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Background  Dystroglycan (DG) is a cell-surface laminin receptor that links the cytoskeleton to the extracellular matrix in a variety of epithelial tissues. Its function as a matrix receptor requires extensive glycosylation of its extracellular subunit αDG, which involves at least 13 distinct genes. Prior work has shown loss of αDG glycosylation in an assortment of carcinomas, including clear cell renal cell carcinoma (ccRCC) though the cause (s) and functional consequences of this loss are still unclear.    Methods  Using The Cancer Genome Atlas (TCGA) database, we analyzed the DG glycosylation pathway to identify changes in mRNA expression and correlation with clinical outcomes. We validated our findings with a cohort of 65 patients treated with radical nephrectomy by analyzing DG glycosylation via immunohistochemistry and gene expression via qRT-PCR.    Results  Analysis of TCGA database revealed frequent dysregulation of a subset of DG glycosyltransferases. Most notably, there was a frequent, significant downregulation of  GYLTL1B  (LARGE2) and  ISPD . DG glycosylation is frequently impaired in ccRCC patient samples and most strongly associates with downregulation of  GYLTL1B.Conclusions  Reduced levels of  GYLTL1B  and  ISPD  mRNA associated with increased patient mortality and are the likely cause of αDG hypoglycosylation in ccRCC.    Electronic supplementary material  The online version of this article (doi:10.1186/s12943-015-0416-z) contains supplementary material, which is available to authorized users.

Downregulation of dystroglycan glycosyltransferases LARGE2 and ISPD associate with increased mortality in clear cell renal cell carcinoma