|About the author:
||Antonyuk R.V., Lutsik O. D.
|Type of article
||It is known that in the case of malignant degeneration of colon both carbohydrate and protein parts of mucin are transformated. Carbohydrate and peptide epitopes are more or less sulfated, sialated, shortened and often contain T-antigen. To investigate these changes lectins (substances of protein nature that can selectively bind to carbohydrates, but do not produce their chemical transformations) are often used as molecular probes. In the present paper we studied as lectins were binding with carbohydrate receptors in human colon neoplasia. We used two groups of lectins - specific for T-antigen (PNA, ACA) and specific to the N-acethyllactosamine (RCA, PIFA, CNFA).
The aim was to investigate the possibility of using the above mentioned peroxidase-labeled lectins for the diagnosis of neoplastic degeneration in humans in the case of colon cancer of varying degrees of differentiation.
Intraoperational and biopsy material of 28 cases of colon cancer have been investigated: (highly differentiated adenocarcinoma – 14, moderate tumor differentiation - 10, and poorly differentiation - 4, in three samples mucinous carcinomas structure morphology contained). 4 cases of colon adenomas, and 9 samples of autopsy material human colon without signs of disease have been investigated as well.
As a result of the research, it was found that PNA, RCA, CNFA carbohydrate determinants in normal mucosa epitheliocytes of colon virtually were absent, though still in some sections not intense coloration was observed. Whereas lectin-positive epithelial cells to ASA, the PIFA were found in almost all samples.
All used lectins showed selectivity to cytoreceptors of colon tumors. Both, PNA, CNFA were able to selectively interact with carbohydrate determinants incorpotated in neoplasy of colon cancer. Percentage of lectin-positive histological samples using these two lectins almost coincide. of It reached 83% for PNA and 80 % for CNFA in carcinoma cases, in contrast to 9% for PNA and 18% for CNFA interaction with receptors of normal colon mucosa. However, CNFA interacted with over nuclear (but not perіnuсlear) structures of epithelial mucosa of cancer-modified and normal cells, unlike other lectins used in the work. CNFA is considered as N, N'-diacethyllactosediamine specific (GalNAcβ1-4GlcNAc, LacdiNAc). Normally, these receptors are very few common in mammalian cells, but they appear in some cells of tissue of malignant degeneration. However, the applicability of this lectin in the diagnosis isn’t studied enough.
The obtained results can be used to develop methods for early diagnosis of malignant tumors of the colon.
||lectinohistochemistry, colon cancer, diagnostics
- Antonjuk V. A. Kon'jugirovanie lektinov s peroksidazoj hrena: usovershenstvovanie metodiki. / V. A. Antonjuk, A. M. Jashhenko // Klinicheskaja laboratornaja diagnostika – 1996. - № 3.- S. 51-52.
- Antonyuk R. Lectin purification from fruiting bodies of brown roll-rim fungus (Рахillus involutus (Fr.) Fr.) and its application in histochemistry. / R. Antonyuk, A. Lutsyk, V. Antonyuk // Romanian Journal of Morphology and Embryology. – 2014. - Vol.55, No 3. – P. 787–796.
- Boland. C. R. Alterations in human colonie mucin occurring with cellular differentiation and malignant transfor mation. / C. R. Boland, C. K. Montgomery, V. S. Kim. // Proc. Natl. Acad. Sci. USA. - 1982.- Vol. 79. – P. 2051-2055.
- Boland. C. R. Mucin histochemistry in colonie polyps and cancer./ C. R. Boland // Semin. Surg. Oncol.- 1987. - Vol. 3. – P. 183-189.
- Boland C. R. Use of the Lectin from Amaranthus caudatus as a Histochemical Probe of Proliferating Colonic Epithelial Cells. / C. R. Boland, Y-F. Chen , S. J. Rinderle, // Cancer Research. - 1991. – Vol. 51, P. 657-665.
- Baldus, S. E. Thomsen–Friedenreich antigen presents as a prognostic factor in colorectal carcinoma: a clinicopathologic study of 264 patients. / S. E. Baldus, T. K. Zirbes, [et al.] // Cancer. - 2000. – Vol. 88 - P.1536–1543.
- Cooper H. S. Peanut lectin-binding sites in large bowel carcinoma. / H. S. Cooper // Lab. Invest. - 1982. - Vol. 47. – P. 383-390.
