
    • Wells L., Vosseller K., Hart G.W. A role for N-acetylglucosamine as a nutrient sensor and mediator of insulin resistance. Cell Mol. Life Sci. 2003, 60:222-228.
    • (2003) Cell Mol. Life Sci. , vol.60 , pp. 222-228
    • Wells, L.1    Vosseller, K.2    Hart, G.W.3
  • 3
    • 0029742775 scopus 로고    scopus 로고
    • Hexosamines and insulin resistance
    • McClain D.A., Crook E.D. Hexosamines and insulin resistance. Diabetes 1996, 45:1003-1009.
    • (1996) Diabetes , vol.45 , pp. 1003-1009
    • McClain, D.A.1    Crook, E.D.2
  • 5
    • 22244471058 scopus 로고    scopus 로고
    • O-GlcNAc modification on IRS-1 and Akt2 by PUGNAc inhibits their phosphorylation and induces in sulin resistance in rat primary adipocytes
    • Park S.Y., Ryu J., Lee W. O-GlcNAc modification on IRS-1 and Akt2 by PUGNAc inhibits their phosphorylation and induces in sulin resistance in rat primary adipocytes. Exp. Mol. Med. 2005, 37:220-229.
    • (2005) Exp. Mol. Med. , vol.37 , pp. 220-229
    • Park, S.Y.1    Ryu, J.2    Lee, W.3
  • 7
    • 33644873810 scopus 로고    scopus 로고
    • Hexosamines, insulin resistance, and the complications of diabetes: current status
    • Buse M.G. Hexosamines, insulin resistance, and the complications of diabetes: current status. Am. J. Physiol. Endocrinol. Metab. 2006, 290:E1-E8.
    • (2006) Am. J. Physiol. Endocrinol. Metab. , vol.290
    • Buse, M.G.1
  • 8
    • 0021960614 scopus 로고
    • The intracellular accumulation of UDP-N-acetylhexosamines is concomitant with the inability of human colon cancer cells to differentiate
    • Wice B.M., Trugnan G., Pinto M., Rousset M., Chevalier G., Dussaulx E., Lacroix B., Zweibaum A. The intracellular accumulation of UDP-N-acetylhexosamines is concomitant with the inability of human colon cancer cells to differentiate. J. Biol. Chem. 1985, 260:139-146.
    • (1985) J. Biol. Chem. , vol.260 , pp. 139-146
    • Wice, B.M.1    Trugnan, G.2    Pinto, M.3    Rousset, M.4    Chevalier, G.5    Dussaulx, E.6    Lacroix, B.7    Zweibaum, A.8
  • 9
    • 33749160125 scopus 로고    scopus 로고
    • Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability
    • Yang W.H., Kim J.E., Nam H.W., Ju J.W., Kim H.S., Kim Y.S., Cho J.W. Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability. Nat. Cell Biol. 2006, 8:1074-1083.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 1074-1083
    • Yang, W.H.1    Kim, J.E.2    Nam, H.W.3    Ju, J.W.4    Kim, H.S.5    Kim, Y.S.6    Cho, J.W.7
  • 10
    • 0001510491 scopus 로고    scopus 로고
    • The RB and p53 pathways in cancer
    • Sherr C.J., McCormick F. The RB and p53 pathways in cancer. Cancer Cell 2002, 2:103-112.
    • (2002) Cancer Cell , vol.2 , pp. 103-112
    • Sherr, C.J.1    McCormick, F.2
  • 11
    • 0029049198 scopus 로고
    • C-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas
    • Chou T.Y., Hart G.W., Dang C.V. c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas. J. Biol. Chem. 1995, 270:18961-18965.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18961-18965
    • Chou, T.Y.1    Hart, G.W.2    Dang, C.V.3
  • 13
    • 62549161375 scopus 로고    scopus 로고
    • Loss of p53 enhances catalytic activity of IKKbeta through O-linked beta-N-acetyl glucosamine modification
    • Kawauchi K., Araki K., Tobiume K., Tanaka N. Loss of p53 enhances catalytic activity of IKKbeta through O-linked beta-N-acetyl glucosamine modification. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:3431-3436.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 3431-3436
    • Kawauchi, K.1    Araki, K.2    Tobiume, K.3    Tanaka, N.4
  • 15
    • 65549090937 scopus 로고    scopus 로고
    • Drosophila IKK-related kinase Ik2 and Katanin p60-like 1 regulate dendrite pruning of sensory neuron during metamorphosis
    • Lee H.H., Jan L.Y., Jan Y.N. Drosophila IKK-related kinase Ik2 and Katanin p60-like 1 regulate dendrite pruning of sensory neuron during metamorphosis. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:6363-6368.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 6363-6368
    • Lee, H.H.1    Jan, L.Y.2    Jan, Y.N.3
  • 17
    • 77952429792 scopus 로고    scopus 로고
    • Nutrient sensor O-GlcNAc transferase regulates breast cancer tumorigenesis through targeting of the oncogenic transcription factor FoxM1
    • Caldwell S.A., Jackson S.R., Shahriari K.S., Lynch T.P., Sethi G., Walker S., Vosseller K., Reginato M.J. Nutrient sensor O-GlcNAc transferase regulates breast cancer tumorigenesis through targeting of the oncogenic transcription factor FoxM1. Oncogene 2010, 29:2831-2842.
