메뉴 건너뛰기




Volumn 25, Issue 4-5, 2008, Pages 267-278

Glycosylation of serum proteins in inflammatory diseases

Author keywords

Glycosylation; Inflammatory diseases; Pancreatitis; Rheumatoid arthritis; Sepsis; Serum proteins; Systemic lupus erythematosus

Indexed keywords

ALPHA 2 MACROGLOBULIN; C REACTIVE PROTEIN; GLYCAN; HAPTOGLOBIN; IMMUNOGLOBULIN A; IMMUNOGLOBULIN G; OROSOMUCOID; PLASMA PROTEIN; TRANSFERRIN;

EID: 58149391280     PISSN: 02780240     EISSN: None     Source Type: Journal    
DOI: 10.1155/2008/493289     Document Type: Review
Times cited : (203)

References (102)
  • 2
    • 0033545342 scopus 로고    scopus 로고
    • Acute-phase proteins and other systemic responses to inflammation
    • C. Gabay and I. Kushner, Acute-phase proteins and other systemic responses to inflammation, N Engl J Med 340 (1999), 448-454.
    • (1999) N Engl J Med , vol.340 , pp. 448-454
    • Gabay, C.1    Kushner, I.2
  • 3
    • 0004106191 scopus 로고    scopus 로고
    • C.S. Harbor, ed, New York: Cold Spring Harbor Laboratory Press
    • A. Varki et al., Essentials of glycobiology, C.S. Harbor, ed., 1999, New York: Cold Spring Harbor Laboratory Press.
    • (1999) Essentials of glycobiology
    • Varki, A.1
  • 4
    • 0035937574 scopus 로고    scopus 로고
    • Searching for medicine's sweet spot
    • J. Alper, Searching for medicine's sweet spot, Science 291 (2001), 2338-2343.
    • (2001) Science , vol.291 , pp. 2338-2343
    • Alper, J.1
  • 7
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in cellular mechanisms of health and disease
    • K. Ohtsubo and J.D. Marth, Glycosylation in cellular mechanisms of health and disease, Cell 126 (2006), 855-867.
    • (2006) Cell , vol.126 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 8
    • 33646111199 scopus 로고    scopus 로고
    • Sweet secret of the multicellular life
    • G. Lauc, Sweet secret of the multicellular life, Biochim Biophys Acta 1760 (2006), 525-526.
    • (2006) Biochim Biophys Acta , vol.1760 , pp. 525-526
    • Lauc, G.1
  • 9
    • 27844500647 scopus 로고    scopus 로고
    • Glycoproteomics: Protein modifications for versatile functions. Meeting on glycoproteomics
    • R.T. Lee, G. Lauc, and Y.C. Lee, Glycoproteomics: protein modifications for versatile functions. Meeting on glycoproteomics, EMBO Rep 6(2005), 1018-22.
    • (2005) EMBO Rep , vol.6 , pp. 1018-1022
    • Lee, R.T.1    Lauc, G.2    Lee, Y.C.3
  • 10
    • 0036019907 scopus 로고    scopus 로고
    • Protein glycosylation: Nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds
    • R.G. Spiro, Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds, Glycobiology 12 (2002), 43R-56R.
    • (2002) Glycobiology , vol.12
    • Spiro, R.G.1
  • 11
    • 0034918138 scopus 로고    scopus 로고
    • The impact of glycobiology on medicine
    • J. Axford, The impact of glycobiology on medicine, Trends Immunol 22 (2001), 237-239.
    • (2001) Trends Immunol , vol.22 , pp. 237-239
    • Axford, J.1
  • 12
    • 0026772958 scopus 로고
    • N-glycosylation of serum proteins in disease and its investigation using lectins
    • G.A. Turner, N-glycosylation of serum proteins in disease and its investigation using lectins, Clin Chim Acta 208 (1992), 149-171.
    • (1992) Clin Chim Acta , vol.208 , pp. 149-171
    • Turner, G.A.1
  • 14
    • 0019819634 scopus 로고
    • Comparative study of the carbohydrate moieties of rat and human plasma alpha 1-acid glycoproteins
    • H. Yoshima, A. Matsumoto, T. Mizuochi, T. Kawasaki and A. Kobata, Comparative study of the carbohydrate moieties of rat and human plasma alpha 1-acid glycoproteins, J Biol Chem 256 (1981), 8476-8484.
    • (1981) J Biol Chem , vol.256 , pp. 8476-8484
    • Yoshima, H.1    Matsumoto, A.2    Mizuochi, T.3    Kawasaki, T.4    Kobata, A.5
  • 15
    • 0642274950 scopus 로고    scopus 로고
    • Drug binding analysis of human alpha 1-acid glycoprotein using capillary electrophoresis
    • Y. Kuroda, A. Shibukawa and T. Nakagawa, Drug binding analysis of human alpha 1-acid glycoprotein using capillary electrophoresis, Yakugaku Zasshi 123 (2003), 781-788.
    • (2003) Yakugaku Zasshi , vol.123 , pp. 781-788
    • Kuroda, Y.1    Shibukawa, A.2    Nakagawa, T.3
  • 16
    • 0031809628 scopus 로고    scopus 로고
    • Inflammation-induced expression of sialyl LewisX is not restricted to alpha1-acid glycoprotein but also occurs to a lesser extent on alpha1-antichymotrypsin and haptoglobin
    • E.C. Brinkman-van der Linden, P.F. de Haan, E.C. Havenaar and W. van Dijk, Inflammation-induced expression of sialyl LewisX is not restricted to alpha1-acid glycoprotein but also occurs to a lesser extent on alpha1-antichymotrypsin and haptoglobin, Glycoconj J 15 (1998), 177-182.
