Open Access

VHL-dependent regulation of a β-dystroglycan glycoform and glycogene expression in renal cancer

  • Authors:
    • Vassilis Aggelis
    • Rachel A. Craven
    • Jianhe Peng
    • Patricia Harnden
    • Lana Schaffer
    • Gilberto E. Hernandez
    • Steven R. Head
    • Eamonn R. Maher
    • Robert Tonge
    • Peter J. Selby
    • Rosamonde E. Banks
  • View Affiliations

  • Published online on: August 21, 2013     https://doi.org/10.3892/ijo.2013.2066
  • Pages: 1368-1376
  • Copyright: © Aggelis et al. This is an open access article distributed under the terms of Creative Commons Attribution License [CC BY_NC 3.0].

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Abstract

Identification of novel biomarkers and targets in renal cell carcinoma (RCC) remains a priority and one cellular compartment that is a rich potential source of such molecules is the plasma membrane. A shotgun proteomic analysis of cell surface proteins enriched by cell surface biotinylation and avidin affinity chromatography was explored using the UMRC2- renal cancer cell line, which lacks von Hippel-Lindau (VHL) tumour suppressor gene function, to determine whether proteins of interest could be detected. Of the 814 proteins identified ~22% were plasma membrane or membrane-associated, including several with known associations with cancer. This included β-dystroglycan, the transmembrane subunit of the DAG1 gene product. VHL-dependent changes in the form of β-dystroglycan were detected in UMRC2-/+VHL transfectants. Deglycosylation experiments showed that this was due to differential sialylation. Analysis of normal kidney cortex and conventional RCC tissues showed that a similar change also occurred in vivo. Investigation of the expression of genes involved in glycosylation in UMRC2-/+VHL cells using a focussed microarray highlighted a number of enzymes involved in sialylation; upregulation of bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE) was validated in UMRC2- cells compared with their +VHL counterparts and also found in conventional RCC tissue. These results implicate VHL in the regulation of glycosylation and raise interesting questions regarding the extent and importance of such changes in RCC.
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November 2013
Volume 43 Issue 5

Print ISSN: 1019-6439
Online ISSN:1791-2423

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APA
Aggelis, V., Craven, R.A., Peng, J., Harnden, P., Schaffer, L., Hernandez, G.E. ... Banks, R.E. (2013). VHL-dependent regulation of a β-dystroglycan glycoform and glycogene expression in renal cancer. International Journal of Oncology, 43, 1368-1376. https://doi.org/10.3892/ijo.2013.2066
MLA
Aggelis, V., Craven, R. A., Peng, J., Harnden, P., Schaffer, L., Hernandez, G. E., Head, S. R., Maher, E. R., Tonge, R., Selby, P. J., Banks, R. E."VHL-dependent regulation of a β-dystroglycan glycoform and glycogene expression in renal cancer". International Journal of Oncology 43.5 (2013): 1368-1376.
Chicago
Aggelis, V., Craven, R. A., Peng, J., Harnden, P., Schaffer, L., Hernandez, G. E., Head, S. R., Maher, E. R., Tonge, R., Selby, P. J., Banks, R. E."VHL-dependent regulation of a β-dystroglycan glycoform and glycogene expression in renal cancer". International Journal of Oncology 43, no. 5 (2013): 1368-1376. https://doi.org/10.3892/ijo.2013.2066