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Volumn 12, Issue 2, 2013, Pages 283-301

Alteration of the serum N-glycome of mice locally exposed to high doses of ionizing radiation

Author keywords

[No Author keywords available]

Indexed keywords

GLYCAN; INTERLEUKIN 1BETA; INTERLEUKIN 6; N GLYCOME; PROTEIN; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 84874046869     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M111.014639     Document Type: Article
Times cited : (24)

References (56)
  • 1
    • 0025228531 scopus 로고
    • The skin: Its structure and response to ionizing radiation
    • Hopewell, J. W. (1990) The skin: its structure and response to ionizing radiation. Int. J. Radiat. Biol. 57, 751-773
    • (1990) Int. J. Radiat. Biol. , vol.57 , pp. 751-773
    • Hopewell, J.W.1
  • 3
    • 77954010910 scopus 로고    scopus 로고
    • The cutaneous radiation syndrome: Diagnosis and treatment
    • Peter, R. U., Steinert, M., and Gottlober, P. (2001) The cutaneous radiation syndrome: diagnosis and treatment. Radioprotection 49, 451-457
    • (2001) Radioprotection , vol.49 , pp. 451-457
    • Peter, R.U.1    Steinert, M.2    Gottlober, P.3
  • 4
    • 77952007369 scopus 로고    scopus 로고
    • Advances in the management of localized radiation injuries
    • Muller, K., and Meineke, V. (2010) Advances in the management of localized radiation injuries. Health Phys. 98, 843-850
    • (2010) Health Phys. , vol.98 , pp. 843-850
    • Muller, K.1    Meineke, V.2
  • 5
    • 75149158317 scopus 로고    scopus 로고
    • The role of damage to the cutaneous system in radiation-induced multi-organ failure
    • Meineke, V. (2005) The role of damage to the cutaneous system in radiation-induced multi-organ failure. Br. J. Radiol. Suppl. 27, 85-99
    • (2005) Br. J. Radiol. Suppl. , vol.27 , pp. 85-99
    • Meineke, V.1
  • 9
    • 77951988662 scopus 로고    scopus 로고
    • Mesenchymal stem cell therapy for cutaneous radiation syndrome
    • Akita, S., Akino, K., Hirano, A., Ohtsuru, A., and Yamashita, S. (2010) Mesenchymal stem cell therapy for cutaneous radiation syndrome. Health Phys. 98, 858-862
    • (2010) Health Phys. , vol.98 , pp. 858-862
    • Akita, S.1    Akino, K.2    Hirano, A.3    Ohtsuru, A.4    Yamashita, S.5
  • 11
    • 70350336281 scopus 로고    scopus 로고
    • Protein biomarkers for radiation exposure: Towards a proteomic approach as a new investigation tool
    • Guipaud, O., and Benderitter, M. (2009) Protein biomarkers for radiation exposure: towards a proteomic approach as a new investigation tool. Ann. Ist. Super. Sanita 45, 278-286
    • (2009) Ann. Ist. Super. Sanita , vol.45 , pp. 278-286
    • Guipaud, O.1    Benderitter, M.2
  • 13
    • 0031773119 scopus 로고    scopus 로고
    • How do tissues respond to damage at the cellular level? The role of cytokines in irradiated tissues
    • Barcellos-Hoff, M. H. (1998) How do tissues respond to damage at the cellular level? The role of cytokines in irradiated tissues. Radiat. Res. 150, S109-S120
    • (1998) Radiat. Res. , vol.150
    • Barcellos-Hoff, M.H.1
  • 14
    • 33947219001 scopus 로고    scopus 로고
    • Radiation-induced alterations in cytokine production by skin cells
    • Muller, K., and Meineke, V. (2007) Radiation-induced alterations in cytokine production by skin cells. Exp. Hematol. 35, 96-104
    • (2007) Exp. Hematol. , vol.35 , pp. 96-104
    • Muller, K.1    Meineke, V.2
  • 15
    • 0033545342 scopus 로고    scopus 로고
    • Acute-phase proteins and other systemic responses to inflammation
    • Gabay, C., and Kushner, I. (1999) Acute-phase proteins and other systemic responses to inflammation. N. Engl. J. Med. 340, 448-454
