Microheterogeneity of serum transferrin in the diagnosis of hepatocellular carcinoma

Journal of Gastroenterology and Hepatology (Australia)

Volumn 11, Issue 4, 1996, Pages 358-365

  Suzuki, Y ^a   Aoyagi, Y ^a   Mori, S ^a   Suda, T ^a   Naitoh, A ^a   Isokawa, O ^a   Yanagi, M ^a   Igarashi, H ^a   Asakura, H ^a  

^a NIIGATA UNIVERSITY   (Japan)

Author keywords

alpha fetoprotein; concanavalin A; crossed immunoaffinity electrophoresis; hepatocellular carcinoma; Lens culinaris agglutinin; liver cirrhosis; transferrin

Indexed keywords

CONCANAVALIN A; LECTIN; TRANSFERRIN;

ADULT; AGED; ARTICLE; CLINICAL TRIAL; CONTROLLED CLINICAL TRIAL; CONTROLLED STUDY; CROSSED IMMUNOELECTROPHORESIS; FEMALE; HUMAN; LIVER CELL CARCINOMA; LIVER CIRRHOSIS; MAJOR CLINICAL STUDY; MALE; MEASUREMENT; PRIORITY JOURNAL; PROTEIN STRUCTURE;

EID: 0029927626     PISSN: 08159319     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1440-1746.1996.tb01384.x     Document Type: Article

References (34)

