Home Medicine Fucosylation of serum glycoproteins in lung cancer patients
Article
Licensed
Unlicensed Requires Authentication

Fucosylation of serum glycoproteins in lung cancer patients

  • Barbara Kossowska , Mirosława Ferens-Sieczkowska , Roman Gancarz , Ewa Passowicz-Muszyńska and Renata Jankowska
Published/Copyright: July 5, 2005

Abstract

Increased expression of sialyl Lewis X or A antigens on metastatic cancer cells leads to their selectin-mediated extravasation. Profound fucosylation of the serum microenvironment may be a factor that interrupts adhesion and influences the formation of metastases. In this study we quantitatively analyzed fucosylation of serum glycoproteins in small-cell and non-small-cell lung cancer patients. Fucosylation of four chosen glycoprotein bands was measured as the reactivity with Aleuria aurantia lectin on nitrocellulose blots, preceded by polyacrylamide gel electrophoresis. Relative fucosylation and fucosylation coefficients were calculated by densitometric analysis. Fucosylated oligosaccharides were observed in higher amounts in cancer sera when compared to sera from healthy individuals in all bands analyzed. Glycoproteins of a molecular mass of 29kDa appear to carry more fucose residues than the 42-kDa band, comprising α 1-acid glycoprotein and haptoglobin. Glycans of the 26-kDa band were fucosylated to a higher extent in non-small-cell vs. small-cell lung cancer. The results suggest that the extent of fucosylation could be a useful marker for estimation of the glycosylation status of serum proteins in cancer patients. Cluster analysis leads to the preliminary suggestion that the fucosylation status could serve as a predictive factor for patient survival.


Corresponding author: Mirosława Ferens-Sieczkowska, Department of Chemistry and Immunochemistry, Wrocław Medical University, Bujwida 44A, 51-345 Wrocław, Poland Phone: +48-71-328-2695, Fax: +48-71-328-1649,

References

1 Ørntoft TF, Vestergaard EM. Clinical aspects of altered glycosylation of glycoproteins in cancer. Electrophoresis 1999; 20: 362–71. 10.1002/(SICI)1522-2683(19990201)20:2<362::AID-ELPS362>3.0.CO;2-VSearch in Google Scholar

2 Gabius H-J, André S, Kaltner H, Siebert H-C. The sugar code: functional lectinomics. Biochim Biophys Acta 2002; 1572: 165–77. 10.1016/S0304-4165(02)00306-9Search in Google Scholar

3 O'Donnell N. Intracellular glycosylation and development. Biochim Biophys Acta 2002; 1573: 336–45. 10.1016/S0304-4165(02)00401-4Search in Google Scholar

4 Marquardt T, Denecke J. Congenital disorders of glycosylation: review of their molecular bases, clinical presentations and specific therapies. Eur J Pediatr 2003; 162: 359–79. 10.1007/s00431-002-1136-0Search in Google Scholar

5 Hakomori S. Glycosylation defining cancer malignancy: new wine in an old bottle. Proc Natl Acad Sci USA 2002; 99: 10231–3. 10.1073/pnas.172380699Search in Google Scholar

6 Lowe JB. Glycosylation, immunity and autoimmunity. Cell 2001; 104: 809–12. 10.1016/S0092-8674(01)00277-XSearch in Google Scholar

7 Miyagi T, Wada T, Yamaguchi K, Hata K. Sialidase and malignancy: a minireview. Glycoconj J 2004; 20: 189–98. 10.1023/B:GLYC.0000024250.48506.bfSearch in Google Scholar

8 Becker DJ, Lowe JB. Fucose: biosynthesis and biological functions in mammals. Glycobiology 2003; 13: 41R–53R. 10.1093/glycob/cwg054Search in Google Scholar

9 Sturla L, Rampal R, Haltiwanger RS, Fruscione F, Etzioni A, Tonetti M. Differential terminal fucosylation of N-linked glycans versus protein O-fucosylation in leukocyte adhesion deficiency type II (CDG IIc). J Biol Chem 2003; 278: 26727–33. 10.1074/jbc.M304068200Search in Google Scholar

10 Nangia-Makker P, Conklin J, Hogan V, Raz A. Carbohydrate-binding proteins in cancer, and their ligands as therapeutic agents. Trends Mol Med 2002; 8: 187–92. 10.1016/S1471-4914(02)02295-5Search in Google Scholar

11 Kannagi R, Izawa M, Koike T, Miyazaki K, Kimura N. Carbohydrate-mediated cell adhesion in cancer metastasis and angiogenesis. Cancer Sci 2004; 95: 377–84. 10.1111/j.1349-7006.2004.tb03219.xSearch in Google Scholar

12 Kannagi R. Regulatory roles of carbohydrate ligands for selectins in the homing of lymphocytes. Curr Opin Struct Biol 2002; 12: 599–608. 10.1016/S0959-440X(02)00365-2Search in Google Scholar

