ArticleMolecular genetics and metabolism2009
Exogenous mannose does not raise steady state mannose-6-phosphate pools of normal or N-glycosylation-deficient human fibroblasts.
Article in Molecular genetics and metabolism, 2009. 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, 15 citations in OpenAlex.
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- Article
- Generation and degradation of free asparagine-linked glycans.Cellular and molecular life sciences : CMLS · 2015Review
- Mannose metabolism: more than meets the eye.Biochemical and biophysical research communications · 2014Review
- Mannose phosphate isomerase regulates fibroblast growth factor receptor family signaling and glioma radiosensitivity.PloS one · 2014Article
- A zebrafish model of PMM2-CDG reveals altered neurogenesis and a substrate-accumulation mechanism for N-linked glycosylation deficiency.Molecular biology of the cell · 2012Article
- Mannose-6-phosphate regulates destruction of lipid-linked oligosaccharides.Molecular biology of the cell · 2011Article
- Towards a therapy for phosphomannomutase 2 deficiency, the defect in CDG-Ia patients.Biochimica et biophysica acta · 2009Review
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Increasing intracellular mannose-6-phosphate (Man-6-P) was previously reported to reduce the amount of the major lipid linked oligosaccharide (LLO) precursor of N-glycans; a loss that might decrease cellular N-glycosylation. If so, providing dietary mannose supplements to glycosylation-deficient patients might further impair their glycosylation. To address this question, we studied the effects of exogenous mannose on intracellular levels of Man-6-P, LLO, and N-glycosylation in human and mouse fibroblasts. Mannose (500microM) did not increase Man-6-P pools in human fibroblasts from controls or from patients with Congenital Disorders of Glycosylation (CDG), who have 90-95% deficiencies in either phosphomannomutase (CDG-Ia) or phosphomannose isomerase (MPI) (CDG-Ib), enzymes that both use Man-6-P as a substrate. In the extreme case of fibroblasts derived from Mpi null mice (<0.001% MPI activity), intracellular Man-6-P levels greatly increased in response to exogenous mannose, and this produced a dose-dependent decrease in the steady state level of the major LLO precursor. However, LLO loss did not decrease total protein N-glycosylation or that of a hypoglycosylation indicator protein, DNaseI. These results make it very unlikely that exogenous mannose could impair N-glycosylation in glycosylation-deficient CDG patients.
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