• 1
    Van Dijk W, Havenaar EC, Brinkman-van der Linden ECM. Alpha1-acid glycoprotein (orosomucoid): pathophysiological changes in glycosylation in relation to its function. Glycoconjugate J. 1995; 12: 227233.
  • 2
    Chiu KM, Mortensen RF, Osmand AP, Gewurz, H. Interaction of α1-acid glycoprotein with the immune system. I. Purification and effects upon lymphocytes responsiveness. Immunology. 1977; 32: 9971005.
  • 3
    Kremer JMH, Wilting J, Janssen LHM. Drug binding to human α1-acid glycoprotein in health and disease. Pharmacol Rev. 1988; 40: 147.
  • 4
    Libert C, Brouckart P, Fiers W. Protection by α1-acid glycoprotein against tumor necrosis factor-induced lethality. J Exp Med. 1994; 180: 17511775.
  • 5
    Fournier T, Medjoubi-N N, Porquet D. Alpha-1-acid glycoprotein. Biochim Biophys Acta. 2000; 1482: 157171.
  • 6
    Hansen JE, Larsen VA, Bøg-Hansen TC. The microheterogeneity of alpha 1-acid glycoprotein in inflammatory lung disease, cancer of the ling and normal health. Clin Chim Acta. 1984; 138: 4147.
  • 7
    Bories PN, Feger J, Benbernou N, Rouzeau JD, Agneray J, Durand G. Prevalence of tri- and tetraantennary glycans of human alpha 1-acid glycoprotein in release of macrophage inhibitor of interleukin-1 activity. Inflammation. 1990; 14: 315323.
  • 8
    Hrycaj P, Sobieska M, Mackiewicz S, Muller W. Microheterogeneity of alpha 1-acid glycoprotein in early and established rheumatoid arthritis. J Rheumatol. 1993; 20: 20202024.
  • 9
    Mackiewicz A, Mackiewicz K. Glycoforms of serum alpha 1-acid glycoprotein as markers of inflammation and cancer. Glycoconjugate J. 1995; 12: 241247.
  • 10
    Brinkman-Van der Linden ECM, Havenaar EC, Van Ommen ECR, Van Kamp GJ, Gooren LJG, Van Dijk W. Oral estrogen treatment induces a decrease in expression of sialyl Lewisx on α1-acid glycoprotein in females and male-to-female transsexuals. Glycobiology. 1996; 6: 407412.
  • 11
    Shiyan SD, Bovin NV. Carbohydrate composition and immunomodulator activity of different glycoforms of alpha 1-acid glycoprotein. Glycoconjugate J. 1997; 14: 631638.
  • 12
    Zimmermann-Belsing T, Feldt-Rasmussen U, From G, Perrild H, Bøg-Hansen TC. Long-term pathologic changes of α1-acid glycoprotein (orosomucoid) glycoforms in autoimmune thyroid disease. Autoimmunity. 2002; 35: 441447.
  • 13
    De Graaf TW, Van der Stelt ME, Anbergen MG, Van Dijk W. Inflammation-induced expression of sialyl Lewis X-containing glycan structures on α1-acid glycoprotein (orosomucoid) in human sera. J Exp Med. 1993; 177: 657666.
  • 14
    Turunen JP, Majuri ML, Seppo A, et al. De novo expression of endothelial sialyl Lewisa and sialyl Lewisx during cardiac transplant rejection: superior capacity of a tetravalent sialyl Lewisx oligosaccharide in inhibiting L-selectin-dependent lymphocyte adhesion. J Exp Med. 1995; 182: 11331141.
  • 15
    Rydén I, Skude G, Lundblad A, Påhlsson P. Glycosylation of α1-acid glycoprotein in inflammatory disease: analysis by high pH anion-exchange chromatography and concanavalin A crossed affinity immunoelectrophoresis. Glycoconjugate J. 1997; 14: 481488.
  • 16
    Havenaar EC, Axford JS, Brinkman-Van der Linden ECM, et al. Severe rheumatoid arthritis prohibits the pregnancy-induced decrease in α3-fucosylation of α1-acid glycoprotein. Glycoconjugate J. 1998; 15: 723729.
  • 17
    Jorgensen HG, Elliott MA, Priest R, Smith KD. Modulation of sialyl Lewis X dependent binding to E-selectin by glycoforms of alpha-1-acid glycoprotein expressed in rheumatoid arthritis. Biomed Chromatogr. 1998; 12: 343349.