1. 1 Aisen P., Listowsky I. Iron transport and storage proteins. In: Snell EE, Boyer PD, Meister A., Richardson CC, eds. Annual Review of Biochemistry, vol. 49. Palo Alto: Annual Reviews Inc. 1980 ; 357–93.
2. 2 Meliconi R., Parracino O., Facchini A. et al. Acute phase proteins in chronic and malignant liver diseases. Liver 1988 ; 8: 65–74.
3. 3 MacGilliray RTA, Mendez E., Shewale JG, Sinha SK, Lineback‐Zins J., Brew K. The primary structure of human serum transferrin. J. Biol. Chem. 1983 ; 258: 3543–53.
4. 4 Spik G., Bayard B., Fournet B., Strecker G., Bouquelet S., Montreuil J. Studies on glycoconjugates LXIV complete structure of two carbohydrate units of human serotransferrin. FEBS Lett. 1975 ; 50: 296–9.
5. 5 Yamashita K., Koide N., Endo T., Iwaki Y., Kobata A. Altered glycosylation of serum transferrin of patients with hepatocellular carcinoma. J. Biol. Chem. 1989 ; 264: 2415–23.
6. 6 Poupon RE, Papoz L., Sarmini H., Elinck R. A study of the microheterogeneity of transferrin in cirrhotic patients. Clin. Chim. Acta 1985 ; 151: 245–51.
7. 7 Matsumoto K., Maeda Y., Kato S., Yuki H. Alteration of asparagine‐linked glycosylation in serum transferrin of patients with hepatocellular carcinoma. Clin. Chim. Acta 1994 ; 224: 1–8.
8. 8 Aoyagi Y., Suzuki Y., Isemura M. et al. Differential reactivity of alpha‐fetoprotein with lectins and evaluation of its usefulness in the diagnosis of hepatocellular carcinoma. Gann 1984 ; 75: 809–15.
9. 9 Aoyagi Y., Isemura M., Yosizawa Z. et al. Fucosylation of serum alpha‐fetoprotein in patients with primary hepatocellular carcinoma. Biochim. Biophys. Acta 1985 ; 830: 217–23.
10. 10 Aoyagi Y., Suzuki Y., Isemura M. et al. The fucosylation index of alpha‐fetoprotein and its usefulness in the early diagnosis of hepatocellular carcinoma. Cancer 1988 ; 61: 769–74.
11. 11 Aoyagi Y., Suzuki Y., Igarashi K. et al. The usefulness of simultaneous determinations of glucosaminylation and fucosylation indices of alpha‐fetoprotein in the differential diagnosis of neoplastic diseases of the liver. Cancer 1991 ; 67: 2390–4.
12. 12 Suzuki Y., Aoyagi Y., Muramatsu M., Sekine C., Isemura M., Ichida F. Close topographical relationship in alpha fetoprotein (AFP) between a Lens culinaris binding glycan and the epitope recognized by AFP‐reactive monoclonal antibody, 18H4. Br. J. Cancer 1987 ; 55: 147–52.
13. 13 Suzuki Y., Aoyagi Y., Muramatsu M. et al. A lectin‐based monoclonal enzyme immunoassay to distinguish fucosylated and non‐fucosylated alpha‐fetoprotein molecular variants. Ann. Clin. Biochem. 1990 ; 27: 121–8.
14. 14 Sekine C., Aoyagi Y., Suzuki Y., Ichida F. The reactivity of alpha‐1–antitrypsin with Lens culinaris agglutinin and its usefulness in the diagnosis of neoplastic diseases of the liver. Br. J. Cancer 1987 ; 56: 371–5.
15. 15 Kornfeld K., Reitman ML, Kornfeld R. The carbohydrate‐specificity of pea and lentil lectins. J. Bio. Chem. 1981 ; 256: 6633–40.
16. 16 Saitoh A., Aoyagi Y., Asakura H. Structural analysis on the sugar chains of human alpha‐1–antitrypsin: Presence of fucosylated biantennary glycan in hepatocellular carcinoma. Arch. Biochem. Biophys. 1993 ; 303: 281–7.
17. 17 Bog‐Hansen T‐C. Crossed immuno‐affinoelectro‐phoresis: An analytical method to predict the results of affinity chromatography. Anal. Biochem. 1973 ; 56: 480–8.
18. 18 Aoyagi Y., Saitoh A., Suzuki Y. et al. Fucosylation index of alpha‐fetoprotein: A possible aid in the early recognition of hepatocellular carcinoma in patients with cirrhosis. Hepatology 1993 ; 17: 50–2.
19. 19 Aoyagi Y., Suzuki Y., Igarashi K. et al. Carbohydrate structures of human alpha‐fetoprotein of patients with hepatocellular carcinoma: Presence of fucosylated and non‐fucosylated triantennary glycans. Br. J. Cancer 1993 ; 67: 486–92.
20. 20 Baezinger JU, Fiete D. Structural determinations of concanavalin A specificity for oligosaccharides. J. Biol. Chem. 1979 ; 254: 2400–7.
21. 21 Turner GA. N ‐Glycosylation of serum proteins in disease and its investigation using lectins. Clin. Chim. Acta 1992 ; 208: 149–71.
22. 22 Campion B., Leger D., Wieruszeski J‐M, Montreuil J., Spik G. Presence of fucosylated triantennary, tetraantennary and pentaantennary glycans in transferrin synthesized by the human hepatocarcinoma cell line Hep G2. Eur. J. Biochem. 1989 ; 184: 405–13.
23. 23 Heegaard NHH, Hagerup M., Thomsen AC, Heegaard PMH. Concanavalin A crossed affinity immunoelectro‐phoresis and image analysis for semi‐quantitative evaluation of microheterogeneity profiles of human serum transferrin from alcoholics and normal individuals. Electrophoresis 1989 ; 10: 836–40.
24. 24 Spik G., Debruyne V., Montreuil J. Alterations of the carbohydrate structure of human serotransferun in liver diseases. In: Popper H., Reutter W., Kottgen E., Gudat F., eds. Structural Carbohydrates in the Liver. Basel: MTP Press Limited, 1983 ; 477–83.
25. 25 Spik G., Debruyne V., Montreuil J., Van Halbeek H., Vliegenthart J‐FG. Primary structure of two sialylated triantennary glycans from human serotransferrin. FEBS Lett. 1985 ; 183: 65–9.
26. 26 Leger D., Campion B., Decottignies J‐P, Montreuil J., Spik G. Physiological significance of the marked increased branching of the glycans of human serotransferrin during pregnancy. Biochem. J. 1989 ; 257: 231–8.
27. 27 Kobata A. Structural changes induced in the sugar chains of glycoproteins by malignant transformation of producing cells and their clinical application. Biochimie 1988 ; 70: 1575–85.
28. 28 Hahn TJ, Goochee CF. Growth‐associated glycosylation of transferrin secreted by Hep G2 cells. J. Biol. Chem. 1992 ; 267: 23 982–7.
29. 29 Saito H., Nishikawa A., Gu J. et al. cDNA cloning and chromosomal mapping of human N ‐acetylglucosaminyl‐transferase V +. Biochem. Biophys. Res. Commun. 1994 ; 198: 318–27.
30. 30 Hutchinson WL, Du M‐Q, Johnson PJ, Williams R. Fucosyltransferase: Differential plasma and tissue alterations in hepatocellular carcinoma and cirrhosis. Hepatology 1991 ; 13: 683–8.
31. 31 Hahn TJ, Goochee CF. Removal of the artifactual peak associated with concanavalin A crossed affinoimmuno‐electrophoresis. Anal. Biochem. 1991 ; 199: 243–8.
32. 32 Koj A., Dubin A., Kasperczyk H., Bereta J., Gordon AH. Changes in the blood level and affinity to concanavalin A of rat plasma glycoproteins during acute inflammation and hepatoma growth. Biochem. J. 1982 ; 206: 545–53.
33. 33 Nicollet I., Lebreton J‐P, Fontaine M., Hiron M. Evidence of alpha‐1–acid glycoprotein populations of different pI values after concanavalin A affinity chromatography. Biochim. Biophys. Acta 1981 ; 668: 235–45.
34. 34 Vaughan L., Lorier MA, Carrel RW. Alpha‐antitrypsin microheterogeneity. Isolation and physiological significance of isoforms. Biochim. Biophys. Acta 1982 ; 701: 339–45.