    • (1998) Glycoconj J , vol.15 , pp. 177-182
    • Brinkman-van der Linden, E.C.1    de Haan, P.F.2    Havenaar, E.C.3    van Dijk, W.4
  • 17
    • 23844520619 scopus 로고    scopus 로고
    • Glycosylation of site-specific glycans of alpha1-acid glycoprotein and alterations in acute and chronic inflammation
    • K. Higai, Y. Aoki, Y. Azuma and K. Matsumoto, Glycosylation of site-specific glycans of alpha1-acid glycoprotein and alterations in acute and chronic inflammation, Biochim Biophys Acta 1725 (2005), 128-135.
    • (2005) Biochim Biophys Acta , vol.1725 , pp. 128-135
    • Higai, K.1    Aoki, Y.2    Azuma, Y.3    Matsumoto, K.4
  • 18
    • 0037365579 scopus 로고    scopus 로고
    • Altered glycosylation of alpha1-acid glycoprotein in patients with inflammation and diabetes mellitus
    • K. Higai, Y. Azuma, Y. Aoki and K. Matsumoto, Altered glycosylation of alpha1-acid glycoprotein in patients with inflammation and diabetes mellitus, Clin Chim Acta 329 (2003), 117-125.
    • (2003) Clin Chim Acta , vol.329 , pp. 117-125
    • Higai, K.1    Azuma, Y.2    Aoki, Y.3    Matsumoto, K.4
  • 19
    • 0034747132 scopus 로고    scopus 로고
    • D.C. Poland, C.G. Schalkwijk, C.D. Stehouwer, C.A. Koeleman, B. van het Hofand W. van Dijk, Increased alpha3-fucosylation of alpha1-acid glycoprotein in Type I diabetic patients is related to vascular function, Glycoconj J 18 (2001), 261-268.
    • D.C. Poland, C.G. Schalkwijk, C.D. Stehouwer, C.A. Koeleman, B. van het Hofand W. van Dijk, Increased alpha3-fucosylation of alpha1-acid glycoprotein in Type I diabetic patients is related to vascular function, Glycoconj J 18 (2001), 261-268.
  • 20
    • 0023774268 scopus 로고
    • Glycosylation of three molecular forms of human alpha 1-acid glycoprotein having different interactions with concanavalin A. Variations in the occurrence of di-, tri-, and tetraantennary glycans and the degree of sialylation
    • M.F. Bierhuizen, M. De Wit, C.A. Govers, W. Ferwerda, C. Koeleman, O. Pos and W. Van Dijk, Glycosylation of three molecular forms of human alpha 1-acid glycoprotein having different interactions with concanavalin A. Variations in the occurrence of di-, tri-, and tetraantennary glycans and the degree of sialylation, Eur J Biochem 175 (1988), 387-394.
    • (1988) Eur J Biochem , vol.175 , pp. 387-394
    • Bierhuizen, M.F.1    De Wit, M.2    Govers, C.A.3    Ferwerda, W.4    Koeleman, C.5    Pos, O.6    Van Dijk, W.7
  • 21
    • 0027410273 scopus 로고
    • Inflammation-induced expression of sialyl Lewis X-containing glycan structures on alpha 1-acid glycoprotein (orosomucoid) in human sera
    • T.W. De Graaf, M.E. Van der Stelt, M.G. Anbergen and W. van Dijk, Inflammation-induced expression of sialyl Lewis X-containing glycan structures on alpha 1-acid glycoprotein (orosomucoid) in human sera, J Exp Med 177 (1993), 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
  • 22
    • 0024514114 scopus 로고
    • Serum IgA, acute phase proteins, and glycosylation of alpha 1-acid glycoprotein in ankylosing spondylitis
    • A. Mackiewicz, M.A. Khan, T.L. Reynolds, S. van der Linden and I. Kushner, Serum IgA, acute phase proteins, and glycosylation of alpha 1-acid glycoprotein in ankylosing spondylitis, Ann Rheum Dis 48 (1989), 99-103.
    • (1989) Ann Rheum Dis , vol.48 , pp. 99-103
    • Mackiewicz, A.1    Khan, M.A.2    Reynolds, T.L.3    van der Linden, S.4    Kushner, I.5
  • 23
    • 0023252023 scopus 로고
    • Microheterogeneity of alpha 1-acid glycoprotein in the detection of intercurrent infection in systemic lupus erythematosus
    • A. Mackiewicz, R. Marcinkowska-Pieta, S. Ballou, S. Mackiewicz and I. Kushner, Microheterogeneity of alpha 1-acid glycoprotein in the detection of intercurrent infection in systemic lupus erythematosus, Arthritis Rheum 30 (1987), 513-518.
    • (1987) Arthritis Rheum , vol.30 , pp. 513-518
    • Mackiewicz, A.1    Marcinkowska-Pieta, R.2    Ballou, S.3    Mackiewicz, S.4    Kushner, I.5
  • 24
    • 0022264068 scopus 로고
    • Microheterogeneity of alpha 1-acid glycoprotein: Lack of discrimination between benign and malignant inflammatory disease of the lung
    • A.J. Bleasby, J.C. Knowles and N.J. Cooke, Microheterogeneity of alpha 1-acid glycoprotein: lack of discrimination between benign and malignant inflammatory disease of the lung, Clin Chim Acta 150 (1985), 231-235.
