메뉴 건너뛰기




Volumn 13, Issue 12, 2014, Pages 3294-3307

Global mass spectrometry and transcriptomics array based drug profiling provides novel insight into glucosamine induced endoplasmic reticulum stress

Author keywords

[No Author keywords available]

Indexed keywords

CALNEXIN; GLUCOSAMINE; GLUCOSE REGULATED PROTEIN 78; GLUCOSIDASE; GLUCOSIDASE 2 SUBUNIT BETA; N ACETYLGLUCOSAMINE; O LINKED BETA N ACETYLGLUCOSAMINE; UNCLASSIFIED DRUG; HEAT SHOCK PROTEIN; MOLECULAR CHAPERONE GRP78; TRANSCRIPTOME;

EID: 84924284221     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M113.034363     Document Type: Article
Times cited : (39)

References (56)
  • 2
    • 34247583996 scopus 로고    scopus 로고
    • Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins
    • Hart, G. W., Housley, M. P., and Slawson, C. (2007) Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins. Nature 446, 1017-1022
    • (2007) Nature , vol.446 , pp. 1017-1022
    • Hart, G.W.1    Housley, M.P.2    Slawson, C.3
  • 4
    • 0037117511 scopus 로고    scopus 로고
    • Elevated nucleocytoplasmic glycosylation by O-GlcNAc results in insulin resistance associated with defects in Akt activation in 3T3-L1 adipocytes
    • Vosseller, K., Wells, L., Lane, M. D., and Hart, G. W. (2002) Elevated nucleocytoplasmic glycosylation by O-GlcNAc results in insulin resistance associated with defects in Akt activation in 3T3-L1 adipocytes. Proc. Natl. Acad. Sci. U. S. A. 99, 5313-5318
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 5313-5318
    • Vosseller, K.1    Wells, L.2    Lane, M.D.3    Hart, G.W.4
  • 5
    • 23844452765 scopus 로고    scopus 로고
    • O-GlcNAc modification of nucleocytoplasmic proteins and diabetes
    • Akimoto, Y., Hart, G. W., Hirano, H., and Kawakami, H. (2005) O-GlcNAc modification of nucleocytoplasmic proteins and diabetes. Med. Mol. Morphol. 38, 84-91
    • (2005) Med. Mol. Morphol. , vol.38 , pp. 84-91
    • Akimoto, Y.1    Hart, G.W.2    Hirano, H.3    Kawakami, H.4
  • 6
    • 0028199990 scopus 로고
    • The neglect of glucosamine as a treatment for osteoarthritis - A personal perspective
    • McCarty, M. F. (1994) The neglect of glucosamine as a treatment for osteoarthritis-a personal perspective. Med. Hypotheses 42, 323-327
    • (1994) Med. Hypotheses , vol.42 , pp. 323-327
    • McCarty, M.F.1
  • 8
    • 65849118869 scopus 로고    scopus 로고
    • Dietary glucosamine under question
    • Silbert, J. E. (2009) Dietary glucosamine under question. Glycobiology 19, 564-567
    • (2009) Glycobiology , vol.19 , pp. 564-567
    • Silbert, J.E.1
  • 9
    • 79952160646 scopus 로고    scopus 로고
    • Glucosamine and osteoarthritis: Time to quit?