    • (2010) Oncogene , vol.29 , pp. 2831-2842
    • Caldwell, S.A.1    Jackson, S.R.2    Shahriari, K.S.3    Lynch, T.P.4    Sethi, G.5    Walker, S.6    Vosseller, K.7    Reginato, M.J.8
  • 19
    • 77953713601 scopus 로고    scopus 로고
    • Modulation of transcription factor function by O-GlcNAc modification
    • Ozcan S., Andrali S.S., Cantrell J.E. Modulation of transcription factor function by O-GlcNAc modification. Biochim. Biophys. Acta 2010, 1799:353-364.
    • (2010) Biochim. Biophys. Acta , vol.1799 , pp. 353-364
    • Ozcan, S.1    Andrali, S.S.2    Cantrell, J.E.3
  • 20
    • 25444501339 scopus 로고    scopus 로고
    • Perturbations in O-linked beta-N-acetylglucosamine protein modification cause severe defects in mitotic progression and cytokinesis
    • Slawson C., Zachara N.E., Vosseller K., Cheung W.D., Lane M.D., Hart G.W. Perturbations in O-linked beta-N-acetylglucosamine protein modification cause severe defects in mitotic progression and cytokinesis. J. Biol. Chem. 2005, 280:32944-32956.
    • (2005) J. Biol. Chem. , vol.280 , pp. 32944-32956
    • Slawson, C.1    Zachara, N.E.2    Vosseller, K.3    Cheung, W.D.4    Lane, M.D.5    Hart, G.W.6
  • 22
    • 33744953426 scopus 로고    scopus 로고
    • Stabilization of plakoglobin and enhanced keratinocyte cell-cell adhesion by intracellular O-glycosylation
    • Hu P., Berkowitz P., Madden V.J., Rubenstein D.S. Stabilization of plakoglobin and enhanced keratinocyte cell-cell adhesion by intracellular O-glycosylation. J. Biol. Chem. 2006, 281:12786-12791.
    • (2006) J. Biol. Chem. , vol.281 , pp. 12786-12791
    • Hu, P.1    Berkowitz, P.2    Madden, V.J.3    Rubenstein, D.S.4
  • 23
    • 0035503219 scopus 로고    scopus 로고
    • Cytoplasmic O-glycosylation prevents cell surface transport of E-cadherin during apoptosis
    • Zhu W., Leber B., Andrews D.W. Cytoplasmic O-glycosylation prevents cell surface transport of E-cadherin during apoptosis. EMBO J. 2001, 20:5999-6007.
    • (2001) EMBO J. , vol.20 , pp. 5999-6007
    • Zhu, W.1    Leber, B.2    Andrews, D.W.3
  • 24
    • 79751525993 scopus 로고    scopus 로고
    • Cong, Wengong Yu. O-GlcNAcylation is a novel regulator of lung and colon cancer Malignancy
    • Wenyi Mi Yuchao, Gu Cuifang, Han Haiyan, Liu Qiong, Fan Xinling, Zhang Qi Cong, Wengong Yu. O-GlcNAcylation is a novel regulator of lung and colon cancer Malignancy. Biochim. Biophys. Acta 2011, 1812:514-519.
    • (2011) Biochim. Biophys. Acta , vol.1812 , pp. 514-519
    • Wenyi Mi, Y.1    Gu, C.2    Han, H.3    Liu, Q.4    Fan, X.5    Zhang, Q.6
  • 25
    • 84859484538 scopus 로고    scopus 로고
    • Critical role of O-GlcNAc transferase in prostate cancer invasion, angiogenesis and metastasis
    • Lynch Thomas P., Ferrer Christina M., RaElle Jackson S., Shahriari Kristina S., Vosseller Keith, Reginato Mauricio J. Critical role of O-GlcNAc transferase in prostate cancer invasion, angiogenesis and metastasis. J. Biol. Chem. 2012, 287:11070-11081.