    • (1985) Clin Chim Acta , vol.150 , pp. 231-235
    • Bleasby, A.J.1    Knowles, J.C.2    Cooke, N.J.3
  • 26
    • 0026332953 scopus 로고
    • Glycosylation of alpha 1-acid glycoprotein in relation to duration of disease in acute and chronic infection and inflammation
    • K. Fassbender, W. Zimmerli, R. Kissling, M. Sobieska, A. Aeschlimann, M. Kellner and W. Muller, Glycosylation of alpha 1-acid glycoprotein in relation to duration of disease in acute and chronic infection and inflammation, Clin Chim Acta 203 (1991), 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
  • 27
    • 0025201215 scopus 로고
    • Changes in the serum concentration and the glycosylation of human alpha 1-acid glycoprotein and alpha 1-protease inhibitor in severely burned persons: Relation to interleukin-6 levels
    • O. Pos, M.E. van der Stelt, G.J. Wolbink, M.W. Nijsten, G.L. van der Tempel and W. van Dijk, Changes in the serum concentration and the glycosylation of human alpha 1-acid glycoprotein and alpha 1-protease inhibitor in severely burned persons: relation to interleukin-6 levels, Clin Exp Immunol 82 (1990), 579-582.
    • (1990) Clin Exp Immunol , vol.82 , pp. 579-582
    • Pos, O.1    van der Stelt, M.E.2    Wolbink, G.J.3    Nijsten, M.W.4    van der Tempel, G.L.5    van Dijk, W.6
  • 28
    • 0028981439 scopus 로고
    • Alpha 1-acid glycoprotein (orosomucoid): Pathophysiological changes in glycosylation in relation to its function
    • W. van Dijk, E.C. Havenaar and E.C. Brinkman-van der Linden, Alpha 1-acid glycoprotein (orosomucoid): pathophysiological changes in glycosylation in relation to its function, Glycoconj J 12 (1995), 227-233.
    • (1995) Glycoconj J , vol.12 , pp. 227-233
    • van Dijk, W.1    Havenaar, E.C.2    Brinkman-van der Linden, E.C.3
  • 29
    • 0030011909 scopus 로고    scopus 로고
    • Toward a theory regarding the pathogenesis of the systemic inflammatory response syndrome: What we do and do not know about cytokine regulation
    • R.C. Bone, Toward a theory regarding the pathogenesis of the systemic inflammatory response syndrome: what we do and do not know about cytokine regulation, Crit Care Med 24 (1996), 163-172.
    • (1996) Crit Care Med , vol.24 , pp. 163-172
    • Bone, R.C.1
  • 30
    • 0029669985 scopus 로고    scopus 로고
    • Glycosylation of alpha 1-acid glycoprotein in septic shock: Changes in degree of branching and in expression of sialyl Lewis(x) groups
    • E.C. Brinkman-van der Linden, E.C. van Ommen and W. van Dijk, Glycosylation of alpha 1-acid glycoprotein in septic shock: changes in degree of branching and in expression of sialyl Lewis(x) groups, Glycoconj J 13 (1996), 27-31.
    • (1996) Glycoconj J , vol.13 , pp. 27-31
    • Brinkman-van der Linden, E.C.1    van Ommen, E.C.2    van Dijk, W.3
  • 31
    • 0019522383 scopus 로고
    • Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution
    • J. Deisenhofer, Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution, Biochemistry 20 (1981), 2361-2370.
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 33
    • 0035827222 scopus 로고    scopus 로고
    • Molecular basis for immune complex recognition: A comparison of Fc-receptor structures
    • P. Sondermann, J. Kaiser and U. Jacob, Molecular basis for immune complex recognition: a comparison of Fc-receptor structures, J Mol Biol 309 (2001), 737-749.
    • (2001) J Mol Biol , vol.309 , pp. 737-749
    • Sondermann, P.1    Kaiser, J.2    Jacob, U.3
  • 34
    • 30444461383 scopus 로고    scopus 로고
    • Fcgamma receptors: Old friends and new family members
    • F. Nimmerjahn and J.V. Ravetch, Fcgamma receptors: old friends and new family members, Immunity 24 (2006), 19-28.
    • (2006) Immunity , vol.24 , pp. 19-28
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 35
    • 33746888249 scopus 로고    scopus 로고
    • Antiinflammatory activity of immunoglobulin G resulting from Fc sialylation
    • Y. Kaneko, F. Nimmerjahn and J.V. Ravetch, Antiinflammatory activity of immunoglobulin G resulting from Fc sialylation, Science 313 (2006), 670-673.
    • (2006) Science , vol.313 , pp. 670-673
    • Kaneko, Y.1    Nimmerjahn, F.2    Ravetch, J.V.3
  • 37
    • 0035910392 scopus 로고    scopus 로고
    • Anti-inflammatory activity of IVIG mediated through the inhibitory Fc receptor
    • A. Samuelsson, T.L. Towers and J.V. Ravetch, Anti-inflammatory activity of IVIG mediated through the inhibitory Fc receptor, Science 291 (2001), 484-486.
    • (2001) Science , vol.291 , pp. 484-486
    • Samuelsson, A.1    Towers, T.L.2    Ravetch, J.V.3
  • 38
    • 33645080442 scopus 로고    scopus 로고
    • Pathology and protection in nephrotoxic nephritis is determined by selective engagement of specific Fc receptors
    • Y. Kaneko, F. Nimmerjahn, M.P. Madaio and J.V. Ravetch, Pathology and protection in nephrotoxic nephritis is determined by selective engagement of specific Fc receptors, J Exp Med 203 (2006), 789-797.
    • (2006) J Exp Med , vol.203 , pp. 789-797
    • Kaneko, Y.1    Nimmerjahn, F.2    Madaio, M.P.3    Ravetch, J.V.4
  • 39
    • 0027115518 scopus 로고
    • Manipulating the immune system with immune globulin
    • J.M. Dwyer, Manipulating the immune system with immune globulin, N Engl J Med 326 (1992), 107-116.