    • Muniyappa, R. (2011) Glucosamine and osteoarthritis: time to quit? Diabetes Metab. Res. Rev. 27, 233-234
    • (2011) Diabetes Metab. Res. Rev. , vol.27 , pp. 233-234
    • Muniyappa, R.1
  • 10
    • 34250841706 scopus 로고    scopus 로고
    • Glucosamine cardioprotection in perfused rat hearts associated with increased O-linked N-acetylglucosamine protein modification and altered p38 activation
    • Fulop, N., Zhang, Z., Marchase, R. B., and Chatham, J. C. (2007) 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, H2227-H2236
    • (2007) Am. J. Physiol. Heart Circ. Physiol. , vol.292 , pp. H2227-H2236
    • Fulop, N.1    Zhang, Z.2    Marchase, R.B.3    Chatham, J.C.4
  • 11
    • 70350090622 scopus 로고    scopus 로고
    • Glucosamine suppresses proliferation of human prostate carcinoma DU145 cells through inhibition of STAT3 signaling
    • Chesnokov, V., Sun, C., and Itakura, K. (2009) Glucosamine suppresses proliferation of human prostate carcinoma DU145 cells through inhibition of STAT3 signaling. Cancer Cell Int. 9, 25
    • (2009) Cancer Cell Int. , vol.9 , pp. 25
    • Chesnokov, V.1    Sun, C.2    Itakura, K.3
  • 12
    • 0010982856 scopus 로고
    • Inhibition of tumor growth by D-glucosamine
    • Quastel JH, C. A. (1953) Inhibition of tumor growth by D-glucosamine. Nature 171, 252-254
    • (1953) Nature , vol.171 , pp. 252-254
    • Quastel, J.H.C.A.1
  • 13
    • 80052068559 scopus 로고    scopus 로고
    • O-GlcNAc signaling: Implications for cancer cell biology
    • Slawson, C., and Hart, G. W. (2011) O-GlcNAc signaling: implications for cancer cell biology. Nat. Rev. Cancer 11, 678-684
    • (2011) Nat. Rev. Cancer , vol.11 , pp. 678-684
    • Slawson, C.1    Hart, G.W.2
  • 14
    • 84858324600 scopus 로고    scopus 로고
    • The role of glucosamine-induced ER stress in diabetic atherogenesis
    • Epub 2012, Feb 23
    • Beriault, D. R., and Werstuck, G. H. (2012) The role of glucosamine-induced ER stress in diabetic atherogenesis. Exp. Diabetes Res. Epub 2012, Feb 23
    • (2012) Exp. Diabetes Res.
    • Beriault, D.R.1    Werstuck, G.H.2
  • 15
    • 33644830616 scopus 로고    scopus 로고
    • Glucosamine inhibits angiotensin II-induced cytoplasmic Ca2- elevation in neonatal cardiomyocytes via protein-associated O-linked N-acetylglucosamine
    • Nagy, T., Champattanachai, V., Marchase, R. B., and Chatham, J. C. (2006) Glucosamine inhibits angiotensin II-induced cytoplasmic Ca2- elevation in neonatal cardiomyocytes via protein-associated O-linked N-acetylglucosamine. Am. J. Physiol. Cell Physiol. 290, C57-C65
    • (2006) Am. J. Physiol. Cell Physiol. , vol.290 , pp. C57-C65
    • Nagy, T.1    Champattanachai, V.2    Marchase, R.B.3    Chatham, J.C.4
  • 16
    • 84863610013 scopus 로고    scopus 로고
    • Evidence of the involvement of O-GlcNAc-modified human RNA polymerase II CTD in transcription in vitro and in vivo
    • Ranuncolo, S. M., Ghosh, S., Hanover, J. A., Hart, G. W., and Lewis, B. A. (2012) Evidence of the involvement of O-GlcNAc-modified human RNA polymerase II CTD in transcription in vitro and in vivo. J. Biol. Chem. 287, 23549-23561
    • (2012) J. Biol. Chem. , vol.287 , pp. 23549-23561
    • Ranuncolo, S.M.1    Ghosh, S.2    Hanover, J.A.3    Hart, G.W.4    Lewis, B.A.5
  • 17
    • 52949123249 scopus 로고    scopus 로고
    • Cross-talk between GlcNAcylation and phosphorylation: Site-specific phosphorylation dynamics in response to globally elevated O-GlcNAc
