ArticleBiomolecules2015
Co-Expression of NEU2 and GBA3 Causes a Drastic Reduction in Cytosolic Sialyl Free N-glycans in Human MKN45 Stomach Cancer Cells-Evidence for the Physical Interaction of NEU2 and GBA3.
Article in Biomolecules, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- GBA3 as a regulator of sphingolipid metabolism in the progression of hepatocellular carcinoma.Journal of gastrointestinal oncology · 2025Article
- Free oligosaccharides in serum.BBA advances · 2025Article
- Article
- Transcriptomic networks of gba3 governing specification of the dopaminergic neurons in zebrafish embryos.Genes & genomics · 2022Article
- Review
- GBA3: a polymorphic pseudogene in humans that experienced repeated gene loss during mammalian evolution.Scientific reports · 2020Article
- Cytosolic FreeFrontiers in plant science · 2020Article
- A prognostic prediction system for hepatocellular carcinoma based on gene co-expression network.Experimental and therapeutic medicine · 2019Article
- Identification of metabolism-associated genes and pathways involved in different stages of clear cell renal cell carcinoma.Oncology letters · 2018Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It is well known that the "free" form of glycans that are structurally related to asparagine (N)-linked glycans ("free N-glycans") are found in a wide variety of organisms. The mechanisms responsible for the formation/degradation of high mannose-type free N-glycans have been extensively studied in mammalian cells. Recent evidence, however, also suggests that sialylated, complex-type free N-glycans are also present in the cytosol of various mammalian-derived cultured cells/tissues. We report herein on an investigation of the mechanism responsible for the degradation of such sialyl free N-glycans. The findings show that the amount of glycans is dramatically reduced upon the co-expression of cytosolic sialidase NEU2 with cytosolic β-glycosidase GBA3 in human stomach cancer-derived MKN45 cells. The physical interaction between NEU2 and GBA3 was confirmed by co-precipitation analyses as well as gel filtration assays. The NEU2 protein was found to be stabilized in the presence of GBA3 both in cellulo and in vitro. Our results thus indicate that cytosolic GBA3 is likely involved in the catabolism of cytosolic sialyl free N-glycans, possibly by stabilizing the activity of the NEU2 protein.
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