  • 18
    Van Dijk W, Koeleman C, Van het Hof B, Poland, D, Jakobs C, Jaeken J. Increased α3-fucosylation of α1-acid glycoprotein in patients with congenital disorder of glycosylation type IA (CDG-Ia). FEBS Lett. 2001; 494: 232235.
  • 19
    Bøg-Hansen TC. Crossed immunoaffinoelectrophoresis: an analytical method to predict the result of affinity chromatography. Anal Biochem. 1973; 56: 480488.
  • 20
    Heegaard PMH, Heegaad NHH, Bøg-Hansen TC. Affinity electrophoresis for the characterization of glycoproteins-the use of lectins in combination with immunoelectrophoresis. In: BereborowiczJ, MackiewiczA. editors. Affinity electrophoresis: principles and application. Boca Raton: CRC Press, 1992: 321.
  • 21
    Rydén I, Lundblad A, Påhlsson P. Lectin ELISA for analysis of α1-acid glycoprotein fucosylation in the acute phase response. Clin Chem. 1999; 45: 20102012.
  • 22
    Kakehi K, Kinoshita M, Kawakami D, et al. Capillary electrophoresis of sialic acid-containing glycoprotein. Effect of the heterogeneity of carbohydrate chains on glycoform separation using an α1-acid glycoprotein as a model. Anal Chem. 2001; 73: 26402647.
  • 23
    Liljeblad M, Rydén I, Ohlson S, Lundblad A, Påhlsson P. A lectin immunosensor technique for determination of α1-acid glycoprotein fucosylation. Anal Biochem. 2001; 288: 216224.
  • 24
    Bierhuizen MFA, De Wit M, Govers CARL, et al. Glycosylation of three molecular forms of human α1-acid glycoprotein having different interactions with concanavalin A. Variations in the occurrence of di-, tri-, and tetra-antennary glycans and the degree of sialylation. Eur J Biochem. 1988; 175: 387394.
  • 25
    Kochibe N, Furukawa K. Purification and properties of a novel fucose-specific hemagglutinin of Aleuria aurantia. Biochemistry. 1980; 19: 28412846.
  • 26
    Yazawa S, Madiyalakan R, Izawa H, Asao T, Furukawa K, Matta KL. Cancer-associated elevation of α(1-3)-L-fucosyltransferase activity in human serum. Cancer. 1988; 62: 516520.
  • 27
    Yazawa S, Asao T, Nagamachi Y, Abbas SA, Matta KL. Tumor-related elevation of serum (α1-3)-L-fucosyltransferase activity in gastric cancer. J Cancer Res Clin Oncol. 1989; 115: 451455.
  • 28
    Asao T, Yazawa S, Nagamachi Y, Abbas SA, Matta KL. Serum α(1-3)-L-fucosyltransferase, carcinoembryonic antigen and sialyl Lewis X-i antigen levels in lung cancer. Cancer. 1989; 64: 133137.
  • 29
    Yazawa S, Asao T, Nagamachi Y, Matta KL. Elevated activity of serum α(1-3)-L-fucosyltransferase in human cancer. J Tumor Marker Oncol. 1990; 4: 355362.
  • 30
    Brinkman-Van der Linden ECM, Mollicone R, Oriol R, Larson G, Van den Eijinden, DH, Van Dijk W. A missense mutation in the FUT6 gene results in total absence of α3-fucosylation of human α1-acid glycoprotein. J Biol Chem. 1996; 271: 1449214495.
  • 31
    Yazawa S, Tanaka S, Nishimura T, Miyanaga K, Kochibe N. Plasma α1,3-fucosyltransferase deficiency in schizophrenia. Exp Clin Immunogenet. 1999; 16: 125130.
  • 32
    Tanaka S, Yazawa S, Noguchi K, et al. Molecular analysis of plasma α1,3-fucosyltransferase deficiency and development of the methods for its genotyping. Exp Clin Immunogenet. 2001; 18: 112.
  • 33
    Asao T, Kuwano H, Nakamura J, et al. Tumor cells as the origin of elevated serum α1,3fucosyltransferase in association with malignancy. Clin Exp Metast. 2001; 18: 605610.