    • (2012) J. Biol. Chem. , vol.287 , pp. 11070-11081
    • Lynch, T.P.1    Ferrer, C.M.2    RaElle Jackson, S.3    Shahriari, K.S.4    Vosseller, K.5    Reginato, M.J.6
  • 26
    • 34548588406 scopus 로고    scopus 로고
    • Down-regulation of Forkhead Box M1 transcription factor leads to the inhibition of invasion and angiogenesis of pancreatic cancer cells
    • Wang Z., Banerjee S., Kong D., Li Y., Sarkar F.H. Down-regulation of Forkhead Box M1 transcription factor leads to the inhibition of invasion and angiogenesis of pancreatic cancer cells. Cancer Res. 2007, 67:8293-8300.
    • (2007) Cancer Res. , vol.67 , pp. 8293-8300
    • Wang, Z.1    Banerjee, S.2    Kong, D.3    Li, Y.4    Sarkar, F.H.5
  • 28
    • 78649791823 scopus 로고    scopus 로고
    • Altered O-GlcNAc modification and phosphorylation of mitochondrial proteins in myoblast cells exposed to high glucose
    • Gu Y., Ande S.R., Mishra S. Altered O-GlcNAc modification and phosphorylation of mitochondrial proteins in myoblast cells exposed to high glucose. Arch. Biochem. Biophys. 2011, 505:98-104.
    • (2011) Arch. Biochem. Biophys. , vol.505 , pp. 98-104
    • Gu, Y.1    Ande, S.R.2    Mishra, S.3
  • 29
    • 84865276011 scopus 로고    scopus 로고
    • O-Linked beta-N-Acetylglucosaminylation (O-GlcNAcylation) in primary and metastatic colorectal cancer clones and effect of N-Acetyl-beta-D-glucosaminidase silencing on cell phenotype and transcriptome
    • Yehezkel G., Cohen L., Kliger A., Manor E., Khalaila I. O-Linked beta-N-Acetylglucosaminylation (O-GlcNAcylation) in primary and metastatic colorectal cancer clones and effect of N-Acetyl-beta-D-glucosaminidase silencing on cell phenotype and transcriptome. J. Biol. Chem. 2012, 287:28755-28769.
    • (2012) J. Biol. Chem. , vol.287 , pp. 28755-28769
    • Yehezkel, G.1    Cohen, L.2    Kliger, A.3    Manor, E.4    Khalaila, I.5
  • 30
    • 84864766367 scopus 로고    scopus 로고
    • O-GlcNAcylation plays a role in tumor recurrence of hepatocellular carcinoma following liver transplantation
    • Zhu Q., Zhou L., Yang Z., Lai M., Xie H., Wu L., Xing C., Zhang F., Zheng S. O-GlcNAcylation plays a role in tumor recurrence of hepatocellular carcinoma following liver transplantation. Med. Oncol. 2011, 29:985-993.
    • (2011) Med. Oncol. , vol.29 , pp. 985-993
    • Zhu, Q.1    Zhou, L.2    Yang, Z.3    Lai, M.4    Xie, H.5    Wu, L.6    Xing, C.7    Zhang, F.8    Zheng, S.9
  • 32
    • 78149268785 scopus 로고    scopus 로고
    • Glucosamine treatment-mediated O-GlcNAc modification of paxillin depends on adhesion state of rat insulinoma INS-1 Cells
    • Kwak Tae Kyoung, Kim Hyeonjung, Jung Oisun, Lee Sin-Ae, Kang Minkyung, Kim Hyun Jeong, Park Ji-Min, Kim Sung-Hoon, Lee Jung Weon Glucosamine treatment-mediated O-GlcNAc modification of paxillin depends on adhesion state of rat insulinoma INS-1 Cells. J. Biol. Chem. 2010, 285:36021-36031.
    • (2010) J. Biol. Chem. , vol.285 , pp. 36021-36031
    • Kwak, T.K.1    Kim, H.2    Jung, O.3    Lee, S.-A.4    Kang, M.5    Kim, H.J.6    Park, J.-M.7    Kim, S.-H.8    Lee, J.W.9
  • 33
    • 50049117442 scopus 로고    scopus 로고
    • O-GlcNAc-glycosylation of β-catenin regulates its nuclear localization and transcriptional activity
    • Sayat R., Leber B., Grubac V., Wiltshire L., Persad S. O-GlcNAc-glycosylation of β-catenin regulates its nuclear localization and transcriptional activity. Exp. Cell Res. 2008, 314:2774-2787.
