메뉴 건너뛰기




Volumn 16, Issue 1, 2006, Pages 22-28

Modulation of HSP70 GlcNAc-directed lectin activity by glucose availability and utilization

Author keywords

Glucose; Heat shock proteins; Hexosamine biosynthetic pathway; Lectin; O GlcNAc

Indexed keywords

CYTOCHALASIN B; DEOXYGLUCOSE; GLUCOSE; HEAT SHOCK COGNATE PROTEIN 70; HEAT SHOCK PROTEIN 70; LECTIN; N ACETYLGLUCOSAMINE;

EID: 29444443797     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwj041     Document Type: Article
Times cited : (33)

References (23)
  • 1
    • 1842580187 scopus 로고    scopus 로고
    • Prolonged incubation in PUGNAc results in increased protein O-linked glycosylation and insulin resistance in rat skeletal muscle
    • Arias, E.B., Kim, J., and Cartee, G.D. (2004) Prolonged incubation in PUGNAc results in increased protein O-linked glycosylation and insulin resistance in rat skeletal muscle. Diabetes, 53, 921-930.
    • (2004) Diabetes , vol.53 , pp. 921-930
    • Arias, E.B.1    Kim, J.2    Cartee, G.D.3
  • 2
    • 0034718570 scopus 로고    scopus 로고
    • Alternative O-glycosylation/O-phosphorylation of the murine estrogen receptor beta
    • Cheng, X., Cole, R.N., Zaia, J., and Hart, G.W. (2000) Alternative O-glycosylation/O-phosphorylation of the murine estrogen receptor beta. Biochemistry, 39, 11609-11620.
    • (2000) Biochemistry , vol.39 , pp. 11609-11620
    • Cheng, X.1    Cole, R.N.2    Zaia, J.3    Hart, G.W.4
  • 3
    • 3042815335 scopus 로고    scopus 로고
    • Identification of O-linked N-acetylglucosamine proteins in rat skeletal muscle using two-dimensional gel electrophoresis and mass spectrometry
    • Cieniewski-Bernard, C., Bastide, B., Lefebvre, T., Lemoine, J., Mounier, Y., and Michalski, J.-C. (2004) Identification of O-linked N-acetylglucosamine proteins in rat skeletal muscle using two-dimensional gel electrophoresis and mass spectrometry. Mol. Cell. Proteomics, 3, 577-585.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 577-585
    • Cieniewski-Bernard, C.1    Bastide, B.2    Lefebvre, T.3    Lemoine, J.4    Mounier, Y.5    Michalski, J.-C.6
  • 4
    • 0032915738 scopus 로고    scopus 로고
    • Mechanism of hexosamine-induced insulin resistance in transgenic mice overexpressing glutamine: Fructose-6-phosphate amidotransferase: Decreased glucose transporter GLUT4 translocation and reversal by treatment with thiazolidinedione
    • Cooksey, R.C., Hebert, L.F., Jr., Zhu, J.H., Wofford, P., Garvey, W.T., and McClain, D.A. (1999) Mechanism of hexosamine-induced insulin resistance in transgenic mice overexpressing glutamine: fructose-6-phosphate amidotransferase: Decreased glucose transporter GLUT4 translocation and reversal by treatment with thiazolidinedione. Endocrinology, 140, 1151-1157.
    • (1999) Endocrinology , vol.140 , pp. 1151-1157
    • Cooksey, R.C.1    Hebert Jr., L.F.2    Zhu, J.H.3    Wofford, P.4    Garvey, W.T.5    McClain, D.A.6
  • 5
    • 2442687675 scopus 로고    scopus 로고
    • 70-kDa-heat shock protein presents an adjustable lectinic activity towards O-linked N-acetylglucosamine
    • Guinez, C., Lemoine, J., Michalski, J.C., and Lefebvre, T. (2004) 70-kDa-heat shock protein presents an adjustable lectinic activity towards O-linked N-acetylglucosamine. Biochem. Biophys. Res. Commun, 319, 21-26.
    • (2004) Biochem. Biophys. Res. Commun. , vol.319 , pp. 21-26
    • Guinez, C.1    Lemoine, J.2    Michalski, J.C.3    Lefebvre, T.4
  • 6
    • 13444266255 scopus 로고    scopus 로고
    • O-GlcNAc glycosylation: A signal for the nuclear transport of cytosolic proteins?
    • Guinez, C., Morelle, W., Michalski, J.-C., and Lefebvre, T. (2005) O-GlcNAc glycosylation: A signal for the nuclear transport of cytosolic proteins? Int. J. Biochem. Cell. Biol., 37, 765-774.
    • (2005) Int. J. Biochem. Cell. Biol. , vol.37 , pp. 765-774
    • Guinez, C.1    Morelle, W.2    Michalski, J.-C.3    Lefebvre, T.4
  • 7
    • 0030907389 scopus 로고    scopus 로고