    • (1992) N Engl J Med , vol.326 , pp. 107-116
    • Dwyer, J.M.1
  • 40
    • 0032424701 scopus 로고    scopus 로고
    • Sialyl Lewis(x) expression on IgG in rheumatoid arthritis and other arthritic conditions: A preliminary study
    • M.T. Goodarzi, J.S. Axford, S.S. Varanasi, A. Alavi, G. Cunnane, O. Fitzgerald and G.A. Turner, Sialyl Lewis(x) expression on IgG in rheumatoid arthritis and other arthritic conditions: a preliminary study, Glycoconj J 15 (1998), 1149-1154.
    • (1998) Glycoconj J , vol.15 , pp. 1149-1154
    • Goodarzi, M.T.1    Axford, J.S.2    Varanasi, S.S.3    Alavi, A.4    Cunnane, G.5    Fitzgerald, O.6    Turner, G.A.7
  • 41
    • 0031823336 scopus 로고    scopus 로고
    • Quantitation of the oligosaccharides of human serum IgG from patients with rheumatoid arthritis: A critical evaluation of different methods
    • F.H. Routier, E.F. Hounsell, P.M. Rudd, N. Takahashi, A. Bond, F.C. Hay, A. Alavi, J.S. Axford and R. Jefferis, Quantitation of the oligosaccharides of human serum IgG from patients with rheumatoid arthritis: a critical evaluation of different methods, J Immunol Methods 213 (1998), 113-130.
    • (1998) J Immunol Methods , vol.213 , pp. 113-130
    • Routier, F.H.1    Hounsell, E.F.2    Rudd, P.M.3    Takahashi, N.4    Bond, A.5    Hay, F.C.6    Alavi, A.7    Axford, J.S.8    Jefferis, R.9
  • 42
    • 0032881550 scopus 로고    scopus 로고
    • Glycosylation and rheumatic disease
    • J.S. Axford, Glycosylation and rheumatic disease, Biochim Biophys Acta 1455 (1999), 219-229.
    • (1999) Biochim Biophys Acta , vol.1455 , pp. 219-229
    • Axford, J.S.1
  • 43
    • 0029962752 scopus 로고    scopus 로고
    • Site-specific glycosylation of human immunoglobulin G is altered in four rheumatoid arthritis patients
    • A. Youings, S.C. Chang, R.A. Dwek and I.G. Scragg, Site-specific glycosylation of human immunoglobulin G is altered in four rheumatoid arthritis patients, Biochem J 314(Pt 2) (1996), 621-630.
    • (1996) Biochem J , vol.314 , Issue.PART 2 , pp. 621-630
    • Youings, A.1    Chang, S.C.2    Dwek, R.A.3    Scragg, I.G.4
  • 45
    • 34347235526 scopus 로고    scopus 로고
    • Agalactosylated IgG antibodies depend on cellular Fc receptors for in vivo activity
    • F. Nimmerjahn, R.M. Anthony and J.V. Ravetch, Agalactosylated IgG antibodies depend on cellular Fc receptors for in vivo activity, Proc Natl Acad Sci USA 104 (2007), 8433-8437.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 8433-8437
    • Nimmerjahn, F.1    Anthony, R.M.2    Ravetch, J.V.3
  • 46
    • 0036867947 scopus 로고    scopus 로고
    • Binding of rheumatoid and lupus synovial fluids and sera-derived human IgG rheumatoid factor to degalactosylated IgG
    • C.T. Chou, Binding of rheumatoid and lupus synovial fluids and sera-derived human IgG rheumatoid factor to degalactosylated IgG, Arch Med Res 33 (2002), 541-544.
    • (2002) Arch Med Res , vol.33 , pp. 541-544
    • Chou, C.T.1
  • 48
    • 0029914789 scopus 로고    scopus 로고
    • Agalactosyl IgG Gal(o)-an analysis of its clinical utility in the long-term follow-up of patients with rheumatoid arthritis
    • K. Bodman-Smith, N. Sumar, H. Sinclair, I. Roitt, D. Isenberg and A. Young, Agalactosyl IgG Gal(o)-an analysis of its clinical utility in the long-term follow-up of patients with rheumatoid arthritis, Br J Rheumatol 35 (1996), 1063-1066.
    • (1996) Br J Rheumatol , vol.35 , pp. 1063-1066
    • Bodman-Smith, K.1    Sumar, N.2    Sinclair, H.3    Roitt, I.4    Isenberg, D.5    Young, A.6
  • 49
    • 0028065317 scopus 로고
    • The severity of rheumatoid arthritis: A 6-year followup study of younger women with symptoms of recent onset
    • D. van Zeben, J.M. Hazes, A.H. Zwinderman, J.P. Vandenbroucke and F.C. Breedveld, The severity of rheumatoid arthritis: a 6-year followup study of younger women with symptoms of recent onset, J Rheumatol 21 (1994), 1620-1625.
    • (1994) J Rheumatol , vol.21 , pp. 1620-1625
    • van Zeben, D.1    Hazes, J.M.2    Zwinderman, A.H.3    Vandenbroucke, J.P.4    Breedveld, F.C.5
  • 50
    • 0028009255 scopus 로고
    • Early agalactosylation of IgG is associated with a more progressive disease course in patients with rheumatoid arthritis: Results of a follow-up study
    • D. van Zeben, G.A. Rook, J.M. Hazes, A.H. Zwinderman, Y. Zhang, S. Ghelani, T.W. Rademacher and F.C. Breedveld, Early agalactosylation of IgG is associated with a more progressive disease course in patients with rheumatoid arthritis: results of a follow-up study, Br J Rheumatol 33 (1994), 36-43.