    • (2008) Exp. Cell Res. , vol.314 , pp. 2774-2787
    • Sayat, R.1    Leber, B.2    Grubac, V.3    Wiltshire, L.4    Persad, S.5
  • 34
    • 0036462599 scopus 로고    scopus 로고
    • The emerging significance of O-GlcNAc in cellular regulation
    • Zachara N.E., Hart G.W. The emerging significance of O-GlcNAc in cellular regulation. Chem. Rev. 2002, 102:431-438.
    • (2002) Chem. Rev. , vol.102 , pp. 431-438
    • Zachara, N.E.1    Hart, G.W.2
  • 35
    • 72449187655 scopus 로고    scopus 로고
    • The intersections between O-GlcNAcylation and phosphorylation: implications for multiple signaling pathways
    • Zeidan Q., Hart G.W. The intersections between O-GlcNAcylation and phosphorylation: implications for multiple signaling pathways. J. Cell Sci. 2010, 123:13-22.
    • (2010) J. Cell Sci. , vol.123 , pp. 13-22
    • Zeidan, Q.1    Hart, G.W.2
  • 36
    • 40949083086 scopus 로고    scopus 로고
    • Hexosamine biosynthesis and protein O-glycosylation: the first line of defense against stress, ischemia, and trauma
    • Chatham J.C., Not L.G., Fulop N., Marchase R.B. Hexosamine biosynthesis and protein O-glycosylation: the first line of defense against stress, ischemia, and trauma. Shock 2008, 29:431-440.
    • (2008) Shock , vol.29 , pp. 431-440
    • Chatham, J.C.1    Not, L.G.2    Fulop, N.3    Marchase, R.B.4
  • 37
    • 34247583996 scopus 로고    scopus 로고
    • Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins
    • Hart G.W., Housley M.P., Slawson C. Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins. Nature 2007, 446:1017-1022.
    • (2007) Nature , vol.446 , pp. 1017-1022
    • Hart, G.W.1    Housley, M.P.2    Slawson, C.3
  • 38
    • 77953566942 scopus 로고    scopus 로고
    • Nuclear factor-kappaB signaling and ezrin are essential for L1-mediated metastasis of colon cancer cells
    • Gavert N., Ben-Shmuel A., Lemmon V., Brabletz T., Ben-Ze'ev A. Nuclear factor-kappaB signaling and ezrin are essential for L1-mediated metastasis of colon cancer cells. J. Cell Sci. 2010, 123:2135-2143.
    • (2010) J. Cell Sci. , vol.123 , pp. 2135-2143
    • Gavert, N.1    Ben-Shmuel, A.2    Lemmon, V.3    Brabletz, T.4    Ben-Ze'ev, A.5
  • 39
    • 35548932457 scopus 로고    scopus 로고
    • Structure and mechanism of cadherins and catenins in cell-cell contacts
    • Pokutta S., Weis W.I. Structure and mechanism of cadherins and catenins in cell-cell contacts. Annu. Rev. Cell Dev. Biol. 2007, 23:237-261.
    • (2007) Annu. Rev. Cell Dev. Biol. , vol.23 , pp. 237-261
    • Pokutta, S.1    Weis, W.I.2
  • 40
    • 0033593803 scopus 로고    scopus 로고
    • Coupling assembly of the E-cadherin/β-catenin complex to efficient endoplasmic reticulum exit and basal-lateal membrane targeting of E-cadherin in polarized MDCK cells
    • Chen Y.T., Stewart D.B., Nelson W.J. Coupling assembly of the E-cadherin/β-catenin complex to efficient endoplasmic reticulum exit and basal-lateal membrane targeting of E-cadherin in polarized MDCK cells. J. Cell. Biol. 1999, 144:687-699.
    • (1999) J. Cell. Biol. , vol.144 , pp. 687-699
    • Chen, Y.T.1    Stewart, D.B.2    Nelson, W.J.3
  • 44
    • 79251611901 scopus 로고    scopus 로고
    • Structure of human O-GlcNAc transferase and its complex with a peptide substrate
    • Lazarus M.B., Nam Y., Jiang J., Sliz P., Walker S. Structure of human O-GlcNAc transferase and its complex with a peptide substrate. Nature 2011, 469:564-567.
    • (2011) Nature , vol.469 , pp. 564-567
    • Lazarus, M.B.1    Nam, Y.2    Jiang, J.3    Sliz, P.4    Walker, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.