    • Wang, Z., Gucek, M., and Hart, G. W. (2008) Cross-talk between GlcNAcylation and phosphorylation: site-specific phosphorylation dynamics in response to globally elevated O-GlcNAc. Proc. Natl. Acad. Sci. U. S. A. 105, 13793-13798
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 13793-13798
    • Wang, Z.1    Gucek, M.2    Hart, G.W.3
  • 18
    • 80052999905 scopus 로고    scopus 로고
    • Cellular content of UDP-N-acetylhexosamines controls hyaluronan synthase 2 expression and correlates with O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1
    • Jokela, T. A., Makkonen, K. M., Oikari, S., Karna, R., Koli, E., Hart, G. W., Tammi, R. H., Carlberg, C., and Tammi, M. I. (2011) Cellular content of UDP-N-acetylhexosamines controls hyaluronan synthase 2 expression and correlates with O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1. J. Biol. Chem. 286, 33632-33640
    • (2011) J. Biol. Chem. , vol.286 , pp. 33632-33640
    • Jokela, T.A.1    Makkonen, K.M.2    Oikari, S.3    Karna, R.4    Koli, E.5    Hart, G.W.6    Tammi, R.H.7    Carlberg, C.8    Tammi, M.I.9
  • 19
    • 77955578557 scopus 로고    scopus 로고
    • Glucosamine induces autophagic cell death through the stimulation of ER stress in human glioma cancer cells
    • Hwang, M. S., and Baek, W. K. (2010) Glucosamine induces autophagic cell death through the stimulation of ER stress in human glioma cancer cells. Biochem. Biophys. Res. Commun. 399, 111-116
    • (2010) Biochem. Biophys. Res. Commun. , vol.399 , pp. 111-116
    • Hwang, M.S.1    Baek, W.K.2
  • 21
    • 10344222124 scopus 로고    scopus 로고
    • The role of the unfolded protein response in tumour development: Friend or foe?
    • Ma, Y., and Hendershot, L. M. (2004) The role of the unfolded protein response in tumour development: friend or foe? Nat. Rev. Cancer 4, 966-977
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 966-977
    • Ma, Y.1    Hendershot, L.M.2
  • 23
    • 77956510773 scopus 로고    scopus 로고
    • Inhibition of phospholamban phosphorylation by OGlcNAcylation: Implications for diabetic cardiomyopathy
    • Yokoe, S., Asahi, M., Takeda, T., Otsu, K., Taniguchi, N., Miyoshi, E., and Suzuki, K. (2010) Inhibition of phospholamban phosphorylation by OGlcNAcylation: implications for diabetic cardiomyopathy. Glycobiology 20, 1217-1226
    • (2010) Glycobiology , vol.20 , pp. 1217-1226
    • Yokoe, S.1    Asahi, M.2    Takeda, T.3    Otsu, K.4    Taniguchi, N.5    Miyoshi, E.6    Suzuki, K.7
  • 25
    • 33645287677 scopus 로고    scopus 로고
    • affylmGUI: A graphical user interface for linear modeling of single channel microarray data
    • Wettenhall, J. M., Simpson, K. M., Satterley, K., and Smyth, G. K. (2006) affylmGUI: a graphical user interface for linear modeling of single channel microarray data. Bioinformatics 22, 897-899
    • (2006) Bioinformatics , vol.22 , pp. 897-899
    • Wettenhall, J.M.1    Simpson, K.M.2    Satterley, K.3    Smyth, G.K.4
  • 26
    • 0037316303 scopus 로고    scopus 로고
    • A comparison of normalization methods for high density oligonucleotide array data based on variance and bias
    • Bolstad, B. M., Irizarry, R. A., Astrand, M., and Speed, T. P. (2003) A comparison of normalization methods for high density oligonucleotide array data based on variance and bias. Bioinformatics 19, 185-193
    • (2003) Bioinformatics , vol.19 , pp. 185-193
