메뉴 건너뛰기




Volumn 1840, Issue 1, 2014, Pages 191-198

Implications of the O-GlcNAc modification in the regulation of nuclear apoptosis in T cells

Author keywords

Apoptosis; DFF; DFF45; O (2 acetamidO 2 deoxy D glucopyranosylidene) amino N phenylcarbamate; O linked N acetylglucosamine; TBT

Indexed keywords

2 ACETAMIDO 2 DEOXY GLUCOPYRANOSYLIDENE AMINO N PHENYLCARBAMATE; ACETYLGLUCOSAMINIDASE; CASPASE; CASPASE ACTIVATED DEOXYRIBONUCLEASE; CELL PROTEIN; DFF45 PROTEIN; GLUCOSAMINE; GLYCOSIDASE INHIBITOR; N ACETYLGLUCOSAMINE; TRIBUTYLTIN; UNCLASSIFIED DRUG; WHEAT GERM AGGLUTININ;

EID: 84885340029     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2013.09.011     Document Type: Article
Times cited : (14)

References (37)
  • 1
  • 4
    • 0030884480 scopus 로고    scopus 로고
    • Increases in mRNA levels of glucose transporters types 1 and 3 in Ehrlich ascites tumor cells during tumor development
    • DOI 10.1002/(SICI)1097-4644(19971001)67:1<131::AID-JCB13>3.0.CO;2-K
    • K.K. Au, E. Liong, J.Y. Li, P.S. Li, C.C. Liew, T.T. Kwok, Y.M. Choy, C.Y. Lee, and K.P. Fung Increases in mRNA levels of glucose transporters types 1 and 3 in Ehrlich ascites tumor cells during tumor development J. Cell. Biochem. 67 1997 131 135 (Pubitemid 27430330)
    • (1997) Journal of Cellular Biochemistry , vol.67 , Issue.1 , pp. 131-135
    • Au, K.K.1    Liong, E.2    Li, J.Y.3    Li, P.S.4    Liew, C.C.5    Kwok, T.T.6    Choy, Y.M.7    Lee, C.Y.8    Fung, K.P.9
  • 5
    • 77449100681 scopus 로고    scopus 로고
    • Neuronal apoptosis by prolyl hydroxylation: Implication in nervous system tumours and the Warburg conundrum
    • S. Schlisio Neuronal apoptosis by prolyl hydroxylation: implication in nervous system tumours and the Warburg conundrum J. Cell. Mol. Med. 13 2009 4104 4112
    • (2009) J. Cell. Mol. Med. , vol.13 , pp. 4104-4112
    • Schlisio, S.1
  • 6
    • 0032488979 scopus 로고    scopus 로고
    • Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-β-N- acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-D- glucopyranosylidene) amino-N-phenylcarbamate
    • DOI 10.1074/jbc.273.6.3611
    • R.S. Haltiwanger, K. Grove, and G.A. Philipsberg Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptideo-GlcNAc-beta-N-acetylglucosaminidase inhibitoro-(2-acetamido-2-deoxy- dglucopyranosylidene)amino-N-phenylcarbamate J. Biol. Chem. 273 1998 3611 3617 (Pubitemid 28109786)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.6 , pp. 3611-3617
    • Haltiwanger, R.S.1    Grove, K.2    Philipsberg, G.A.3
  • 7
    • 45149112314 scopus 로고    scopus 로고
    • O-GlcNAc modulation at Akt1 Ser473 correlates with apoptosis of murine pancreatic β cells
    • DOI 10.1016/j.yexcr.2008.04.014, PII S0014482708001791
    • E.-S. Kang, D. Han, J. Park, T.K. Kwak, M.-A. Oh, S.-A. Lee, S. Choi, Z.Y. Park, Y. Kim, and J.W. Lee O-GlcNAc modulation at Akt1 Ser473 correlates with apoptosis of murine pancreatic [beta] cells Exp. Cell Res. 314 2008 2238 2248 (Pubitemid 351833109)
    • (2008) Experimental Cell Research , vol.314 , Issue.11-12 , pp. 2238-2248
    • Kang, E.-S.1    Han, D.2    Park, J.3    Kwak, T.K.4    Oh, M.-A.5    Lee, S.-A.6    Choi, S.7    Park, Z.Y.8    Kim, Y.9    Lee, J.W.10
  • 8
    • 70349270677 scopus 로고    scopus 로고
    • O-GlcNAc cycling: Implications for neurodegenerative disorders
    • B.D. Lazarus, D.C. Love, and J.A. Hanover O-GlcNAc cycling: Implications for neurodegenerative disorders Int. J. Biochem. Cell Biol. 41 2009 2134 2146
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 2134-2146
    • Lazarus, B.D.1    Love, D.C.2    Hanover, J.A.3
  • 10
    • 33846317766 scopus 로고    scopus 로고
