Litcius/Paper detail

Aberrant sialylation in a patient with a HNF1α variant and liver adenomatosis

Luisa Sturiale, Marie‐Cécile Nassogne, Angelo Palmigiano, Angela Messina, Immacolata Speciale, Rosangela Artuso, Gaetano Bertino, Nicole Revençu, Xavier Stéphenne, Cristina De Castro, Gert Matthijs, Rita Barone, Jaak Jaeken, Domenico Garozzo

2021iScience16 citationsDOIOpen Access PDF

Abstract

variant. Serum transferrin isoelectric focusing showed a surprising N-glycosylation pattern consisting on hyposialylation, as well as remarkable hypersialylation. Mass spectrometry-based glycomic analyses of individual serum glycoproteins enabled to unveil hypersialylated complex N-glycans comprising up to two sialic acids per antenna. Further advanced MS analysis showed the additional sialic acid is bonded through an α2-6 linkage to the peripheral N-acetylglucosamine residue.

Topics & Concepts

Computational biologyMutationChemistryGeneticsBiologyBiochemistryGeneGlycosylation and Glycoproteins ResearchProteoglycans and glycosaminoglycans researchPeptidase Inhibition and Analysis
Aberrant sialylation in a patient with a HNF1α variant and liver adenomatosis | Litcius