13 Yamazaki N, Kojima S, Bovin NV, André S, Gabius S, Gabius H-J. Endogenous lectins as targets for drug delivery. Adv Drug Deliv Rev 2000; 43: 225–44. 10.1016/S0169-409X(00)00071-5Search in Google Scholar

14 Kaila N, Thomas BE, Thakker P, Alvarez JC, Camphausen RT, Crommie D. Design and synthesis of sialyl Lewis X mimics as E-selectin inhibitors. Bioorg Med Chem Lett 2001; 11: 151–5. 10.1016/S0960-894X(00)00623-5Search in Google Scholar

15 Chervin SM, Lowe JB, Koreeda M. Synthesis and biological evaluation of a new sialyl Lewis X mimetic derived from lactose. J Org Chem 2002; 67: 5654–62. 10.1021/jo025579tSearch in Google Scholar

16 Turner GA. N-glycosylation of serum proteins in disease and its investigation using lectins. Clin Chim Acta 1992; 208: 149–71. 10.1016/0009-8981(92)90073-YSearch in Google Scholar

17 De Graaf TW, Van der Stelt ME, Anbergen MG, van Dijk W. Inflammation-induced expression of sialyl Lewis X-containing glycan structures on α 1-acid glycoprotein (orosomucoid) in human sera. J Exp Med 1993; 177: 657–66. 10.1084/jem.177.3.657Search in Google Scholar

18 Van Dijk W, Brinkman-Van der Linden EC, Havenaar EC. Glycosylation of α 1-acid glycoprotein (orosomucoid) in health and disease: occurrence, regulation and possible functional implications. Trends Glycosci Glycotechnol 1998; 10: 235–45. 10.4052/tigg.10.235Search in Google Scholar

19 Rydén I, Påhlsson P, Lundblad A, Skogh T. Fucosylation of α 1-acid glycoprotein (orosomukoid) compared with traditional biochemical markers of inflammation in recent onset rheumatoid arthritis. Clin Chim Acta 2002; 317: 221–9. 10.1016/S0009-8981(01)00803-8Search in Google Scholar

20 Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680–5. 10.1038/227680a0Search in Google Scholar PubMed

21 Merril CR, Goldman D, Sedman SA, Ebert MH. Ultrasensitive stain for proteins in polyacrylamide gels show variation in cerebrospinal fluid proteins. Science 1981; 211: 1437–8. 10.1126/science.6162199Search in Google Scholar

22 Towbin H, Stachelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 1979; 76: 4350–3. 10.1073/pnas.76.9.4350Search in Google Scholar

23 Yamashita K, Kochibe N, Ohkura T, Ueda I, Kobata A. Fractionation of L-fucose containing oligosaccharides on immobilized Aleuria aurantia lectin. J Biol Chem 1985; 260: 4688–93. 10.1016/S0021-9258(18)89125-6Search in Google Scholar

24 Rydén I, Lundblad A, Påhlsson P. Lectin ELISA for analysis of α 1-acid glycoprotein fucosylation in the acute phase response. Clin Chem 1999; 45: 2010–2. 10.1093/clinchem/45.11.2010Search in Google Scholar

25 Strouf O. Chemical pattern recognition. Letchworth: Research Studies Press, 1986. Search in Google Scholar

26 Borsig L, Wong R, Hynes RO, Varki NM, Varki A. Synergistic effects of L- and P-selectin in facilitating tumor metastasis can involve non-mucin ligands and implicate leukocytes as enhancers of metastasis. Proc Natl Acad Sci USA 2002; 99: 2193–8. 10.1073/pnas.261704098Search in Google Scholar

27 Okuno K, Kawai I, Hirai N, Narimatsu H, Yasutomi M. Role of sialyl Lewis X in liver metastasis in view of liver-associated immunity. Hepatogastroenterology 2003; 50: 756–60. Search in Google Scholar

28 Zipin A, Israeli-Amit M, Meshel T, Sagi-Assif O, Yron I, Lifshitz V, et al. Tumor-microenvironment interactions: the fucose-generating FX enzyme controls adhesive properties of colorectal cancer cells. Cancer Res 2004; 64: 6571–8. 10.1158/0008-5472.CAN-03-4038Search in Google Scholar

29 Brown JR, Fuster MM, Whisenant T, Esko JD. Expression patterns of α2,3-sialyltransferase and α1,3-fucosyltransferase determine the mode of sialyl Lewis X inhibition by disaccharide decoys. J Biol Chem 2003; 278: 23352–9. 10.1074/jbc.M303093200Search in Google Scholar

30 Kim YJ, Varki A. Perspectives on the significance of altered glycosylation of glycoproteins in cancer. Glycoconj J 1997; 14: 569–76. 10.1023/A:1018580324971Search in Google Scholar

31 Nakagoe T, Sawai T, Tsuji T, Jibiki M-A, Nanashima A, Yamaguchi H, et al. Predictive factors for preoperative serum levels of sialyl Lewis X, sialyl Lewis A and sialyl Tn antigens in gastric cancer patients. Anticancer Res 2002; 22: 451–8. Search in Google Scholar