    • (1999) N. Engl. J. Med. , vol.340 , pp. 448-454
    • Gabay, C.1    Kushner, I.2
  • 16
    • 36048953086 scopus 로고    scopus 로고
    • Time-course analysis of mouse serum proteome changes following exposure of the skin to ionizing radiation
    • Guipaud, O., Holler, V., Buard, V., Tarlet, G., Royer, N., Vinh, J., and Benderitter, M. (2007) Time-course analysis of mouse serum proteome changes following exposure of the skin to ionizing radiation. Proteomics 7, 3992-4002
    • (2007) Proteomics , vol.7 , pp. 3992-4002
    • Guipaud, O.1    Holler, V.2    Buard, V.3    Tarlet, G.4    Royer, N.5    Vinh, J.6    Benderitter, M.7
  • 17
    • 0030937062 scopus 로고    scopus 로고
    • Glycosylation: Heterogeneity and the 3D structure of proteins
    • Rudd, P. M., and Dwek, R. A. (1997) Glycosylation: heterogeneity and the 3D structure of proteins. Crit. Rev. Biochem. Mol. Biol. 32, 1-100
    • (1997) Crit. Rev. Biochem. Mol. Biol. , vol.32 , pp. 1-100
    • Rudd, P.M.1    Dwek, R.A.2
  • 18
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • Apweiler, R., Hermjakob, H., and Sharon, N. (1999) On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim. Biophys. Acta 1473, 4-8
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 19
    • 20844437106 scopus 로고    scopus 로고
    • Glycans in cancer and inflammation - Potential for therapeutics and diagnostics
    • Dube, D. H., and Bertozzi, C. R. (2005) Glycans in cancer and inflammation - potential for therapeutics and diagnostics. Nat. Rev. Drug Discov. 4, 477-488
    • (2005) Nat. Rev. Drug Discov. , vol.4 , pp. 477-488
    • Dube, D.H.1    Bertozzi, C.R.2
  • 20
    • 77951930076 scopus 로고    scopus 로고
    • Glycoproteomics and clinical applications
    • Tian, Y., and Zhang, H. (2010) Glycoproteomics and clinical applications. Proteomics Clin. Appl. 4, 124-132
    • (2010) Proteomics Clin. Appl. , vol.4 , pp. 124-132
    • Tian, Y.1    Zhang, H.2
  • 22
    • 50449083310 scopus 로고    scopus 로고
    • Evaluation of the serum N-linked glycome for the diagnosis of cancer and chronic inflammation
    • Arnold, J. N., Saldova, R., Hamid, U. M., and Rudd, P. M. (2008) Evaluation of the serum N-linked glycome for the diagnosis of cancer and chronic inflammation. Proteomics 8, 3284-3293
    • (2008) Proteomics , vol.8 , pp. 3284-3293
    • Arnold, J.N.1    Saldova, R.2    Hamid, U.M.3    Rudd, P.M.4
  • 24
    • 79952389488 scopus 로고    scopus 로고
    • Glycomic and glycoproteomic analysis of serum from patients with stomach cancer reveals potential markers arising from host defense response mechanisms
    • Bones, J., Byrne, J. C., O'Donoghue, N., McManus, C., Scaife, C., Boissin, H., Nastase, A., and Rudd, P. M. (2011) Glycomic and glycoproteomic analysis of serum from patients with stomach cancer reveals potential markers arising from host defense response mechanisms. J. Proteome Res. 10, 1246-1265
    • (2011) J. Proteome Res. , vol.10 , pp. 1246-1265
    • Bones, J.1    Byrne, J.C.2    O'Donoghue, N.3    McManus, C.4    Scaife, C.5    Boissin, H.6    Nastase, A.7    Rudd, P.M.8
  • 25
    • 34447097453 scopus 로고    scopus 로고
    • Analysis of protein glycosylation by mass spectrometry
    • Morelle, W., and Michalski, J. C. (2007) Analysis of protein glycosylation by mass spectrometry. Nat. Protoc. 2, 1585-1602
    • (2007) Nat. Protoc. , vol.2 , pp. 1585-1602
    • Morelle, W.1    Michalski, J.C.2
  • 26
    • 79551499066 scopus 로고    scopus 로고
    • Glycan analysis by modern instrumental methods
    • Pabst, M., and Altmann, F. (2011) Glycan analysis by modern instrumental methods. Proteomics 11, 631-643