    • Bolstad, B.M.1    Irizarry, R.A.2    Astrand, M.3    Speed, T.P.4
  • 27
    • 0001677717 scopus 로고
    • Controlling the false discovery rate: A practical and powerful approach to multiple testing
    • Benjamini, Y. H., Yosef (1995) Controlling the false discovery rate: a practical and powerful approach to multiple testing. J. Roy. Stat. Soc. B 57, 289-300
    • (1995) J. Roy. Stat. Soc. B , vol.57 , pp. 289-300
    • Benjamini, Y.H.1    Yosef2
  • 28
    • 64749108158 scopus 로고    scopus 로고
    • Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics
    • Boersema, P. J., Raijmakers, R., Lemeer, S., Mohammed, S., and Heck, A. J. (2009) Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics. Nat. Protoc. 4, 484-494
    • (2009) Nat. Protoc. , vol.4 , pp. 484-494
    • Boersema, P.J.1    Raijmakers, R.2    Lemeer, S.3    Mohammed, S.4    Heck, A.J.5
  • 29
    • 71549117585 scopus 로고    scopus 로고
    • Combination of FASP and StageTip-based fractionation allows in-depth analysis of the hippocampal membrane proteome
    • Wisniewski, J. R., Zougman, A., and Mann, M. (2009) Combination of FASP and StageTip-based fractionation allows in-depth analysis of the hippocampal membrane proteome. J. Proteome Res. 8, 5674-5678
    • (2009) J. Proteome Res. , vol.8 , pp. 5674-5678
    • Wisniewski, J.R.1    Zougman, A.2    Mann, M.3
  • 30
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micropurification, enrichment, prefractionation and storage of peptides for proteomics using StageTips
    • Rappsilber, J., Mann, M., and Ishihama, Y. (2007) Protocol for micropurification, enrichment, prefractionation and storage of peptides for proteomics using StageTips. Nat. Protoc. 2, 1896-1906
    • (2007) Nat. Protoc. , vol.2 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3
  • 31
    • 0038617421 scopus 로고    scopus 로고
    • Volatile polydimethylcyclosiloxanes in the ambient laboratory air identified as source of extreme background signals in nanoelectrospray mass spectrometry
    • Schlosser, A., and Volkmer-Engert, R. (2003) Volatile polydimethylcyclosiloxanes in the ambient laboratory air identified as source of extreme background signals in nanoelectrospray mass spectrometry. J. Mass Spectrom. 38, 523-525
    • (2003) J. Mass Spectrom. , vol.38 , pp. 523-525
    • Schlosser, A.1    Volkmer-Engert, R.2
  • 33
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox, J., and Mann, M. (2008) MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26, 1367-1372
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 34
    • 84883202191 scopus 로고    scopus 로고
    • LC-MS spectra processing
    • Matthiesen, R. (2013) LC-MS spectra processing. Methods Mol. Biol. 1007, 47-63
    • (2013) Methods Mol. Biol. , vol.1007 , pp. 47-63
    • Matthiesen, R.1
  • 35
    • 84883170685 scopus 로고    scopus 로고
    • Algorithms for database-dependent search of MS/MS data
    • Matthiesen, R. (2013) Algorithms for database-dependent search of MS/MS data. Methods Mol. Biol. 1007, 119-138
    • (2013) Methods Mol. Biol. , vol.1007 , pp. 119-138
    • Matthiesen, R.1
  • 36
    • 77955643959 scopus 로고    scopus 로고
    • The minotaur proteome: Avoiding cross-species identifications deriving from bovine serum in cell culture models
    • Bunkenborg, J., Garcia, G. E., Paz, M. I., Andersen, J. S., and Molina, H. (2010) The minotaur proteome: avoiding cross-species identifications deriving from bovine serum in cell culture models. Proteomics 10, 3040-3044