- Chacko B. K. Peanut (Arachis hypogaea) lectin recognizes alpha-linked galactose, but not N-acetyl lactosamine in N-linked oligosaccharide terminals. / B. K. Chacko, P. S. Appukuttan // Int J Biol Macromol.- 2001.- Vol.28, No 5.-P. 365-371.
- Cazet A. Tumour-associated carbohydrate antigens in breast cancer. /A. Cazet, S. Julien, M. Bobowski [et al.] // Breast Cancer Research. – 2010. – Vol. 12. P. 204 – 217.
- Huang J. 1,4-N-Acetylgalactosaminyltransferase III enhances malignant phenotypes of colon cancer cells. / J. Huang, J. T., Liang, H. C. Huang [et al.] // Mol. Cancer Res. - 2007, Vol.5, P. 543–552.
- Hirano K. Method for determining prostate cancer. / K. Hirano, T. Nakamura, J. Amano // International Patent WO/2010/064683, December 3, - 2009.
- Hirano K. Expression of LacdiNAc Groups on N-Glycans among Human Tumors Is Complex / K. Hirano, A. Matsuda, T. Shirai [et al.] // Biomed Res Int. 2014, Published online - 2014 May 18.
- Kannan S. Expression of peanut agglutinin-binding mucin-type glycoprotein in human esophageal squamous cell peanut agglutininas a marker. / S. Kannan, R.A. Lakku, D. Niranjali [et al.] //Mol Cancer. - 2003.- Vol.2, No 1 P.38 -45.
- Kumar S. R. Thomsen–Friedenreich and Tn antigens in nipple fluid: carbohydrate biomarkers for breast cancer detection./ S.R. Kumar, E.R. Sauter, T.P. Quinn, S.L. Deutscher // Clin. Cancer Res.- 2005. - Vol. 11. - P. 6868–6871.
- Machado E. N-Glycosylation of total cellular glycoproteins from the human ovarian carcinoma SKOV3 cell line and of recombinantly expressed human erythropoietin / E.Machado, S.Kandzia, R. Carilho [et al.]. //Glycobiology.–2011.–Vol. 21.–P.376–386.
- Nakane Р. К. Peroxidase labelled antibody. A new method of conjugation. / Р. К. Nakane, A. Kawaoi // J. Histochem. Cytochem. - 1974. - Vol. 22, No 12. - P. 1084-1091.
- Pohleven J. Purification, characterization, and cloning of a ricin B-like lectin from mushroom Clitocybe nebularis with antiproliferative activity against human leukemic T cells. / J. Pohleven, N. Obermajer, J. Sabotic [et al.] //Biochim.Biophys. Acta. – 2009. –Vol. 1990. – P. 173–181.
- Sata T. Studies on the Thomsen-Friedenreich antigen in human colon with the lectin Amaranthin. Normal and neoplastic epithelium express only cryptic T antigen. / T. Sata, J. Roth, C. Zuber [et al.] // Lab. Invest. – 1992. - Vol. 66, No 2, - P. 175-186.
- Schultz M. J. Regulation of the metastatic cell phenotype by sialylated glycans. / M. J. Schultz, A. F. Swindall, S. L. Bellis // Cancer Meta. Rev. – 2012. –Vol. 31, No 3-4. – P. 501-518.
- Siegel R. Cancer statistics. / R. Siegel, D. Naishadham, A. Jemal // CA: A Cancer Journal for Clinicians. - 2013. – Vol. 63, No 1 – P. 11 – 30.
- Wu J. H. Defining carbohydrate specificity of Ricinus communis agglutinin as Gal beta 1→4GlcNAc (II) >Gal beta 1→3GlcNAc (I) > Gal alpha 1→3Gal (B) > Gal beta 1→3GalNAc (T). / J.H. Wu, A. Herp, A.M. Wu // Mol Immunol. - 1993.- Vol. 30, No 4.- P.333-339.
- Wang D. Prostate Cancer Glycans Markers and Autoantibode Signatures. / D. Wang, L. A. Herzenberg, D. M. Peehl [et al.] // International Patent Pub. No,- 2009.
|Publication of the article
||«World of Medicine and Biology» №2(49) 1 part 2015 year, 073-078 pages, index UDK [611.018+ 616.345-006]+547.96