    • (2011) Proteomics , vol.11 , pp. 631-643
    • Pabst, M.1    Altmann, F.2
  • 27
    • 58149391280 scopus 로고    scopus 로고
    • Glycosylation of serum proteins in inflam- matory diseases
    • Gornik, O., and Lauc, G. (2008) Glycosylation of serum proteins in inflam- matory diseases. Dis. Markers 25, 267-278
    • (2008) Dis. Markers , vol.25 , pp. 267-278
    • Gornik, O.1    Lauc, G.2
  • 28
    • 0001644020 scopus 로고    scopus 로고
    • The human plasma proteome: History, character, and diagnostic prospects
    • Anderson, N. L., and Anderson, N. G. (2002) The human plasma proteome: history, character, and diagnostic prospects. Mol. Cell. Proteomics 1, 845-867
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 845-867
    • Anderson, N.L.1    Anderson, N.G.2
  • 29
    • 34447326804 scopus 로고
    • A simple and rapid method for the permethylation of carbohydrates
    • Ciucanu, I., and Kerek, F. (1984) A simple and rapid method for the permethylation of carbohydrates. Carbohydr. Res. 131, 209-217
    • (1984) Carbohydr. Res. , vol.131 , pp. 209-217
    • Ciucanu, I.1    Kerek, F.2
  • 30
    • 34848927484 scopus 로고    scopus 로고
    • The glycan builder: A fast, intuitive and flexible software tool for building and displaying glycan structures
    • Ceroni, A., Dell, A., and Haslam, S. M. (2007) The Glycan Builder: a fast, intuitive and flexible software tool for building and displaying glycan structures. Source Code Biol. Med. 2, 3
    • (2007) Source Code Biol. Med. , vol.2 , pp. 3
    • Ceroni, A.1    Dell, A.2    Haslam, S.M.3
  • 32
    • 46749110034 scopus 로고    scopus 로고
    • FactoMineR: An R package for multivariate analysis
    • Lê, S., Josse, J., and Husson, F. (2008) FactoMineR: an R package for multivariate analysis. J. Stat. Soft. 25, 1-18
    • (2008) J. Stat. Soft. , vol.25 , pp. 1-18
    • Lê, S.1    Josse, J.2    Husson, F.3
  • 35
    • 34248334942 scopus 로고    scopus 로고
    • Reproducibility in protein profiling by MALDI-TOF mass spectrometry
    • Albrethsen, J. (2007) Reproducibility in protein profiling by MALDI-TOF mass spectrometry. Clin. Chem. 53, 852-858
    • (2007) Clin. Chem. , vol.53 , pp. 852-858
    • Albrethsen, J.1
  • 36
    • 0142151385 scopus 로고    scopus 로고
    • Overcoming technical variation and biological variation in quantitative proteomics
    • Molloy, M. P., Brzezinski, E. E., Hang, J., McDowell, M. T., and VanBogelen, R. A. (2003) Overcoming technical variation and biological variation in quantitative proteomics. Proteomics 3, 1912-1919
    • (2003) Proteomics , vol.3 , pp. 1912-1919
    • Molloy, M.P.1    Brzezinski, E.E.2    Hang, J.3    McDowell, M.T.4    VanBogelen, R.A.5
  • 37
    • 17044432706 scopus 로고    scopus 로고
    • Large-scale evaluation of quantitative reproducibility and proteome coverage using acid cleavable isotope coded affinity tag mass spectrometry for proteomic profiling
    • Molloy, M. P., Donohoe, S., Brzezinski, E. E., Kilby, G. W., Stevenson, T. I., Baker, J. D., Goodlett, D. R., and Gage, D. A. (2005) Large-scale evaluation of quantitative reproducibility and proteome coverage using acid cleavable isotope coded affinity tag mass spectrometry for proteomic profiling. Proteomics 5, 1204-1208
    • (2005) Proteomics , vol.5 , pp. 1204-1208
    • Molloy, M.P.1    Donohoe, S.2    Brzezinski, E.E.3    Kilby, G.W.4    Stevenson, T.I.5    Baker, J.D.6    Goodlett, D.R.7    Gage, D.A.8
  • 38
    • 35548952624 scopus 로고    scopus 로고
    • A method for improving SELDI-TOF mass spectrometry data quality