    • Glucosamine protects neonatal cardiomyocytes from ischemia-reperfusion injury via increased protein-associated O-GlcNAc
    • V. Champattanachai, R.B. Marchase, and J.C. Chatham Glucosamine protects neonatal cardiomyocytes from ischemia-reperfusion injury via increased protein-associated O-GlcNAc Am. J. Physiol. Cell Physiol. 292 2007 C178 C187
    • (2007) Am. J. Physiol. Cell Physiol. , vol.292
    • Champattanachai, V.1    Marchase, R.B.2    Chatham, J.C.3
  • 11
    • 47249102179 scopus 로고    scopus 로고
    • Glucosamine protects neonatal cardiomyocytes from ischemia-reperfusion injury via increased protein O-GlcNAc and increased mitochondrial Bcl-2
    • V. Champattanachai, R.B. Marchase, and J.C. Chatham Glucosamine protects neonatal cardiomyocytes from ischemia-reperfusion injury via increased protein O-GlcNAc and increased mitochondrial Bcl-2 Am. J. Physiol. Cell Physiol. 294 2008 C1509 C1520
    • (2008) Am. J. Physiol. Cell Physiol. , vol.294
    • Champattanachai, V.1    Marchase, R.B.2    Chatham, J.C.3
  • 12
    • 34250841706 scopus 로고    scopus 로고
    • Glucosamine cardioprotection in perfused rat hearts associated with increased O-linked N-acetylglucosamine protein modification and altered p38 activation
    • N. Fülöp, Z. Zhang, R.B. Marchase, and J.C. Chatham Glucosamine cardioprotection in perfused rat hearts associated with increased O-linked N-acetylglucosamine protein modification and altered p38 activation Am. J. Physiol. Heart Circ. Physiol. 292 2007 H2227 H2236
    • (2007) Am. J. Physiol. Heart Circ. Physiol. , vol.292
    • Fülöp, N.1    Zhang, Z.2    Marchase, R.B.3    Chatham, J.C.4
  • 13
    • 34548424133 scopus 로고    scopus 로고
    • Increased O-GlcNAc levels during reperfusion lead to improved functional recovery and reduced calpain proteolysis
    • J. Liu, R.B. Marchase, and J.C. Chatham Increased O-GlcNAc levels during reperfusion lead to improved functional recovery and reduced calpain proteolysis Am. J. Physiol. Heart Circ. Physiol. 293 2007 H1391 H1399
    • (2007) Am. J. Physiol. Heart Circ. Physiol. , vol.293
    • Liu, J.1    Marchase, R.B.2    Chatham, J.C.3
  • 15
    • 3042613480 scopus 로고    scopus 로고
    • O-GlcNAc a sensor of cellular state: The role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress
    • DOI 10.1016/j.bbagen.2004.03.016, PII S0304416504001023
    • N.E. Zachara, and G.W. Hart O-GlcNAc a sensor of cellular state: the role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress Biochim. Biophys. Acta Gen. Subj. 1673 2004 13 28 (Pubitemid 38844791)
    • (2004) Biochimica et Biophysica Acta - General Subjects , vol.1673 , Issue.1-2 , pp. 13-28
    • Zachara, N.E.1    Hart, G.W.2
  • 16
    • 44449166220 scopus 로고    scopus 로고
    • Glucose deprivation stimulates O-GlcNAc modification of proteins through up-regulation of O-linked N-acetylglucosaminyltransferase
    • R.P. Taylor, G.J. Parker, M.W. Hazel, Y. Soesanto, W. Fuller, M.J. Yazzie, and D.A. McClain Glucose deprivation stimulates O-GlcNAc modification of proteins through up-regulation of O-linked N-acetylglucosaminyltransferase J. Biol. Chem. 283 2008 6050 6057
    • (2008) J. Biol. Chem. , vol.283 , pp. 6050-6057
    • Taylor, R.P.1    Parker, G.J.2    Hazel, M.W.3    Soesanto, Y.4    Fuller, W.5    Yazzie, M.J.6    McClain, D.A.7
  • 17
    • 0030916417 scopus 로고    scopus 로고
    • DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis
    • X. Liu, H. Zou, C. Slaughter, and X. Wang DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis Cell 89 1997 175 184 (Pubitemid 27199890)
    • (1997) Cell , vol.89 , Issue.2 , pp. 175-184
    • Liu, X.1    Zou, H.2    Slaughter, C.3    Wang, X.4
  • 18
