PL EN


Preferences help
enabled [disable] Abstract
Number of results
2017 | 64 | 3 | 465-470
Article title

Reduced expression of E-cadherin and increased sialylation level in clear cell renal cell carcinoma

Content
Title variants
Languages of publication
EN
Abstracts
EN
Cancer cells are characterized by an aberrant increase in protein N-glycosylation and by disruption of E-cadherin-mediated adherens junctions. However, the relationship between alterations in N-glycosylation process and loss of E-cadherin adhesion in cancer remains unclear. The mechanisms of altered expression of adhesive glycoproteins in cancer cells have not been fully elucidated. Thus, the aim of this study was to examine the expression of E-cadherin and sialyl Lewisa/x, NeuAcα2-3Gal, NeuAcα2-6Gal/GalNAc structures in the normal renal tissue and intermediate and cancerous tissues from patients with clear cell RCC. Moreover, we attempted to correlate the E-cadherin expression with some specific sugar residues of renal cancer tissue glycoproteins. The expression of E-cadherin was analysed using ELISA test and immunoblotting. Oligosaccharide structures and sialylation level were detected with ELISA test using specific biotinylated lectins or antibodies. A significant decrease of E-cadherin expression as well as a significant increase in sialylated oligosaccharides level in intermediate zone and renal cancer tissue in comparison to normal renal tissue are reported. Significant decrease in expression of cadherins and increase in sialylation of oligosaccharide structures in renal cancer tissue in comparison to normal renal tissue, and in renal cancer tissue in comparison to intermediate zone of renal tissue, are important for the future research concerning detection and quantification of cadherins and sialylated oligosaccharide structures in urine and cells of urinary sediment as possible non-invasive marker of early RCC.
Year
Volume
64
Issue
3
Pages
465-470
Physical description
Dates
published
2017
received
2015-11-24
revised
2016-03-29
accepted
2017-02-19
(unknown)
2017-07-24
References
  • Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P (2008) Molecular Biology of the Cell, 5th edn, Garland Science, Taylor & Francis Group, NY USA & Abingdon UK.
  • Berx G, van Roy F (2009) Involvement of members of the cadherin superfamily in cancer. Cold Spring Harb Perspect Biol 1: a003129. doi: 10.1101/cshperspect.a003129.
  • Borzym-Kluczyk M, Radziejewska I (2013) Changes of the expression of Lewis blood group antigens in glycoproteins of renal cancer tissues. Acta Biochim Pol 60: 223-226.
  • Borzym-Kluczyk M, Radziejewska I, Cechowska-Pasko M (2015) Increased expression of MUC1 and sialyl Lewis antigens in different areas of clear renal cell carcinoma. Clin Exp Nephrol 19: 732-737. doi: 10.1007/s10157-014-1013-y.
  • Borzym-Kluczyk M, Radziejewska I, Darewicz B (2012) Glycosylation of proteins in healthy and pathological human renal tissues. Folia Histochem Cytobiol 50: 599-604. doi: 10.5603/17895.
  • Durand G, Seta N (2000) Protein glycosylation and diseases: blood and urinary oligosaccharides as markers for diagnosis and therapeutic monitoring. Clin Chem 46: 795-805.
  • Gervais ML, Henry PC, Saravanan A, Burry TN, Gallie BL, Jewett MA, Hill RP, Evans AJ, Ohh M. (2007) Nuclear E-cadherin and VHL immunoreactivity are prognostic indicators of clear-cell renal cell carcinoma. Lab Invest 87: 1252-1264. doi: 10.1038/labinvest.3700684.
  • Giepmans BN, van Ijzendoorn SC (2009) Epithelial cell-cell junctions and plasma membrane domains. Biochim Biophys Acta 1788: 820-831. doi: 10.1016/j.bbamem.2008.07.015.