  • 34
    Rydén I, Påhlsson P, Lindgren S. Diagnostic accuracy of α1-acid glycoprotein fucosylation for liver cirrhosis in patients undergoing hepatic biopsy. Clin Chem. 2002; 48: 21952201.
  • 35
    Rydén I, Påhlsson P, Lundblad A, Skogh T. Fucosylation of α1-acid glycoprotein (orosomucoid) compared with traditional biochemical markers of inflammation in recent onset rheumatoid arthritis. Clin Chim Acta. 2002; 317: 22192229.
  • 36
    Tachikawa T, Yazawa S, Asao T, Shin S, Yanaihara N. Novel method for quantifying α(1-3)-L-fucosyltransferase activity in serum. Clin Chem. 1991; 37: 20812086.
  • 37
    Hakomori S. Aberrant glycosylation in cancer cell membranes as focused on glycolipids: overview and perspectives. Cancer Res. 1985; 45: 24052414.
  • 38
    Le Pendu J, Marionneau S, Cailleau-Thomas A, Rocher J, Le Moullac-Vaidye B, Clément M. ABH and Lewis histo-blood group antigens in cancer. APMIS. 2001; 109: 931.
  • 39
    Yazawa S, Asao T, Izawa H, Miyamoto Y, Matta KL. The presence of CA19-9 in serum and saliva from Lewis blood-group negative cancer patients. Jpn J Cancer Res. 1988; 79: 538543.
  • 40
    Yazawa S, Akamatsu S, Tachikawa T, et al. Development and characterization of a novel anti-fucosylated antigen monoclonal antibody YB-2 and its usefulness in the immunohistochemical diagnosis of colorectal cancer. Jpn J Cancer Res. 1993; 84: 641648.
  • 41
    Akamatsu S, Yazawa S, Zenita K, Matsumoto H, Tachikawa T, Kannagi R. Elevation of an α(1,3)fucosyltransferase activity correlated with apoptosis in the human colon adenocarcinoma cell line, HT-29. Glycoconjugate J. 1996; 13: 10211029.
  • 42
    Yazawa S, Kochibe N, Nishimura T, et al. A novel method for determination of α1,6fucosyltransferase activity using a reducing oligosaccharide from egg yolk as a specific acceptor. Glycoconjugate J. 1998; 15: 863871.
  • 43
    Yazawa S, Nishimura T, Ide M, et al. Tumor-related expression of α1,2fucosylated antigens on colorectal carcinoma cells and its suppression by cell-mediated priming using sugar acceptors for α1,2fucosyltransferase. Glycobiology. 2002; 12: 545553.
  • 44
    Kushner I, Mackiewicz A. Acute phase proteins. In: MackiewiczA, KushmerI, BaumannH, editors. Molecular biology, biochemistry and clinical applications. Boca Raton: CRC Press, 1993: 419.
  • 45
    Hansen JE, Iversen J, Lihme A, Bøg-Hansen TC. Acute phase reaction, heterogeneity, and microheterogeneity of serum proteins as nonspecific tumor markers in lung cancer. Cancer. 1987; 60: 16301635.
  • 46
    Dobryszycka W, Katnik I. Interaction of haptoglobin with concanavalin A and wheat germ agglutinin: basis research and clinical applications. In: Breborowicz, J, Mackiewicz, A, editors. Affinity electrophoresis: principles and application. Boca Raton: CRC Press, 1992: 211225.
  • 47
    Van Dijk W, Brinkman-Vander Linden ECM, Navenaar EC. Glycosylation of α1-acid glycoprotein (orosomucoid) in healthy and disease: occurrence, regulation and possible functional implications. TIGG. 1998; 10: 235245.
  • 48
    Fournet B, Montreuil J, Strecker G, et al. Determination of the primary structures of 16 asialo-carbohydrate units derived from human plasma α1-acid glycoprotein by 360-MHz 1H NMR spectroscopy and permethylation analysis. Biochemistry. 1978; 17: 52065214.
  • 49
    Yazawa S, Nakamura J, Asao T, et al. Aberrant α1-2 fucosyltransferases found in human colorectal carcinoma involved in the accumulation of Leb and Y antigens in colorectal tumors. Jpn J Cancer Res. 1993; 84: 989995.
  • 50
    Yoshima H, Matsumoto A, Mizuochi T, Kawasaki T, Kobata A. Comparative study of the carbohydrate moieties of rat and human α1-acid glycoproteins. J Biol Chem. 1981; 256: 84768484.