    • Reduced O-glycosylation of Spl is associated with increased proteasome susceptibility
    • Han, I. and Kudlow, J.E. (1997) Reduced O-glycosylation of Spl is associated with increased proteasome susceptibility. Mol. Cell. Biol., 17, 2550-2558.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2550-2558
    • Han, I.1    Kudlow, J.E.2
  • 8
    • 0141844491 scopus 로고    scopus 로고
    • Plakoglobin is O-glycosylated close to the N-terminal destruction box
    • Hatsell, S., Medina, L., Merola, J., Haltiwanger. R., and Cowin, P. (2003) Plakoglobin is O-glycosylated close to the N-terminal destruction box. J. Biol. Chem., 278, 37745-37752.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37745-37752
    • Hatsell, S.1    Medina, L.2    Merola, J.3    Haltiwanger, R.4    Cowin, P.5
  • 9
    • 0345277743 scopus 로고    scopus 로고
    • Dynamic interplay between O-glycosylation and O-phosphorylation of nucleocytoplasmic proteins: A new paradigm for metabolic control of signal transduction and transcription
    • Kamemura, K. and Hart, G.W. (2003) Dynamic interplay between O-glycosylation and O-phosphorylation of nucleocytoplasmic proteins: A new paradigm for metabolic control of signal transduction and transcription. Prog. Nucleic Acid Res. Mol. Biol., 73, 107-136.
    • (2003) Prog. Nucleic Acid Res. Mol. Biol. , vol.73 , pp. 107-136
    • Kamemura, K.1    Hart, G.W.2
  • 10
    • 0035890905 scopus 로고    scopus 로고
    • Identification of N-acetyl-d-glucosamine-specific lectins from rat liver cytosolic and nuclear compartments as heat-shock proteins
    • Lefebvre, T., Cieniewski, C., Lemoine, J., Guerardel, Y., Leroy, Y., Zanetta, J.P., and Michalski, J.C. (2001) Identification of N-acetyl-d-glucosamine-specific lectins from rat liver cytosolic and nuclear compartments as heat-shock proteins. Biochem. J., 360, 179-188.
    • (2001) Biochem. J. , vol.360 , pp. 179-188
    • Lefebvre, T.1    Cieniewski, C.2    Lemoine, J.3    Guerardel, Y.4    Leroy, Y.5    Zanetta, J.P.6    Michalski, J.C.7
  • 11
    • 0034646669 scopus 로고    scopus 로고
    • Functional expression of O-linked GlcNAc transferase. Domain structure and substrate specificity
    • Lubas, W.A. and Hanover, J.A. (2000) Functional expression of O-linked GlcNAc transferase. Domain structure and substrate specificity. J. Biol. Chem., 275, 10983-10988.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10983-10988
    • Lubas, W.A.1    Hanover, J.A.2
  • 12
    • 0025855139 scopus 로고
    • Discovery of a metabolic pathway mediating glucose-induced desensitization of the glucose transport system. Role of hexosamine biosynthesis in the induction of insulin resistance
    • Marshall, S., Bacote, V., and Traxinger, R.R. (1991) Discovery of a metabolic pathway mediating glucose-induced desensitization of the glucose transport system. Role of hexosamine biosynthesis in the induction of insulin resistance. J. Biol. Chem., 266, 4706-4712.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4706-4712
    • Marshall, S.1    Bacote, V.2    Traxinger, R.R.3
  • 14
    • 0344298921 scopus 로고    scopus 로고
    • Activation of the hexosamine pathway by glucosamine in vivo induces insulin resistance of early postreceptor insulin signaling events in skeletal muscle
    • Patti, M.E., Virkamäki, A., Landaker, E.J., Kahn, C.R., and Yki-Järvinen, H. (1999) Activation of the hexosamine pathway by glucosamine in vivo induces insulin resistance of early postreceptor insulin signaling events in skeletal muscle. Diabetes, 48, 1562-1571.
    • (1999) Diabetes , vol.48 , pp. 1562-1571
    • Patti, M.E.1    Virkamäki, A.2    Landaker, E.J.3    Kahn, C.R.4    Yki-Järvinen, H.5
  • 15
    • 0027275367 scopus 로고
    • Pre-exposure to glucosamine induces insulin resistance of glucose transport and glycogen synthesis in isolated rat skeletal muscles. Study of mechanisms in muscle and in rat-1 fibroblasts overexpressing the human insulin receptor