  • Gupta S, Spiess PE (2013) The prospects of pazopanib in advanced renal cell carcinoma. Ther Adv Urol 5: 223-232. doi: 10.1177/1756287213495099.
  • Hakomori S (1989) Aberrant glycosylation in tumors and tumor-associated carbohydrate antigens. Adv Cancer Res 52: 257-331.
  • Hakomori S (1984) Tumor-associated carbohydrate antigens. Annu Rev Immunol 2: 103-126. doi: 10.1146/annurev.iy.02.040184.000535.
  • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
  • Lange T, Samatov TR, Tonevitsky AG, Schumacher U (2014) Importance of altered glycoprotein-bound N- and O-glycans for epithelial-to-mesenchymal transition and adhesion of cancer cells. Carbohydr Res 389: 39-45. doi: 10.1016/j.carres.2014.01.010.
  • Langner C, Ratschek M, Rehak P, Schips L, Zigeuner R (2004) Expression of MUC1 (EMA) and E-cadherin in renal cell carcinoma: a systematic immunohistochemical analysis of 188 cases. Mod Pathol 17: 180-188. doi: 10.1038/modpathol.3800032.
  • Leckband D, Israelachvili J (2001) Intermolecular forces in biology. Q Rev Biophys 34: 105-267.
  • Leckband DE, de Rooij J (2014) Cadherin adhesion and mechanotransduction. Annu Rev Cell Dev Biol 30: 291-315. doi: 10.1146/annurev-cellbio-100913-013212.
  • McEwen AE, Escobar DE, Gottardi CJ (2012) Signaling from the adherens junction. Subcell Biochem 60: 171-196. doi: 10.1007/978-94-007-4186-7_8.
  • Paulson AF, Prasad MS, Thuringer AH, Manzerra P (2014) Regulation of cadherin expression in nervous system development. Cell Adh Migr 8: 19-28. doi: 10.4161/cam.27839.
  • Pinho SS, Seruca R, Gärtner F, Yamaguchi Y, Gu J, Taniguchi N, Reis CA (2011) Modulation of E-cadherin function and dysfunction by N-glycosylation. Cell Mol Life Sci 68: 1011-1020. doi: 10.1007/s00018-010-0595-0.
  • Ronkainen H, Kauppila S, Hirvikoski P, Vaarala MH (2010) Evaluation of myosin VI, E-cadherin and beta-catenin immunostaining in renal cell carcinoma. J Exp Clin Cancer Res 29: 2. doi: 10.1186/1756-9966-29-2.
  • Smith PK, Krohn RI, Hermanson GT, Mallia AK, Gartner FH, Provenzano MD, Fujimoto EK, Goeke NM, Olson BJ, Klenk DC (1985) Measurement of protein using bicinchoninic acid. Anal Biochem 150: 76-85.
  • Stemmler MP (2008) Cadherins in development and cancer. Mol Biosyst 4: 835-850. doi: 10.1039/b719215k.
  • Syed SE, Trinnaman B, Martin S, Major S, Hutchinson J, Magee AI (2002) Molecular interactions between desmosomal cadherins. Biochem J 362: 317-327.
  • Thedieck C, Kuczyk M, Klingel K, Steiert I, Müller CA, Klein G (2005) Expression of Ksp-cadherin during kidney development and in renal cell carcinoma. Br J Cancer 92: 2010-2017. doi: 10.1038/sj.bjc.6602597.
  • Truong LD, Shen SS (2011) Immunohistochemical diagnosis of renal neoplasms. Arch Pathol Lab Med 135: 92-109. doi: 10.1043/2010-0478-RAR.1.
  • Varelas X, Bouchie MP, Kukuruzinska MA (2014) Protein N-glycosylation in oral cancer: dysregulated cellular networks among DPAGT1, E-cadherin adhesion and canonical Wnt signaling. Glycobiology 24: 579-591. doi: 10.1093/glycob/cwu031.
  • Varki A, Freeze HH (2009) Glycans in acquired human diseases. In Essentials of Glycobiology. Varki A, Cummings RD, Esko JD, Freeze HH, Stanley P, Bertozzi CR, Hart GW, Etzler ME, eds. Cold Spring Harbor (NY): Cold Spring Harbor Press.
  • Zhao YY, Takahashi M, Gu JG, Miyoshi E, Matsumoto A, Kitazume S, Taniguchi N (2008) Functional roles of N-glycans in cell signaling and cell adhesion in cancer. Cancer Sci 99: 1304-1310. doi: 10.1111/j.1349-7006.2008.00839.x.
Document Type
Publication order reference
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv64p465kz
Identifiers
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.