    • (1994) Br J Rheumatol , vol.33 , pp. 36-43
    • van Zeben, D.1    Rook, G.A.2    Hazes, J.M.3    Zwinderman, A.H.4    Zhang, Y.5    Ghelani, S.6    Rademacher, T.W.7    Breedveld, F.C.8
  • 52
    • 0023894058 scopus 로고
    • Galactosylation of IgG associated oligosaccharides: Reduction in patients with adult and juvenile onset rheumatoid arthritis and relation to disease activity
    • R.B. Parekh, I.M. Roitt, D.A. Isenberg, R.A. Dwek, B.M. Ansell and T.W. Rademacher, Galactosylation of IgG associated oligosaccharides: reduction in patients with adult and juvenile onset rheumatoid arthritis and relation to disease activity, Lancet 1 (1988), 966-969.
    • (1988) Lancet , vol.1 , pp. 966-969
    • Parekh, R.B.1    Roitt, I.M.2    Isenberg, D.A.3    Dwek, R.A.4    Ansell, B.M.5    Rademacher, T.W.6
  • 53
    • 0344542074 scopus 로고    scopus 로고
    • Fucosylation and galactosylation of IgG heavy chains differ between acute and remission phases of juvenile chronic arthritis
    • M. Flogel, G. Lauc, I. Gornik and B. Macek, Fucosylation and galactosylation of IgG heavy chains differ between acute and remission phases of juvenile chronic arthritis, Clin Chem Lab Med 36 (1998), 99-102.
    • (1998) Clin Chem Lab Med , vol.36 , pp. 99-102
    • Flogel, M.1    Lauc, G.2    Gornik, I.3    Macek, B.4
  • 56
    • 0036324907 scopus 로고    scopus 로고
    • Modified immunoglobulin G glycosylation pattern during turpentine-induced acute inflammation in rats
    • A. Canellada and R.A. Margni, Modified immunoglobulin G glycosylation pattern during turpentine-induced acute inflammation in rats, Medicina (B Aires) 62 (2002), 249-255.
    • (2002) Medicina (B Aires) , vol.62 , pp. 249-255
    • Canellada, A.1    Margni, R.A.2
  • 57
    • 0023912648 scopus 로고
    • Age-related galactosylation of the N-linked oligosaccharides of human serum IgG
    • R. Parekh, I. Roitt, D. Isenberg, R. Dwek and T. Rademacher, Age-related galactosylation of the N-linked oligosaccharides of human serum IgG, J Exp Med 167 (1988), 1731-1736.
    • (1988) J Exp Med , vol.167 , pp. 1731-1736
    • Parekh, R.1    Roitt, I.2    Isenberg, D.3    Dwek, R.4    Rademacher, T.5
  • 61
    • 0026597003 scopus 로고
    • Relationship between interleukin 6, agalactosyl IgG and pristane-induced arthritis
    • Y. Hitsumoto, S.J. Thompson, Y.W. Zhang, G.A. Rook and C.J. Elson, Relationship between interleukin 6, agalactosyl IgG and pristane-induced arthritis, Autoimmunity 11 (1992), 247-254.
    • (1992) Autoimmunity , vol.11 , pp. 247-254
    • Hitsumoto, Y.1    Thompson, S.J.2    Zhang, Y.W.3    Rook, G.A.4    Elson, C.J.5
  • 62
    • 0026699354 scopus 로고
    • Agalactosyl IgG in pristane-induced arthritis. Pregnancy affects the incidence and severity of arthritis and the glycosylation status of IgG
    • S.J. Thompson, Y. Hitsumoto, Y.W. Zhang, G.A. Rook and C.J. Elson, Agalactosyl IgG in pristane-induced arthritis. Pregnancy affects the incidence and severity of arthritis and the glycosylation status of IgG, Clin Exp Immunol 89 (1992), 434-438.
    • (1992) Clin Exp Immunol , vol.89 , pp. 434-438
    • Thompson, S.J.1    Hitsumoto, Y.2    Zhang, Y.W.3    Rook, G.A.4    Elson, C.J.5
  • 63
    • 0034130028 scopus 로고    scopus 로고
    • Immunoglobulin G glycosylation and clinical outcome in rheumatoid arthritis during pregnancy
    • A. Alavi, N. Arden, T.D. Spector and J.S. Axford, Immunoglobulin G glycosylation and clinical outcome in rheumatoid arthritis during pregnancy, J Rheumatol 27 (2000), 1379-1385.
    • (2000) J Rheumatol , vol.27 , pp. 1379-1385
    • Alavi, A.1    Arden, N.2    Spector, T.D.3    Axford, J.S.4
  • 65
    • 34248168090 scopus 로고    scopus 로고
    • The pathogenic role of IgA1 O-linked glycosylation in the pathogenesis of IgA nephropathy
    • J. Barratt, A.C. Smith and J. Feehally, The pathogenic role of IgA1 O-linked glycosylation in the pathogenesis of IgA nephropathy, Nephrology (Carlton) 12 (2007), 275-284.
    • (2007) Nephrology (Carlton) , vol.12 , pp. 275-284
    • Barratt, J.1    Smith, A.C.2    Feehally, J.3
  • 66
    • 0032973358 scopus 로고    scopus 로고
    • Structural features of IgA molecules which contribute to IgA nephropathy
    • J. Feehally and A.C. Allen, Structural features of IgA molecules which contribute to IgA nephropathy, J Nephrol 12 (1999), 59-65.
