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Altered N-glycosylation profiles as potential biomarkers and drug targets in diabetes (CROSBI ID 268586)

Prilog u časopisu | pregledni rad (znanstveni) | međunarodna recenzija

Rudman, Najda ; Gornik, Olga ; Lauc, Gordan Altered N-glycosylation profiles as potential biomarkers and drug targets in diabetes // FEBS letters, 593 (2019), 13; 1598-1615. doi: 10.1002/1873-3468.13495

Podaci o odgovornosti

Rudman, Najda ; Gornik, Olga ; Lauc, Gordan

engleski

Altered N-glycosylation profiles as potential biomarkers and drug targets in diabetes

N-glycosylation is a ubiquitous protein modification, and N-glycosylation profiles are emerging as both biomarkers and functional effectors in various types of diabetes. Genome- wide association studies identified glycosyltransferase genes as candidate causal genes for type 1 and type 2 diabetes. Studies focused on N-glycosylation changes in type 2 diabetes demonstrated that patients can be distinguished from healthy controls based on N- glycome composition. In addition, individuals at an increased risk of future disease development could be identified based on N- glycome profiles. Moreover, accumulating evidence indicates that N-glycans have a major role in preventing the impairment of glucose- stimulated insulin secretion by maintaining the glucose transporter in proper orientation, indicating that interindividual variation in protein N-glycosylation might be a novel risk factor contributing to diabetes development. Defective N-glycosylation of T cells has been implicated in type 1 diabetes pathogenesis. Furthermore, studies of N-glycan alterations have successfully been used to identify individuals with rare types of diabetes (such as the HNF1A-MODY), and also to evaluate functional significance of novel diabetes- associated mutations. In conclusion, both N- glycans and glycosyltransferases emerge as potential therapeutic targets in diabetes.

glycosyltransferase ; HNF1A-MODY ; N-glycosylation ; type 1 diabetes ; type 2 diabetes

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Podaci o izdanju

593 (13)

2019.

1598-1615

objavljeno

0014-5793

1873-3468

10.1002/1873-3468.13495

Povezanost rada

Interdisciplinarne prirodne znanosti

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