    • Whistler, T., Rollin, D., and Vernon, S. D. (2007) A method for improving SELDI-TOF mass spectrometry data quality. Proteome Sci. 5, 14
    • (2007) Proteome Sci. , vol.5 , pp. 14
    • Whistler, T.1    Rollin, D.2    Vernon, S.D.3
  • 39
    • 0026332953 scopus 로고
    • Glycosylation of alpha 1-acid glycoprotein in relation to duration of disease in acute and chronic infection and inflammation
    • Fassbender, K., Zimmerli, W., Kissling, R., Sobieska, M., Aeschlimann, A., Kellner, M., and Muller, W. (1991) Glycosylation of alpha 1-acid glycoprotein in relation to duration of disease in acute and chronic infection and inflammation. Clin. Chim. Acta 203, 315-327
    • (1991) Clin. Chim. Acta , vol.203 , pp. 315-327
    • Fassbender, K.1    Zimmerli, W.2    Kissling, R.3    Sobieska, M.4    Aeschlimann, A.5    Kellner, M.6    Muller, W.7
  • 40
    • 2942552909 scopus 로고    scopus 로고
    • Chronic oxidative stress and radiation- induced late normal tissue injury: A review
    • Robbins, M. E., and Zhao, W. (2004) Chronic oxidative stress and radiation- induced late normal tissue injury: a review. Int. J. Radiat. Biol. 80, 251-259
    • (2004) Int. J. Radiat. Biol. , vol.80 , pp. 251-259
    • Robbins, M.E.1    Zhao, W.2
  • 43
    • 24044534176 scopus 로고    scopus 로고
    • Increased sialylation and defucosylation of plasma proteins are early events in the acute phase response
    • Chavan, M. M., Kawle, P. D., and Mehta, N. G. (2005) Increased sialylation and defucosylation of plasma proteins are early events in the acute phase response. Glycobiology 15, 838-848
    • (2005) Glycobiology , vol.15 , pp. 838-848
    • Chavan, M.M.1    Kawle, P.D.2    Mehta, N.G.3
  • 44
    • 39749202763 scopus 로고    scopus 로고
    • IL-6 and IL-8 increase the expression of glycosyltransferases and sulfotransferases involved in the biosynthesis of sialylated and/or sulfated lewisx epitopes in the human bronchial mucosa
    • Groux-Degroote, S., Krzewinski-Recchi, M. A., Cazet, A., Vincent, A., Le- houx, S., Lafitte, J. J., Van Seuningen, I., and Delannoy, P. (2008) IL-6 and IL-8 increase the expression of glycosyltransferases and sulfotransferases involved in the biosynthesis of sialylated and/or sulfated Lewisx epitopes in the human bronchial mucosa. Biochem. J. 410, 213-223
    • (2008) Biochem. J. , vol.410 , pp. 213-223
    • Groux-Degroote, S.1    Krzewinski-Recchi, M.A.2    Cazet, A.3    Vincent, A.4    Le-Houx, S.5    Lafitte, J.J.6    Van Seuningen, I.7    Delannoy, P.8
  • 47
    • 0028291625 scopus 로고
    • Differential expression of five sialyltransferase genes in human tissues
    • Kitagawa, H., and Paulson, J. C. (1994) Differential expression of five sialyltransferase genes in human tissues. J. Biol. Chem. 269, 17872-17878
    • (1994) J. Biol. Chem. , vol.269 , pp. 17872-17878
    • Kitagawa, H.1    Paulson, J.C.2
  • 48
    • 34447327216 scopus 로고    scopus 로고
    • Gender disparity in liver cancer due to sex differences in MyD88-dependent IL-6 production
    • Naugler, W. E., Sakurai, T., Kim, S., Maeda, S., Kim, K., Elsharkawy, A. M., and Karin, M. (2007) Gender disparity in liver cancer due to sex differences in MyD88-dependent IL-6 production. Science 317, 121-124
    • (2007) Science , vol.317 , pp. 121-124
    • Naugler, W.E.1    Sakurai, T.2    Kim, S.3    Maeda, S.4    Kim, K.5    Elsharkawy, A.M.6    Karin, M.7
  • 49
    • 0028987134 scopus 로고
    • CD22-mediated cell adhe- sion to cytokine-activated human endothelial cells. Positive and negative regulation by alpha 2-6-sialylation of cellular glycoproteins