    • (1999) J Nephrol , vol.12 , pp. 59-65
    • Feehally, J.1    Allen, A.C.2
  • 68
    • 0024562457 scopus 로고
    • Altered glycosylation of serum transferrin of patients with hepatocellular carcinoma
    • K. Yamashita, N. Koide, T. Endo, Y. Iwaki and A. Kobata, Altered glycosylation of serum transferrin of patients with hepatocellular carcinoma, J Biol Chem 264 (1989), 2415-2423.
    • (1989) J Biol Chem , vol.264 , pp. 2415-2423
    • Yamashita, K.1    Koide, N.2    Endo, T.3    Iwaki, Y.4    Kobata, A.5
  • 69
    • 0028296132 scopus 로고
    • Alteration of asparagine-linked glycosylation in serum transferrin of patients with hepatocellular carcinoma
    • K. Matsumoto, Y. Maeda, S. Kato and H. Yuki, Alteration of asparagine-linked glycosylation in serum transferrin of patients with hepatocellular carcinoma, Clin Chim Acta 224 (1994), 1-8.
    • (1994) Clin Chim Acta , vol.224 , pp. 1-8
    • Matsumoto, K.1    Maeda, Y.2    Kato, S.3    Yuki, H.4
  • 71
    • 33750541508 scopus 로고    scopus 로고
    • Prenatal diagnosis of congenital disorder of glycosylation type Ia (CDGIa) by cordocentesis and transferrin isoelectric focussing of serum of a 27-week fetus with non-immune hydrops
    • M. Edwards, F. McKenzie, S. O'Callaghan, D. Somerset, P. Woodford, J. Spilsbury, M. Fietz and J. Fletcher, Prenatal diagnosis of congenital disorder of glycosylation type Ia (CDGIa) by cordocentesis and transferrin isoelectric focussing of serum of a 27-week fetus with non-immune hydrops, Prenat Diagn 26 (2006), 985-988.
    • (2006) Prenat Diagn , vol.26 , pp. 985-988
    • Edwards, M.1    McKenzie, F.2    O'Callaghan, S.3    Somerset, D.4    Woodford, P.5    Spilsbury, J.6    Fietz, M.7    Fletcher, J.8
  • 72
    • 0031034215 scopus 로고    scopus 로고
    • Increased serum concentration of carbohydrate-deficient transferrin in patients with combined pancreas and kidney transplantation
    • T. Arndt, R. Hackler, T. Muller, T.O. Kleine and A.M. Gressner, Increased serum concentration of carbohydrate-deficient transferrin in patients with combined pancreas and kidney transplantation, Clin Chem 43 (1997), 344-351.
    • (1997) Clin Chem , vol.43 , pp. 344-351
    • Arndt, T.1    Hackler, R.2    Muller, T.3    Kleine, T.O.4    Gressner, A.M.5
  • 73
    • 0027076354 scopus 로고
    • Transferrin microheterogeneity in rheumatoid arthritis. Relation with disease activity and anemia of chronic disease
    • R.A. Feelders, G. Vreugdenhil, G. de Jong, A.J. Swaak and H.G. van Eijk, Transferrin microheterogeneity in rheumatoid arthritis. Relation with disease activity and anemia of chronic disease, Rheumatol Int 12 (1992), 195-199.
    • (1992) Rheumatol Int , vol.12 , pp. 195-199
    • Feelders, R.A.1    Vreugdenhil, G.2    de Jong, G.3    Swaak, A.J.4    van Eijk, H.G.5
  • 74
    • 33748497381 scopus 로고    scopus 로고
    • Microheterogeneity of acute phase proteins in patients with ulcerative colitis
    • M. Grzymislawski, K. Derc, M. Sobieska and K. Wiktorowicz, Microheterogeneity of acute phase proteins in patients with ulcerative colitis, World J Gastroenterol 12 (2006), 5191-5195.
    • (2006) World J Gastroenterol , vol.12 , pp. 5191-5195
    • Grzymislawski, M.1    Derc, K.2    Sobieska, M.3    Wiktorowicz, K.4
  • 76
    • 0022543892 scopus 로고
    • Preferential hepatic uptake of iron from rat asialotransferrin: Possible engagement of two receptors
    • J.R. Rudolph, E. Regoeczi, P.A. Chindemi and M.T. Debanne, Preferential hepatic uptake of iron from rat asialotransferrin: possible engagement of two receptors, Am J Physiol 251 (1986), G398-404.
    • (1986) Am J Physiol , vol.251
    • Rudolph, J.R.1    Regoeczi, E.2    Chindemi, P.A.3    Debanne, M.T.4
  • 78
    • 0023732385 scopus 로고
    • Microheterogeneity of human serum transferrin: A biological phenomenon studied by isoelectric focusing in immobilized pH gradients
    • G. de Jong and H.G. van Eijk, Microheterogeneity of human serum transferrin: a biological phenomenon studied by isoelectric focusing in immobilized pH gradients, Electrophoresis 9 (1988), 589-598.
    • (1988) Electrophoresis , vol.9 , pp. 589-598
    • de Jong, G.1    van Eijk, H.G.2
  • 79
    • 0035713119 scopus 로고    scopus 로고
    • Carbohydrate-deficient transferrin for detection and monitoring of sustained heavy drinking. What have we learned? Where do we go from here?
    • R.F. Anton, Carbohydrate-deficient transferrin for detection and monitoring of sustained heavy drinking. What have we learned? Where do we go from here? Alcohol 25 (2001), 185-188.