    • 28844492992 scopus 로고    scopus 로고
    • Oligomerization state of the DNA fragmentation factor in normal and apoptotic cells
    • DOI 10.1074/jbc.M502220200
    • D. Lechardeur, D. Dougaparsad, C. Nemes, and Gl Lukacs Oligomerization state of the DNA fragmentation factor in normal and apoptotic cells J. Cell Biol. 280 2005 40216 40225 (Pubitemid 41779159)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.48 , pp. 40216-40225
    • Lechardeur, D.1    Dougaparsad, S.2    Nemes, C.3    Lukacs, G.L.4
  • 19
    • 4344594837 scopus 로고    scopus 로고
    • Apoptotic volume decrease, pH acidification and chloride channel activation during apoptosis requires CD45 expression in HPB-ALL T cells
    • DOI 10.1023/B:APPT.0000038031.84705.84
    • G. Dupéré-Minier, C. Hamelin, P. Desharnais, and J. Bernier Apoptotic volume decrease, pH acidification and chloride channel activation during apoptosis requires CD45 expression in HPB-ALL T cells Apoptosis 9 2004 543 551 (Pubitemid 39158630)
    • (2004) Apoptosis , vol.9 , Issue.5 , pp. 543-551
    • Dupere-Minier, G.1    Hamelin, C.2    Desharnais, P.3    Bernier, J.4
  • 20
    • 38649093325 scopus 로고    scopus 로고
    • Involvement of CD45 in DNA fragmentation in apoptosis induced by mitochondrial perturbing agents
    • P. Desharnais, G. Dupéré-Minier, C. Hamelin, P. Devine, and J. Bernier Involvement of CD45 in DNA fragmentation in apoptosis induced by mitochondrial perturbing agents Apoptosis 13 2008 197 212
    • (2008) Apoptosis , vol.13 , pp. 197-212
    • Desharnais, P.1    Dupéré-Minier, G.2    Hamelin, C.3    Devine, P.4    Bernier, J.5
  • 21
    • 0028323164 scopus 로고
    • A selective procedure for DNA extraction from apoptotic cells applicable for gel electrophoresis and flow cytometry
    • DOI 10.1006/abio.1994.1184
    • J.P. Gong, F. Traganos, and Z. Darzynkiewicz A selective procedure for DNA extraction from apoptotic cells applicable for gel electrophoresis and flow cytometry Anal. Biochem. 218 1994 314 319 (Pubitemid 24141629)
    • (1994) Analytical Biochemistry , vol.218 , Issue.2 , pp. 314-319
    • Gong, J.P.1    Traganos, F.2    Darzynkiewicz, Z.3
  • 22
    • 0035940412 scopus 로고    scopus 로고
    • Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington's disease brains, associate with membranes, and undergo calpaindependent proteolysis
    • DOI 10.1073/pnas.221451398
    • Y.J. Kim, Y. Yi, E. Sapp, Y. Wang, B. Cuiffo, K.B. Kegel, Z.-H. Qin, N. Aronin, and M. DiFiglia Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington's disease brains, associate with membranes, and undergo calpain-dependent proteolysis Proc. Natl. Acad. Sci. U.S.A. 98 2001 12784 12789 (Pubitemid 33020022)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.22 , pp. 12784-12789
    • Kim, Y.J.1    Yi, Y.2    Sapp, E.3    Wang, Y.4    Cuiffo, B.5    Kegel, K.B.6    Qin, Z.-H.7    Aronin, N.8    DiFiglia, M.9
  • 23
    • 0034584574 scopus 로고    scopus 로고
    • The DFF40/CAD endonuclease and its role in apoptosis
    • P. Widlak The DFF40/CAD endonuclease and its role in apoptosis Acta Biochim. Pol. 47 2000 1037 1044
    • (2000) Acta Biochim. Pol. , vol.47 , pp. 1037-1044
    • Widlak, P.1
  • 26
    • 33745632818 scopus 로고    scopus 로고
    • Glucosamine administration during resuscitation improves organ function after trauma hemorrhage
    • DOI 10.1097/01.shk.0000209563.07693.db, PII 0002438220060600000008
    • S. Yang, L.-y. Zou, P. Bounelis, I. Chaudry, J.C. Chatham, and R.B. Marchase Glucosamine administration during resuscitation improves organ function after trauma hemorrhage Shock 25 2006 600 607 (Pubitemid 44297021)
    • (2006) Shock , vol.25 , Issue.6 , pp. 600-607