    • Hanasaki, K., Varki, A., and Powell, L. D. (1995) CD22-mediated cell adhe- sion to cytokine-activated human endothelial cells. Positive and negative regulation by alpha 2-6-sialylation of cellular glycoproteins. J. Biol. Chem. 270, 7533-7542
    • (1995) J. Biol. Chem. , vol.270 , pp. 7533-7542
    • Hanasaki, K.1    Varki, A.2    Powell, L.D.3
  • 50
    • 0028177588 scopus 로고
    • Cytokine-induced beta-galactoside alpha-2,6-sialyltransferase in human endothelial cells mediates alpha 2,6-sialylation of adhesion molecules and CD22 ligands
    • Hanasaki, K., Varki, A., Stamenkovic, I., and Bevilacqua, M. P. (1994) Cytokine-induced beta-galactoside alpha-2,6-sialyltransferase in human endothelial cells mediates alpha 2,6-sialylation of adhesion molecules and CD22 ligands. J. Biol. Chem. 269, 10637-10643
    • (1994) J. Biol. Chem. , vol.269 , pp. 10637-10643
    • Hanasaki, K.1    Varki, A.2    Stamenkovic, I.3    Bevilacqua, M.P.4
  • 51
    • 33750518016 scopus 로고    scopus 로고
    • Interleukin- 1beta induces sialyl lewis X on hepatocellular carcinoma HuH-7 cells via enhanced expression of ST3Gal IV and FUT VI gene
    • Higai, K., Miyazaki, N., Azuma, Y., and Matsumoto, K. (2006) Interleukin- 1beta induces sialyl Lewis X on hepatocellular carcinoma HuH-7 cells via enhanced expression of ST3Gal IV and FUT VI gene. FEBS Lett. 580, 6069-6075
    • (2006) FEBS Lett. , vol.580 , pp. 6069-6075
    • Higai, K.1    Miyazaki, N.2    Azuma, Y.3    Matsumoto, K.4
  • 52
    • 24044506666 scopus 로고    scopus 로고
    • Inflammation-dependent changes in alpha2,3-, alpha2,6-, and alpha2,8-sialic acid glycotopes on serum glycoproteins in mice
    • Yasukawa, Z., Sato, C., and Kitajima, K. (2005) Inflammation-dependent changes in alpha2,3-, alpha2,6-, and alpha2,8-sialic acid glycotopes on serum glycoproteins in mice. Glycobiology 15, 827-837
    • (2005) Glycobiology , vol.15 , pp. 827-837
    • Yasukawa, Z.1    Sato, C.2    Kitajima, K.3
  • 53
    • 84860250120 scopus 로고    scopus 로고
    • Acute phase glycoproteins: Bystand- ers or participants in carcinogenesis?
    • Dempsey, E., and Rudd, P. M. (2012) Acute phase glycoproteins: bystand- ers or participants in carcinogenesis? Ann. N. Y. Acad. Sci. 1253, 122-132
    • (2012) Ann. N. Y. Acad. Sci. , vol.1253 , pp. 122-132
    • Dempsey, E.1    Rudd, P.M.2
  • 54
    • 0026445723 scopus 로고
    • Selectins: Interpreters of cell-specific carbohydrate information during inflammation
    • Lasky, L. A. (1992) Selectins: interpreters of cell-specific carbohydrate information during inflammation. Science 258, 964-969
    • (1992) Science , vol.258 , pp. 964-969
    • Lasky, L.A.1
  • 55
    • 0027410273 scopus 로고
    • Inflammation-induced expression of sialyl lewis X-containing glycan structures on alpha 1-acid glycoprotein (orosomucoid) in human sera
    • De Graaf, T. W., Van der Stelt, M. E., Anbergen, M. G., and van Dijk, W. (1993) Inflammation-induced expression of sialyl Lewis X-containing glycan structures on alpha 1-acid glycoprotein (orosomucoid) in human sera. J. Exp. Med. 177, 657-666
    • (1993) J. Exp. Med. , vol.177 , pp. 657-666
    • De Graaf, T.W.1    Van Der Stelt, M.E.2    Anbergen, M.G.3    Van Dijk, W.4
  • 56
    • 0025572708 scopus 로고
    • Recognition by ELAM-1 of the sialyl-lex determinant on myeloid and tumor cells
    • Walz, G., Aruffo, A., Kolanus, W., Bevilacqua, M., and Seed, B. (1990) Recognition by ELAM-1 of the sialyl-Lex determinant on myeloid and tumor cells. Science 250, 1132-1135
    • (1990) Science , vol.250 , pp. 1132-1135
    • Walz, G.1    Aruffo, A.2    Kolanus, W.3    Bevilacqua, M.4    Seed, B.5


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