    • (2001) Alcohol , vol.25 , pp. 185-188
    • Anton, R.F.1
  • 81
    • 0034886115 scopus 로고    scopus 로고
    • Increased serum levels of carbohydrate-deficient transferrin in patients with chronic obstructive pulmonary disease
    • U. Nihlen, P. Montnemery, L.H. Lindholm and C.G. Lofdahl, Increased serum levels of carbohydrate-deficient transferrin in patients with chronic obstructive pulmonary disease, Scand J Clin Lab Invest 61 (2001), 341-347.
    • (2001) Scand J Clin Lab Invest , vol.61 , pp. 341-347
    • Nihlen, U.1    Montnemery, P.2    Lindholm, L.H.3    Lofdahl, C.G.4
  • 82
    • 0031737457 scopus 로고    scopus 로고
    • Elevated carbohydrate-deficient transferrin predicts prolonged intensive care unit stay in traumatized men
    • C.D. Spies, M. Kissner, T. Neumann, S. Blum, C. Voigt, T. Funk, N. Runkel and F. Pragst, Elevated carbohydrate-deficient transferrin predicts prolonged intensive care unit stay in traumatized men, Alcohol Alcohol 33 (1998), 661-669.
    • (1998) Alcohol Alcohol , vol.33 , pp. 661-669
    • Spies, C.D.1    Kissner, M.2    Neumann, T.3    Blum, S.4    Voigt, C.5    Funk, T.6    Runkel, N.7    Pragst, F.8
  • 83
    • 0026331891 scopus 로고
    • Carbohydrate-deficient transferrin in serum: A new marker of potentially harmful alcohol consumption reviewed
    • H. Stibler, Carbohydrate-deficient transferrin in serum: a new marker of potentially harmful alcohol consumption reviewed, Clin Chem 37 (1991), 2029-2037.
    • (1991) Clin Chem , vol.37 , pp. 2029-2037
    • Stibler, H.1
  • 84
    • 41849147087 scopus 로고    scopus 로고
    • Change in transferrin sialylation is a potential prognostic marker for severity of acute pancreatitis
    • O. Gornik, I. Gornik, V. Gašparović and G. Lauc, Change in transferrin sialylation is a potential prognostic marker for severity of acute pancreatitis, Clin Biochem 41 (2008), 504-510.
    • (2008) Clin Biochem , vol.41 , pp. 504-510
    • Gornik, O.1    Gornik, I.2    Gašparović, V.3    Lauc, G.4
  • 86
    • 18544412749 scopus 로고
    • Monosaccharide composition of haptoglobin purified from alcoholic cirrhotic and control sera determined by HPAE
    • A.C. Mann, S. Thompson, C.O. Record, C.H. Self and G.A. Turner, Monosaccharide composition of haptoglobin purified from alcoholic cirrhotic and control sera determined by HPAE, Biochem Soc Trans 21 (1993), 214S.
    • (1993) Biochem Soc Trans , vol.21
    • Mann, A.C.1    Thompson, S.2    Record, C.O.3    Self, C.H.4    Turner, G.A.5
  • 87
    • 0027435685 scopus 로고
    • Abnormally fucosylated haptoglobin as a marker for alcoholic liver disease but not excessive alcohol consumption or non-alcoholic liver disease
    • W. Chambers, S. Thompson, A.W. Skillen, C.O. Record and G.A. Turner, Abnormally fucosylated haptoglobin as a marker for alcoholic liver disease but not excessive alcohol consumption or non-alcoholic liver disease, Clin Chim Acta 219 (1993), 177-182.
    • (1993) Clin Chim Acta , vol.219 , pp. 177-182
    • Chambers, W.1    Thompson, S.2    Skillen, A.W.3    Record, C.O.4    Turner, G.A.5
  • 88
    • 0028235889 scopus 로고
    • Monosaccharide composition of haptoglobin in liver diseases and alcohol abuse: Large changes in glycosylation associated with alcoholic liver disease
    • A.C. Mann, C.O. Record, C.H. Self and G.A. Turner, Monosaccharide composition of haptoglobin in liver diseases and alcohol abuse: large changes in glycosylation associated with alcoholic liver disease, Clin Chim Acta 227 (1994), 69-78.
    • (1994) Clin Chim Acta , vol.227 , pp. 69-78
    • Mann, A.C.1    Record, C.O.2    Self, C.H.3    Turner, G.A.4
  • 89
    • 0031435875 scopus 로고    scopus 로고
    • An increase in the carbohydrate moiety of alpha 2-macroglobulin is associated with systemic lupus erythematosus (SLE)
    • C. Panzironi, B. Silvestrini, M.Y. Mo, R. Lahita, D. Mruk and C.Y. Cheng, An increase in the carbohydrate moiety of alpha 2-macroglobulin is associated with systemic lupus erythematosus (SLE), Biochem Mol Biol Int 43 (1997), 1305-1322.
    • (1997) Biochem Mol Biol Int , vol.43 , pp. 1305-1322
    • Panzironi, C.1    Silvestrini, B.2    Mo, M.Y.3    Lahita, R.4    Mruk, D.5    Cheng, C.Y.6
  • 90
    • 0032868788 scopus 로고    scopus 로고
    • Development of an enzyme-linked immunosorbent assay, using a monoclonal antibody against alpha2-macroglobulin, for the diagnosis of systemic lupus erythematosus
    • N. Cazzolla, L. Saso, J. Grima, M.G. Leone, E. Grippa, C.Y. Cheng and B. Silvestrini, Development of an enzyme-linked immunosorbent assay, using a monoclonal antibody against alpha2-macroglobulin, for the diagnosis of systemic lupus erythematosus, Clin Biochem 32 (1999), 249-255.