    • Robinson, K.A., Sens, D.A., and Buse, M.G. (1993) Pre-exposure to glucosamine induces insulin resistance of glucose transport and glycogen synthesis in isolated rat skeletal muscles. Study of mechanisms in muscle and in rat-1 fibroblasts overexpressing the human insulin receptor. Diabetes, 42, 1333-1346.
    • (1993) Diabetes , vol.42 , pp. 1333-1346
    • Robinson, K.A.1    Sens, D.A.2    Buse, M.G.3
  • 16
    • 0029115944 scopus 로고
    • In vivo glucosamine infusion induces insulin resistance in normoglycemic but not in hyperglycemic conscious rats
    • Rossetti, L., Hawkins, M., Chen, W., Gindi, J., and Barzilai, N. (1995) In vivo glucosamine infusion induces insulin resistance in normoglycemic but not in hyperglycemic conscious rats. J. Clin. Invest., 96, 132-140.
    • (1995) J. Clin. Invest. , vol.96 , pp. 132-140
    • Rossetti, L.1    Hawkins, M.2    Chen, W.3    Gindi, J.4    Barzilai, N.5
  • 17
    • 0345357692 scopus 로고    scopus 로고
    • 26S proteasome subunits are O-linked N-aretylglucosamine-modified in Drosophila melanogaster
    • Sumegi, M., Hunyadi-Gulyas, E., Medzihradszky, K.F., and Udvardy, A. (2003) 26S proteasome subunits are O-linked N-aretylglucosamine-modified in Drosophila melanogaster. Biochem. Biophys. Res. Commun., 312, 1284-1289.
    • (2003) Biochem. Biophys. Res. Commun. , vol.312 , pp. 1284-1289
    • Sumegi, M.1    Hunyadi-Gulyas, E.2    Medzihradszky, K.F.3    Udvardy, A.4
  • 18
    • 0021280147 scopus 로고
    • Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc
    • Torres, C.R. and Hart, G.W. (1984) Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc. J. Biol. Chem., 259, 3308-3317,
    • (1984) J. Biol. Chem. , vol.259 , pp. 3308-3317
    • Torres, C.R.1    Hart, G.W.2
  • 19
    • 0037300799 scopus 로고    scopus 로고
    • A role for N-acetylglucosamine as a nutrient sensor and mediator of insulin resistance
    • Wells, L., Vosseler, K., and Hart, G.W. (2003) A role for N-acetylglucosamine as a nutrient sensor and mediator of insulin resistance. Cell. Mol. Life Sci., 60, 222-228.
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 222-228
    • Wells, L.1    Vosseler, K.2    Hart, G.W.3
  • 20
    • 0037067659 scopus 로고    scopus 로고
    • Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: Coupling protein O-GlcNAcylation to transcriptional repression
    • Yang, X., Zhang, F., and Kudlow, J.E. (2002) Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: Coupling protein O-GlcNAcylation to transcriptional repression. Cell, 110, 69-80.
    • (2002) Cell , vol.110 , pp. 69-80
    • Yang, X.1    Zhang, F.2    Kudlow, J.E.3
  • 21
    • 2342539803 scopus 로고    scopus 로고
    • O-GlcNAc modification: A nutritional sensor that modulates proteasome function
    • Zachara, N.E. and Hart, G.W. (2004) O-GlcNAc modification: A nutritional sensor that modulates proteasome function. Trends Cell. Biol., 14, 218-221.
    • (2004) Trends Cell Biol. , vol.14 , pp. 218-221
    • Zachara, N.E.1    Hart, G.W.2
  • 22
    • 3042534011 scopus 로고    scopus 로고
    • Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress. A survival response of mammalian cells
    • Zachara, N.E., O'Donnell, N., Cheung, W.D., Mercer, J.J., Marth, J.D., and Hart, G.W. (2004) Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress. A survival response of mammalian cells. J. Biol. Chem., 279, 30133-30142.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30133-30142
    • Zachara, N.E.1    O'Donnell, N.2    Cheung, W.D.3    Mercer, J.J.4    Marth, J.D.5    Hart, G.W.6
  • 23
    • 0346965700 scopus 로고    scopus 로고
    • O-GlcNAc modification is an endogenous inhibitor of the proteasome
    • Zhang, F., Su, K., Yang, X., Bowe, D.B., Paterson, A.J., and Kudlow, J.E. (2003) O-GlcNAc modification is an endogenous inhibitor of the proteasome. Cell, 115, 715-725.
    • (2003) Cell , vol.115 , pp. 715-725
    • Zhang, F.1    Su, K.2    Yang, X.3    Bowe, D.B.4    Paterson, A.J.5    Kudlow, J.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.