Comparison of PSA Binding for Prostate Cancer and BPH Using Lectin-Glycoprotein Interactions

Year 2015, Volume: 43 Issue: 3, 205 - 211, 01.09.2015

Neslihan Idil Işık Perçin Önder Kara Burhan Özdemir Nilüfer Aksöz

Abstract

The increased amount of Prostate-specific antigen PSA binding capacity is estimated to be associated with the initial concentration of PSA in the serum or cancer-related glycosylation patterns. The aim of this study was to determine tPSA and fPSA binding capacities of mPGMA-HDMA-Con A beads using the serum samples of patients with PCa and BPH having the same concentration of tPSA. Concanavalin A Con A is preferred to use as ligand due to the high sugar specificity towards mannose. The initial concentration of the Con A in the medium was changed between 0.25 and 2.5 mg/mL in order to determine the optimum amount of Con A immobilized to the beads. Both tPSA and fPSA adsorption capacity of mPGMA-HDMA-ConA beads performed using the serum sample of patient with BPH were found to be higher than that of PCa. Therefore, the reason of high PSA adsorption capacity observed in patients with BPH could be attribute to the glycosylation changes.

Keywords

Prostate cancer, prostate specific antigen, Concanavalin A, Magnetic Beads

Prostat Kanseri için Lektin-Glikoprotein Etkileşimlerini Kullanarak PSA ve BPH Bağlanmalarının Karşılaştırılması

Abstract

P rostat-spesifik antijen PSA bağlanma kapasitesindeki artışın başlangıçta serumda bulunan PSA derişimi ya da kansere bağlı değişen glikozilasyon paternleri ile ilişkili olduğu öngörülmektedir. Bu çalışmada, aynı tPSA derişimine sahip PCa ve BPH’lı hastaların serum örnekleri kullanılarak mPGMA-HDMA-ConA mikrokürelere tPSA ve fPSA bağlanma kapasitesinin belirlenmesi amaçlanmıştır. Concanavalin A Con A mannoza karşı özgüllük göstermesi nedeniyle ligand olarak kullanılması tercih edilmiştir. mPGMA mikrokürelere immobilize olan optimum Con A miktarını belirlemek amacıyla ortamdaki Con A miktarı 0.25-2.5 mg/ml arasında değiştirilmiştir. Hem tPSA hem de fPSA için mPGMA-HDMA-ConA mikrokürelerin bağlanma kapasitesinin PCa ile kıyaslandığında BPH’da daha fazla olduğu gösterilmiştir. Böylece, yüksek PSA bağlanma kapasitesinin kansere bağlı değişen glikozilasyondan kaynaklandığı doğrulanmıştır

Keywords

Prostate kanseri, prostat spesifik antijen, konkanavalin A, manyetik mikroküreler

