Impact of protein glycosylation on lipoprotein metabolism and atherosclerosis

Abstract Protein glycosylation is a post-translational modification consisting in the enzymatic attachment of carbohydrate chains to specific residues of the protein sequence. Several types of glycosylation have been described, with N-glycosylation and O-glycosylation being the most common types imp...

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Bibliographic Details
Published in:Cardiovascular research 2021-03, Vol.117 (4), p.1033-1045
Main Authors: Pirillo, Angela, Svecla, Monika, Catapano, Alberico Luigi, Holleboom, Adriaan G, Norata, Giuseppe Danilo
Format: Article
Language:English
Subjects:
Animals
Apolipoproteins - genetics
Apolipoproteins - metabolism
Atherosclerosis - genetics
Atherosclerosis - metabolism
Atherosclerosis - pathology
Dyslipidemias - genetics
Dyslipidemias - metabolism
Genetic Predisposition to Disease
Glycosylation
Humans
Lipid Metabolism - genetics
Lipoproteins - genetics
Lipoproteins - metabolism
Phenotype
Plaque, Atherosclerotic
Protein Processing, Post-Translational
Receptors, Lipoprotein - genetics
Receptors, Lipoprotein - metabolism
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Summary:Abstract Protein glycosylation is a post-translational modification consisting in the enzymatic attachment of carbohydrate chains to specific residues of the protein sequence. Several types of glycosylation have been described, with N-glycosylation and O-glycosylation being the most common types impacting on crucial biological processes, such as protein synthesis, trafficking, localization, and function. Genetic defects in genes involved in protein glycosylation may result in altered production and activity of several proteins, with a broad range of clinical manifestations, including dyslipidaemia and atherosclerosis. A large number of apolipoproteins, lipoprotein receptors, and other proteins involved in lipoprotein metabolism are glycosylated, and alterations in their glycosylation profile are associated with changes in their expression and/or function. Rare genetic diseases and population genetics have provided additional information linking protein glycosylation to the regulation of lipoprotein metabolism.
ISSN:0008-6363
1755-3245
DOI:10.1093/cvr/cvaa252