ArticleMolecular cancer2015
Downregulation of dystroglycan glycosyltransferases LARGE2 and ISPD associate with increased mortality in clear cell renal cell carcinoma.
Article in Molecular cancer, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 33 citations in OpenAlex.
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- Mathematical and Machine Learning Models of Renal Cell Carcinoma: A Review.Bioengineering (Basel, Switzerland) · 2023Review
- A novel glycosylation-related gene signature predicts survival in patients with lung adenocarcinoma.BMC bioinformatics · 2022Article
- Involvement of abnormal dystroglycan expression and matriglycan levels in cancer pathogenesis.Cancer cell international · 2022Review
- Multi-Omics Immune Interaction Networks in Lung Cancer Tumorigenesis, Proliferation, and Survival.International journal of molecular sciences · 2022Article
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- Biosynthetic Mechanisms and Biological Significance of Glycerol Phosphate-Containing Glycan in Mammals.Molecules (Basel, Switzerland) · 2021Review
- Differential DNA Methylation by Hispanic Ethnicity Among Firefighters in the United States.Epigenetics insights · 2021Article
- Article
- Exogenous expression of the glycosyltransferase LARGE1 restores α-dystroglycan matriglycan and laminin binding in rhabdomyosarcoma.Skeletal muscle · 2019Article
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- Expression pattern in retinal photoreceptors of POMGnT1, a protein involved in muscle-eye-brain disease.Molecular vision · 2016Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundDystroglycan (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.
methodsUsing 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.
resultsAnalysis 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.
conclusionsReduced levels of GYLTL1B and ISPD mRNA associated with increased patient mortality and are the likely cause of αDG hypoglycosylation in ccRCC.
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