References

• Table 2. The first- and second-order kinetic constants for BPH. Table 3. Overview of lectin-based researches associated with PCa and BPH. D.L. Meany, Z. Zhang, L.J. Sokoll, H. Zhang, D.W. Chan, Glycoproteomics for prostate cancer detection: changes in serum PSA glycosylation patterns, J. Proteome Res., 8 (2009) 613.
• H.A. Badr, D.M. Alsadek, A.A. Darwish, A.I. Elsayed, B.O. Bekmanov, E.M. Khussainova, X. Zhang, W.C. Cho, L.B. Djansugurova, C.Z. Li, Lectin approaches for glycoproteomics in FDA-approved cancer biomarkers. Expert Rev. Proteomics, 11 (2014) 227.
• J.J. Jayapalan, K.L. Ng, A.H. Razack, O.H. Hashim, Identification of potential complementary serum biomarkers to differentiate prostate cancer from benign prostatic hyperplasia using gel- and lectin- based proteomics analyses., Electrophoresis, 33 (2012) 1855.
• C. Fania, I. Sogno, M. Vasso, E. Torretta, R. Leone, A. Bruno, P. Consonni, A. Albini, C. Gelfi, A PSA- guided approach for a better diagnosis of prostatic adenocarcinoma based on MALDI profiling and peptide identification, Clin. Chim. Acta, 439 (2015) 42.
• T. Vermassen, C. Van Praet, D. Vanderschaeghe, et al., Capillary electrophoresis of urinary prostate glycoproteins assists in the diagnosis of prostate cancer, Electrophoresis, 35 (2014) 1017.
• S. Fanayan, M. Hincapie, W.S. Hancock, Using lectins to harvest the plasma/serum glycoproteome. Electrophoresis, 33 (2012) 1746.
• C. Babaç, H. Yavuz, I.Y. Galaev, E. Pişkin, A. Denizli, Binding of antibodies to concanavalin A-modified monolithic cryogel, React. Funct. Polym., 66 (2006)
• C. Altunbaş, M. Uygun, D.A. Uygun, S. Akgöl, A. Denizli, Immobilization of Inulinase on Concanavalin A-Attached Super Macroporous Cryogel for 18. N.I. Govorukhina, A. Keizer-Gunnink, A.G.J. van der Production of High-Fructose Syrup, Appl. Biochem. Biotechnol., 170 (2013) 1909.
• E.B. Altintas, N. Tuzmen, N. Candan, A. Denizli, Use of magnetic poly(glycidyl methacrylate) monosize beads for the purification of lysozyme in batch system, J. Chromatogr. B., 853 (2007) 105.
• R. Massart, Preparation of aqueous magnetic liquids in alkaline and acidic media, IEEE Trans. Magn., 17 (1981) 1247.
• D. Horák, N.Benedyk, Magnetic poly(glycidyl methacrylate) microspheres prepared by dispersion polymerization in the presence of electrostatically stabilized ferrofluids. J. Polym. Sci. A Polym. Chem., (2004) 5827.
• M. Andaç, I. Galaev, A. Denizli, Dye attached poly(hydroxyethyl methacrylate) cryogel for albumin depletion from human serum, J. Sep. Sci., 35 (2012)
• L. Urbas, P. Brne, B. Gabor, M. Barut, M. Strlic, T.C. Petric, A. Strancar, Depletion of high-abundance proteins from human plasma using a combination of an affinity and pseudo-affinity column, J. Chromatogr. A., 1216 (2009) 2689.
• J. Zhang, Z. Zhang, Y. Song, H. Cai, Bovine serum albumin (BSA) adsorption with Cibacron Blue F3GA attached chitosan microspheres, React. Funct. Polym., (2006) 916.
• J. Gu, Z. Lei, Y. Qizhi, Novel Method for Human Serum Albumin Adsorption/Separation From Aqueous Solutions and Human Plasma With Cibacron Blue F3GA-Zn(II) Attached Microporous Affinity Membranous Capillaries, J. Membr. Sci. 287 (2007)
• E.B. Altıntaş, A. Denizli, Efficient Removal of Albumin from Human Serum by Monosize Dye Affinity Beads, Journal of Chromatography B, 832 (2006) 216.
• A. Denizli, Preparation of immuno-affinity membranes for cholesterol removal from human plasma, J. Chromatogr. B., 772 (2002) 357.
• Zee, S. de Jong, H.W.A. de Bruijn, R. Bischoff, Sample preparation of human serum for the analysis of tumormarkers: a comparision of different approches for albumin and γ-globulin-depletion, J. Chromatogr. A, 1009 (2003) 171.
• L. Uzun, C. Armutcu, Ö. Biçen, A. Ersöz, R. Say, A. Denizli, Simultaneous depletion of immunoglobulin G and albumin from human plasma using novel monolithic cryogel columns, Colloids Surfaces, B Biointerfaces., 1 (2013) 1.
• P.S. Basu, M. Ramdhan, S.K Batabyal, Lectin and serum– PSA interaction as a screening test for prostate cancer, Clin. Biochem., 36 (2003 )373.
• M.V. Dwek, A. Jenks, A.J. Leathem, A sensitive assay to measure biomarker glycosylation demonstrates increased fucosylation of prostate specific antigen (PSA) in patients with prostate cancer compared with benign prostatic hyperplasia, Clin. Chim. Acta., 14 (2010) 1935.
• C. Ohyama, M. Hosono, K. Nitta, M. Oh-eda, K. Yoshikawa, T. Habuchi, Y. Arai, M. Fukuda, Carbohydrate structure and differential binding of prostate specific antigen to Maackia amurensis lectin between prostate cancer and benign prostate hypertrophy, Glycobiology, 14 (2004) 671.
• K. Fukushima, T. Satoh, S. Baba, K. Yamashita, alpha1,2- Fucosylated and beta-N-acetylgalactosaminylated prostate-specific antigen as an efficient marker of prostatic cancer, Glycobiology, 20 (2010) 452–460.