    • (2010) Proteomics , vol.10 , pp. 3040-3044
    • Bunkenborg, J.1    Garcia, G.E.2    Paz, M.I.3    Andersen, J.S.4    Molina, H.5
  • 38
    • 84883188758 scopus 로고    scopus 로고
    • Methods and algorithms for quantitative proteomics by mass spectrometry
    • Matthiesen, R., and Carvalho, A. S. (2013) Methods and algorithms for quantitative proteomics by mass spectrometry. Methods Mol. Biol. 1007, 183-217
    • (2013) Methods Mol. Biol. , vol.1007 , pp. 183-217
    • Matthiesen, R.1    Carvalho, A.S.2
  • 42
    • 0034799402 scopus 로고    scopus 로고
    • The structure of calnexin, an ER chaperone involved in quality control of protein folding
    • Schrag, J. D., Bergeron, J. J., Li, Y., Borisova, S., Hahn, M., Thomas, D. Y., and Cygler, M. (2001) The Structure of calnexin, an ER chaperone involved in quality control of protein folding. Mol. Cell 8, 633-644
    • (2001) Mol. Cell , vol.8 , pp. 633-644
    • Schrag, J.D.1    Bergeron, J.J.2    Li, Y.3    Borisova, S.4    Hahn, M.5    Thomas, D.Y.6    Cygler, M.7
  • 43
    • 77957758520 scopus 로고    scopus 로고
    • Calcineurin interacts with PERK and dephosphorylates calnexin to relieve ER stress in mammals and frogs
    • Bollo, M., Paredes, R. M., Holstein, D., Zheleznova, N., Camacho, P., and Lechleiter, J. D. (2013) Calcineurin interacts with PERK and dephosphorylates calnexin to relieve ER stress in mammals and frogs. PLoS One 5, e11925
    • (2013) PLoS One , vol.5
    • Bollo, M.1    Paredes, R.M.2    Holstein, D.3    Zheleznova, N.4    Camacho, P.5    Lechleiter, J.D.6
  • 44
    • 77952583799 scopus 로고    scopus 로고
    • Calnexin phosphorylation: Linking cytoplasmic signalling to endoplasmic reticulum lumenal functions
    • Chevet, E., Smirle, J., Cameron, P. H., Thomas, D. Y., and Bergeron, J. J. (2010) Calnexin phosphorylation: linking cytoplasmic signalling to endoplasmic reticulum lumenal functions. Semin. Cell Dev. Biol. 21, 486-490
    • (2010) Semin. Cell Dev. Biol. , vol.21 , pp. 486-490
    • Chevet, E.1    Smirle, J.2    Cameron, P.H.3    Thomas, D.Y.4    Bergeron, J.J.5
  • 45
    • 0032479438 scopus 로고    scopus 로고
    • Conserved in vivo phosphorylation of calnexin at casein kinase II sites as well as a protein kinase C/proline-directed kinase site
    • Wong, H. N., Ward, M. A., Bell, A. W., Chevet, E., Bains, S., Blackstock, W. P., Solari, R., Thomas, D. Y., and Bergeron, J. J. (1998) Conserved in vivo phosphorylation of calnexin at casein kinase II sites as well as a protein kinase C/proline-directed kinase site. J. Biol. Chem. 273, 17227-17235
    • (1998) J. Biol. Chem. , vol.273 , pp. 17227-17235
    • Wong, H.N.1    Ward, M.A.2    Bell, A.W.3    Chevet, E.4    Bains, S.5    Blackstock, W.P.6    Solari, R.7    Thomas, D.Y.8    Bergeron, J.J.9
  • 46
    • 14644405001 scopus 로고    scopus 로고
    • Glucosamine-induced endoplasmic reticulum stress promotes ApoB100 degradation: Evidence for Grp78-mediated targeting to proteasomal degradation
    • Qiu, W., Kohen-Avramoglu, R., Mhapsekar, S., Tsai, J., Austin, R. C., and Adeli, K. (2005) Glucosamine-induced endoplasmic reticulum stress promotes ApoB100 degradation: evidence for Grp78-mediated targeting to proteasomal degradation. Arterioscler. Thromb. Vasc. Biol. 25, 571-577
    • (2005) Arterioscler. Thromb. Vasc. Biol. , vol.25 , pp. 571-577
    • Qiu, W.1    Kohen-Avramoglu, R.2    Mhapsekar, S.3    Tsai, J.4    Austin, R.C.5    Adeli, K.6
