Protein glycosylation and renal cancer

Ferguson, Roisean E.; Vasudev, Naveen S.; Selby, Peter J.; Banks, Rosamonde E.

doi:10.1002/047001153x.g305222

Cited by 2 publications

(1 citation statement)

References 56 publications

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“… 60 ). Changes in glycosylation in RCC have been shown using lectin staining ( 61 ) and we have previously described VHL-dependent changes in glycosylation of CD166 ( 7 ). The extent to which glycosylation of other proteins can also be regulated by VHL remains to be determined.…”

Section: Discussionmentioning

confidence: 87%

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

Aggelis

Craven

Peng

et al. 2013

International Journal of Oncology

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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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Section: Discussionmentioning

confidence: 87%

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

Aggelis

Craven

Peng

et al. 2013

International Journal of Oncology

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Glycosylation of proteins in healthy and pathological human renal tissues

Borzym‐Κluczyk

Radziejewska

Darewicz

2012

Folia Histochem Cytobiol.

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Abstract:Cancer development is associated with the improper glycosylation of proteins. There are alterations in the synthesis and expression of sugar structures. These changes can be important not only in the early stages of tumour development, but also in the next stages connected with cancer invasiveness and its ability to form metastases. Oligosaccharide structures of glycans in tumours deviate from normal cells. Relatively increased degrees of branching and sialylation of N-glycans, enhanced presentation of short-chain mucin-type O-glycans with sialylation, and alterations in the expression of blood group ABO and Lewis epitopes can be observed. The main aim of our study was to assess changes in the glycosylation of proteins in clear cell renal cell carcinoma. This study was performed on tissues taken from 15 patients. The relative amounts of sugar structures of proteins with molecular mass above 30 kDa in tumour (cancer tissue), intermediate zone i.e. tumour-adjacent tissue, and normal tissue uninvolved by tumour, were determined by ELISA-like test with biotinylated lectins highly specific to examined sugar antigens. A higher expression of all examined structures was revealed in cancer tissue. Increased levels of sialic acid, fucose, T and Tn antigens, compared to healthy renal tissue, were characteristic for clear cell renal cell carcinoma.

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Protein glycosylation and renal cancer

Cited by 2 publications

References 56 publications

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

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

Glycosylation of proteins in healthy and pathological human renal tissues

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