32 Sumikura S, Ishigami S, Natsugoe S, Miyazono F, Tokuda K, Nakajo A, et al. Disseminated cancer cells in the blood and expression of sialylated antigen in gastric cancer. Cancer Lett 2003; 200: 77–83. 10.1016/S0304-3835(03)00388-4Search in Google Scholar

33 Dargan E, Thompson S, Cantwell MJ, Wilson RG, Turner GA. Changes in the fucose content of haptoglobin in breast and ovarian cancer: association with disease progression. Glycosyl Disease 1994; 1: 37–43. 10.1007/BF00917467Search in Google Scholar

34 Otake Y, Fujimoto I, Tanaka F, Nakagawa T, Ikeda T, Menon KK, et al. Isolation and characterization of an N-linked oligosaccharide that is significantly increased in sera from patients with non-small cell lung cancer. J Biochem 2001; 129: 537–42. 10.1093/oxfordjournals.jbchem.a002888Search in Google Scholar PubMed

35 Satoh H, Ishikawa H, Kamma H, Yamashita YT, Takahashi H, Ohtsuka M, et al. Serum sialyl Lewis X-I antigen levels in non-small cell lung cancer: correlation with distant metastasis and survival. Clin Cancer Res 1997; 3: 495–9. Search in Google Scholar

36 Satoh H, Ishikawa H, Yamashita YT, Ohtsuka M, Sekizawa K. Serum sialyl Lewis X-i antigen in lung adenocarcinoma and idiopathic pulmonary fibrosis. Thorax 2002; 57: 263–6. 10.1136/thorax.57.3.263Search in Google Scholar PubMed PubMed Central

37 Binz PA, Hochstrasser DF, Appel RD. Mass spectrometry-based proteomics: current status and potential use in clinical chemistry. Clin Chem Lab Med 2003; 41: 1540–51. 10.1515/CCLM.2003.237Search in Google Scholar PubMed

38 Clarke W, Zhang Z, Chan DW. The application of clinical proteomics to cancer and other diseases. Clin Chem Lab Med 2003; 41: 1562–70. 10.1515/CCLM.2003.239Search in Google Scholar PubMed

39 Moldway J, Scheid P, Wild P, Nabil K, Siat j, Borrelly J, et al. Predictive survival markers in patients with surgically resected non-small cell lung carcinoma. Clin Cancer Res 2000; 6: 1125–34. Search in Google Scholar

40 Trapé J, Buxo J, de Olaguer JP, Vidal C. Tumor markers as prognostic factors in treated non-small cell lung cancer. Anticancer Res 2003; 23: 4277–82. Search in Google Scholar

Received: 2004-12-11
Accepted: 2005-2-4
Published Online: 2005-7-5
Published in Print: 2005-4-1

© by Walter de Gruyter Berlin New York

Articles in the same Issue

  1. Autoantibodies against intrinsic factor (IF) measured with an ELISA using recombinant human IF as both catching and detecting reagent
  2. Antibody titer against malondialdehyde-modified LDL compares with HDL cholesterol concentration in identifying angiographically verified coronary artery disease. Comparison of tests by ROC analysis
  3. Fucosylation of serum glycoproteins in lung cancer patients
  4. Association of cytochrome P450 2E1 genetic polymorphisms with squamous cell carcinoma of the oesophagus
  5. α-Tocopherol as an antiretroviral therapy supplement for HIV-1-infected patients for increased lymphocyte viability
  6. The effect of antioxidant supplementation on superoxide dismutase activity, Cu and Zn levels, and total antioxidant status in erythrocytes of patients with Graves' disease
  7. Concentrations of calcium, copper, iron, magnesium, potassium, sodium and zinc in adult female hair with different body mass indexes in Taiwan
  8. Estimation of the limit of detection with a bootstrap-derived standard error by a partly non-parametric approach. Application to HPLC drug assays
  9. Pitfall in the high-throughput quantification of whole blood cyclosporin A using liquid chromatography-tandem mass spectrometry
  10. How accurate are clinical activity indices for scoring of disease activity in inflammatory bowel disease (IBD)?
  11. An iterative method for improved estimation of the mean of peer-group distributions in proficiency testing
  12. Impact of a common CV evaluation scheme on overall laboratory performance: 8-year experience of a large national proficiency testing program in Japan
  13. Significance of small dense low-density lipoproteins as coronary risk factor in diabetic and non-diabetic Korean populations
  14. Evaluation of a rapid bedside test for the quantitative determination of C-reactive protein
  15. Power function of the reference change value in relation to cut-off points, reference intervals and index of individuality
  16. Erythrocyte ferritin concentration: analytical performance of the immunoenzymatic IMx-Ferritin (Abbott) assay
  17. Vitamin C and aberrant electrolyte results
  18. POX-ACT assay and d-ROMs test: comparison impossible
  19. A spectrophotometric micromethod for determining erythrocyte protoporphyrin-IX in whole blood or erythrocytes
Downloaded on 30.12.2025 from https://www.degruyterbrill.com/document/doi/10.1515/CCLM.2005.066/html
Scroll to top button