    • (1999) Clin Biochem , vol.32 , pp. 249-255
    • Cazzolla, N.1    Saso, L.2    Grima, J.3    Leone, M.G.4    Grippa, E.5    Cheng, C.Y.6    Silvestrini, B.7
  • 91
    • 0042847308 scopus 로고    scopus 로고
    • Induction of glycosylation in human C-reactive protein under different pathological conditions
    • T. Das, A.K. Sen, T. Kempf, S.R. Pramanik, C. Mandal and C. Mandal, Induction of glycosylation in human C-reactive protein under different pathological conditions, Biochem J 373 (2003), 345-355.
    • (2003) Biochem J , vol.373 , pp. 345-355
    • Das, T.1    Sen, A.K.2    Kempf, T.3    Pramanik, S.R.4    Mandal, C.5    Mandal, C.6
  • 92
    • 16644399294 scopus 로고    scopus 로고
    • Variations in binding characteristics of glycosylated human C-reactive proteins in different pathological conditions
    • T. Das, C. Mandal and C. Mandal, Variations in binding characteristics of glycosylated human C-reactive proteins in different pathological conditions, Glycoconj J 20 (2004), 537-543.
    • (2004) Glycoconj J , vol.20 , pp. 537-543
    • Das, T.1    Mandal, C.2    Mandal, C.3
  • 93
    • 0032893557 scopus 로고    scopus 로고
    • Occurrence of sialic acid s in healthy humans and different disorders
    • P. Sillanaukee, M. Ponnio and I.P. Jaaskelainen, Occurrence of sialic acid s in healthy humans and different disorders, Eur J Clin Invest 29 (1999), 413-425.
    • (1999) Eur J Clin Invest , vol.29 , pp. 413-425
    • Sillanaukee, P.1    Ponnio, M.2    Jaaskelainen, I.P.3
  • 94
    • 24044506666 scopus 로고    scopus 로고
    • Inflammation-dependent changes in alpha2,3-, alpha2,6-, and alpha2,8-sialic acid glycotopes on serum glycoproteins in mice
    • Z. Yasukawa, C. Sato and K. Kitajima, Inflammation-dependent changes in alpha2,3-, alpha2,6-, and alpha2,8-sialic acid glycotopes on serum glycoproteins in mice, Glycobiology 15 (2005), 827-837.
    • (2005) Glycobiology , vol.15 , pp. 827-837
    • Yasukawa, Z.1    Sato, C.2    Kitajima, K.3
  • 95
    • 24044534176 scopus 로고    scopus 로고
    • Increased sialylation and defucosylation of plasma proteins are early events in the acute phase response
    • M.M. Chavan, P.D. Kawle and N.G. Mehta, Increased sialylation and defucosylation of plasma proteins are early events in the acute phase response, Glycobiology 15 (2005), 838-848.
    • (2005) Glycobiology , vol.15 , pp. 838-848
    • Chavan, M.M.1    Kawle, P.D.2    Mehta, N.G.3
  • 96
    • 0032429592 scopus 로고    scopus 로고
    • Changes of glycosylation of serum proteins in psoriatic arthritis, studied by enzyme-linked lectin assay (ELLA), using concanavalin A
    • L. Saso, G. Valentini, A.M. Giardino, A. Spadaro, V. Riccieri, A. Zoppini and B. Silvestrini, Changes of glycosylation of serum proteins in psoriatic arthritis, studied by enzyme-linked lectin assay (ELLA), using concanavalin A, Biochem Mol Biol Int 46 (1998), 867-875.
    • (1998) Biochem Mol Biol Int , vol.46 , pp. 867-875
    • Saso, L.1    Valentini, G.2    Giardino, A.M.3    Spadaro, A.4    Riccieri, V.5    Zoppini, A.6    Silvestrini, B.7
  • 97
    • 0027280235 scopus 로고
    • Glycosylation of acute phase proteins and interleukins following hip arthroplasty. Inflammation parameters studied in 10 patients
    • K. Fassbender, B. Gerber, U. Karrer, M. Sobieska, A. Aeschlimann and W. Muller, Glycosylation of acute phase proteins and interleukins following hip arthroplasty. Inflammation parameters studied in 10 patients, Acta Orthop Scand 64 (1993), 216-220.
    • (1993) Acta Orthop Scand , vol.64 , pp. 216-220
    • Fassbender, K.1    Gerber, B.2    Karrer, U.3    Sobieska, M.4    Aeschlimann, A.5    Muller, W.6
  • 98
    • 34447310112 scopus 로고    scopus 로고
    • Detailed structural analysis of N-glycans released from glycoproteins in SDS-PAGE gel bands using HPLC combined with exoglycosidase array digestions
    • L. Royle, C.M. Radcliffe, R.A. Dwek and P.M. Rudd, Detailed structural analysis of N-glycans released from glycoproteins in SDS-PAGE gel bands using HPLC combined with exoglycosidase array digestions, Methods Mol Biol 347 (2006), 125-143.
    • (2006) Methods Mol Biol , vol.347 , pp. 125-143
    • Royle, L.1    Radcliffe, C.M.2    Dwek, R.A.3    Rudd, P.M.4
  • 101
    • 33645100884 scopus 로고    scopus 로고
    • Mass spectrometric approach for screening modifications of total serum N-glycome in human diseases: Application to cirrhosis
    • W. Morelle, C. Flahaut, J.C. Michalski, A. Louvet, P. Mathurin and A. Klein, Mass spectrometric approach for screening modifications of total serum N-glycome in human diseases: application to cirrhosis, Glycobiology 16 (2006), 281-293.
    • (2006) Glycobiology , vol.16 , pp. 281-293
    • Morelle, W.1    Flahaut, C.2    Michalski, J.C.3    Louvet, A.4    Mathurin, P.5    Klein, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.