ArticleExperimental & molecular medicine2018
Loss of complex O-glycosylation impairs exocrine pancreatic function and induces MODY8-like diabetes in mice.
Article in Experimental & molecular medicine, 2018. 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, 25 citations in OpenAlex.
- Overexpression of Tn antigen induces chronic pancreatitis in mice.Scientific reports · 2025Article
- Dynamic glycosylation remodeling in neurological disorders.Frontiers in molecular neuroscience · 2025Review
- GalNT2-mediated O-glycosylation affects pancreas development and function in mice.Scientific reports · 2024Article
- CD301 and LSECtin glycan-binding receptors of innate immune cells serve as prognostic markers and potential predictors of immune response in breast cancer subtypes.Glycobiology · 2024Article
- A Comprehensive Analysis of Tn and STn Antigen Expression in Esophageal Adenocarcinoma.Cancers · 2024Article
- Identification and characterization of novel carboxyl ester lipase gene variants in patients with different subtypes of diabetes.BMJ open diabetes research & care · 2023Article
- Global Loss of Core 1-DerivedInternational journal of molecular sciences · 2022Article
- Recent Advances in Mass Spectrometry-Based Glycomic and Glycoproteomic Studies of Pancreatic Diseases.Frontiers in chemistry · 2021Review
- Protein Glycosylation in Diabetes.Advances in experimental medicine and biology · 2021Article
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Authors and funding
16 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cosmc is ubiquitously expressed and acts as a specific molecular chaperone assisting the folding and stability of core 1 synthase. Thus, it plays a crucial role in the biosynthesis of O-linked glycosylation of proteins. Here, we show that ablation of Cosmc in the exocrine pancreas of mice causes expression of truncated O-glycans (Tn antigen), resulting in exocrine pancreatic insufficiency with decreased activities of digestive enzymes and diabetes. To understand the molecular causes of the pleiotropic phenotype, we used Vicia villosa agglutinin to enrich Tn antigen-modified proteins from Cosmc-KO pancreatic lysates and performed a proteomic analysis. Interestingly, a variety of proteins were identified, of which bile salt-activated lipase (also denoted carboxyl-ester lipase, Cel) was the most abundant. In humans, frameshift mutations in CEL cause maturity-onset diabetes of the young type 8 (MODY8), a monogenic syndrome of diabetes and pancreatic exocrine dysfunction. Here, we provide data suggesting that differentially O-glycosylated Cel could negatively affect beta cell function. Taken together, our findings demonstrate the importance of correct O-glycan formation for normal exocrine and endocrine pancreatic function, implying that aberrant O-glycans might be relevant for pathogenic mechanisms of the pancreas.
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