ArticlePloS one2011
LARGE expression augments the glycosylation of glycoproteins in addition to α-dystroglycan conferring laminin binding.
Article in PloS one, 2011. 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, 24 citations in OpenAlex.
- Biomarkers in Primary Focal Segmental Glomerulosclerosis in Optimal Diagnostic-Therapeutic Strategy.Journal of clinical medicine · 2022Review
- Post-translational Modification in Muscular Dystrophies.Advances in experimental medicine and biology · 2022Article
- Defective lysosome reformation during autophagy causes skeletal muscle disease.The Journal of clinical investigation · 2021Article
- Eyes shut homolog (EYS) interacts with matriglycan of O-mannosyl glycans whose deficiency results in EYS mislocalization and degeneration of photoreceptors.Scientific reports · 2020Article
- Recent advancements in understanding mammalian O-mannosylation.Glycobiology · 2017Review
- Article
- Endogenous glucuronyltransferase activity of LARGE or LARGE2 required for functional modification of α-dystroglycan in cells and tissues.The Journal of biological chemistry · 2014Article
- Renal biopsy: use of biomarkers as a tool for the diagnosis of focal segmental glomerulosclerosis.Disease markers · 2014Review
- Biochemical and biophysical changes underlie the mechanisms of basement membrane disruptions in a mouse model of dystroglycanopathy.Matrix biology : journal of the International Society for Matrix Biology · 2013Article
- Adeno-associated viral-mediated LARGE gene therapy rescues the muscular dystrophic phenotype in mouse models of dystroglycanopathy.Human gene therapy · 2013Article
- High throughput screening for compounds that alter muscle cell glycosylation identifies new role for N-glycans in regulating sarcolemmal protein abundance and laminin binding.The Journal of biological chemistry · 2012Article
- Vertebrate protein glycosylation: diversity, synthesis and function.Nature reviews. Molecular cell biology · 2012Review
- Mutations in ISPD cause Walker-Warburg syndrome and defective glycosylation of α-dystroglycan.Nature genetics · 2012Article
- Differential glycosylation of α-dystroglycan and proteins other than α-dystroglycan by like-glycosyltransferase.Glycobiology · 2012Article
- Laminins in basement membrane assembly.Cell adhesion & migrationReview
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Mutations in genes encoding glycosyltransferases (and presumed glycosyltransferases) that affect glycosylation and extracellular matrix binding activity of α-dystroglycan (α-DG) cause congenital muscular dystrophies (CMDs) with central nervous system manifestations. Among the identified genes, LARGE is of particular interest because its overexpression rescues glycosylation defects of α-DG in mutations of not only LARGE but also other CMD-causing genes and restores laminin binding activity of α-DG. It is not known whether LARGE protein glycosylates other proteins in addition to α-DG. In this study, we overexpressed LARGE in DG-deficient cells and analyzed glycosylated proteins by Western blot analysis. Surprisingly, overexpression of LARGE in α-DG-deficient cells led to glycosylation dependent IIH6C4 and VIA4-1 immunoreactivity, despite the prevailing view that these antibodies only recognize glycosylated α-DG. Furthermore, the hyperglycosylated proteins in LARGE-overexpressing cells demonstrated the functional capacity to bind the extracellular matrix molecule laminin and promote laminin assembly at the cell surface, an effect that was blocked by IIH6C4 antibodies. These results indicate that overexpression of LARGE catalyzes the glycosylation of at least one other glycoprotein in addition to α-DG, and that this glycosylation(s) promotes laminin binding activity.
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Registered trials
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