    • Yang, S.1    Zou, L.-Y.2    Bounelis, P.3    Chaudry, I.4    Chatham, J.C.5    Marchase, R.B.6
  • 27
    • 77956412905 scopus 로고    scopus 로고
    • Cytoskeletal keratin glycosylation protects epithelial tissue from injury
    • N.-O. Ku, D.M. Toivola, P. Strnad, and M.B. Omary Cytoskeletal keratin glycosylation protects epithelial tissue from injury Nat. Cell Biol. 12 2010 876 885
    • (2010) Nat. Cell Biol. , vol.12 , pp. 876-885
    • Ku, N.-O.1    Toivola, D.M.2    Strnad, P.3    Omary, M.B.4
  • 28
    • 0038240900 scopus 로고    scopus 로고
    • Activation of the Ets transcription factor Elf-1 requires phosphorylation and glycosylation
    • G.C. Tsokos, M.P. Nambiar, and Y.-T. Juang Activation of the Ets transcription factor Elf-1 requires phosphorylation and glycosylation Ann. N. Y. Acad. Sci. 987 2003 240 245
    • (2003) Ann. N. Y. Acad. Sci. , vol.987 , pp. 240-245
    • Tsokos, G.C.1    Nambiar, M.P.2    Juang, Y.-T.3
  • 30
    • 0033554615 scopus 로고    scopus 로고
    • Multiple domains of DFF45 bind synergistically to DFF40: Roles of caspase cleavage and sequestration of activator domain of DFF40
    • DOI 10.1006/bbrc.1999.1498
    • J.S. McCarty, S.Y. Toh, and P. Li Multiple Domains of DFF45 Bind Synergistically to DFF40: Roles of Caspase Cleavage and Sequestration of Activator Domain of DFF40 Biochem. Biophys. Res. Commun. 264 1999 181 185 (Pubitemid 29500484)
    • (1999) Biochemical and Biophysical Research Communications , vol.264 , Issue.1 , pp. 181-185
    • McCarty, J.S.1    Toh, S.Y.2    Li, P.3
  • 31
    • 78049390185 scopus 로고    scopus 로고
    • O-GlcNAc transferase regulates mitotic chromatin dynamics
    • K. Sakabe, and G.W. Hart O-GlcNAc transferase regulates mitotic chromatin dynamics J. Biol. Chem. 285 2010 34460 34468
    • (2010) J. Biol. Chem. , vol.285 , pp. 34460-34468
    • Sakabe, K.1    Hart, G.W.2
  • 32
    • 11144246904 scopus 로고    scopus 로고
    • Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities
    • DOI 10.1074/jbc.M410406200
    • C. Toleman, A.J. Paterson, T.R. Whisenhunt, and J.E. Kudlow Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities J. Biol. Chem. 279 2004 53665 53673 (Pubitemid 40051874)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.51 , pp. 53665-53673
    • Toleman, C.1    Paterson, A.J.2    Whisenhunt, T.R.3    Kudlow, J.E.4
  • 33
    • 0030772457 scopus 로고    scopus 로고
    • O glycosylation of an Sp1-derived peptide blocks known Sp1 protein interactions
    • M.D. Roos, K. Su, J.R. Baker, and J.E. Kudlow O glycosylation of an Sp1-derived peptide blocks known Sp1 protein interactions Mol. Cell. Biol. 17 1997 6472 6480 (Pubitemid 27451193)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.11 , pp. 6472-6480
    • Roos, M.D.1    Su, K.2    Baker, J.R.3    Kudlow, J.E.4
  • 34
    • 33644874204 scopus 로고    scopus 로고
    • The hexosamine signaling pathway: Deciphering the "o-GlcNAc code"
    • D.C. Love, and J.A. Hanover The hexosamine signaling pathway: deciphering the "O-GlcNAc code" Sci. STKE 2005 2005 re13-
    • (2005) Sci. STKE , vol.2005 , pp. 13
    • Love, D.C.1    Hanover, J.A.2
  • 37
    • 35348836064 scopus 로고    scopus 로고
    • Requirement for O-linked N-acetylglucosaminyltransferase in lymphocytes activation
    • DOI 10.1038/sj.emboj.7601845, PII 7601845
    • A. Golks, T.-T.T. Tran, J.F. Goetschy, and D. Guerini Requirement for O-linked N-acetylglucosaminyltransferase in lymphocytes activation EMBO J. 26 2007 4368 4379 (Pubitemid 47587656)
    • (2007) EMBO Journal , vol.26 , Issue.20 , pp. 4368-4379
    • Golks, A.1    Tran, T.-T.T.2    Goetschy, J.F.3    Guerini, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.