  • 47
    • 34247194251 scopus 로고    scopus 로고
    • Glucosamine-induced increase in Akt phosphorylation corresponds to increased endoplasmic reticulum stress in astroglial cells
    • Matthews, J. A., Belof, J. L., Acevedo-Duncan, M., and Potter, R. L. (2007) Glucosamine-induced increase in Akt phosphorylation corresponds to increased endoplasmic reticulum stress in astroglial cells. Mol. Cell. Biochem. 298, 109-123
    • (2007) Mol. Cell. Biochem. , vol.298 , pp. 109-123
    • Matthews, J.A.1    Belof, J.L.2    Acevedo-Duncan, M.3    Potter, R.L.4
  • 50
    • 1642488945 scopus 로고    scopus 로고
    • The AHNAKs are a class of giant propeller-like proteins that associate with calcium channel proteins of cardiomyocytes and other cells
    • Komuro, A., Masuda, Y., Kobayashi, K., Babbitt, R., Gunel, M., Flavell, R. A., and Marchesi, V. T. (2004) The AHNAKs are a class of giant propeller-like proteins that associate with calcium channel proteins of cardiomyocytes and other cells. Proc. Natl. Acad. Sci. U. S. A. 101, 4053-4058
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 4053-4058
    • Komuro, A.1    Masuda, Y.2    Kobayashi, K.3    Babbitt, R.4    Gunel, M.5    Flavell, R.A.6    Marchesi, V.T.7
  • 51
    • 0026647930 scopus 로고
    • A human gene (AHNAK) encoding an unusually large protein with a 1.2-microns polyionic rod structure
    • Shtivelman, E., Cohen, F. E., and Bishop, J. M. (1992) A human gene (AHNAK) encoding an unusually large protein with a 1.2-microns polyionic rod structure. Proc. Natl. Acad. Sci. U. S. A. 89, 5472-5476
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 5472-5476
    • Shtivelman, E.1    Cohen, F.E.2    Bishop, J.M.3
  • 52
    • 0030888276 scopus 로고    scopus 로고
    • Inhibition of cytosolic phospholipase A2 by annexin V in differentiated permeabilized HL-60 cells. Evidence of crucial importance of domain I type II Ca2+-binding site in the mechanism of inhibition
    • Mira, J. P., Dubois, T., Oudinet, J. P., Lukowski, S., Russo-Marie, F., and Geny, B. (1997) Inhibition of cytosolic phospholipase A2 by annexin V in differentiated permeabilized HL-60 cells. Evidence of crucial importance of domain I type II Ca2+-binding site in the mechanism of inhibition. J. Biol. Chem. 272, 10474-10482
    • (1997) J. Biol. Chem. , vol.272 , pp. 10474-10482
    • Mira, J.P.1    Dubois, T.2    Oudinet, J.P.3    Lukowski, S.4    Russo-Marie, F.5    Geny, B.6
  • 55
    • 4644262462 scopus 로고    scopus 로고
    • O-GlcNAc transferase is in a functional complex with protein phosphatase 1 catalytic subunits
    • Wells, L., Kreppel, L. K., Comer, F. I., Wadzinski, B. E., and Hart, G. W. (2004) O-GlcNAc transferase is in a functional complex with protein phosphatase 1 catalytic subunits. J. Biol. Chem. 279, 38466-38470
    • (2004) J. Biol. Chem. , vol.279 , pp. 38466-38470
    • Wells, L.1    Kreppel, L.K.2    Comer, F.I.3    Wadzinski, B.E.4    Hart, G.W.5
  • 56
    • 0141884304 scopus 로고    scopus 로고
    • Dynamic interplay between O-GlcNAc and O-phosphate: The sweet side of protein regulation
    • Slawson, C., and Hart, G. W. (2003) Dynamic interplay between O-GlcNAc and O-phosphate: the sweet side of protein regulation. Curr. Opin. Struct. Biol. 13, 631-636
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 631-636
    • Slawson, C.1    Hart, G.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.