Abstract
N-glycans are covalently linked to an asparagine residue in a simple acceptor sequence of proteins, called a sequon. This modification is important for protein folding, enhancing thermodynamic stability, and decreasing abnormal protein aggregation within the endoplasmic reticulum (ER), for the lifetime and for the subcellular localization of proteins besides other functions. Hypoglycosylation is the hallmark of a group of rare genetic diseases called congenital disorders of glycosylation (CDG). These diseases are due to defects in glycan synthesis, processing, and attachment to proteins and lipids, thereby modifying signaling functions and metabolic pathways. Defects in N-glycosylation and O-glycosylation constitute the largest CDG groups. Clotting and anticlotting factor defects as well as a tendency to thrombosis or bleeding have been described in CDG patients. However, N-glycosylation of platelet proteins has been poorly investigated in CDG. In this review, we highlight normal and deficient N-glycosylation of platelet-derived molecules and discuss the involvement of platelets in the congenital disorders of N-glycosylation.
Highlights
N-linked protein glycosylation is a conserved process of protein modification that eukaryotic cells use for protein folding, assembly, and trafficking
“trees”) to polypeptides takes place in the endoplasmic reticulum, where the oligosaccharyltransferase (OST) complex catalyzes the transfer of a high mannose oligosaccharide onto asparagine residues within the primary protein sequence of Asn–X–Ser or Asn–X–Thr (NXS/T), where X is any amino acid except proline [1,2]
The OST complex in humans is a protein complex composed of several subunits, including STT3 oligosaccharyltransferase complex catalytic subunit A (STT3A), subunit B
Summary
N (asparagine)-linked protein glycosylation is a conserved process of protein modification that eukaryotic cells use for protein folding, assembly, and trafficking. Two OST complexes have been identified in mammalians with catalytic subunits STT3A or STT3B associated with different non-catalytic subunits [2] They couple oligosaccharides to create a specific sugar tree on the protein surface [2]. N-glycosylation of platelet-derived regulating functions platelets functional role of the protein complex under molecules normal and diseaseseveral conditions has ofnot been and megakaryocytes in thrombosis, biogenesis Glycosylation is involved in calcium homeostasis, ROCE and SOCE in platelets. Glycolysis mitochondrial oxidative metabolism are regulated by undergoing N-glycosylation, which influence glucose homeostasis, and energy metabolism and proteins undergoing N‐glycosylation, which influence glucose homeostasis, and energy metabolism platelet biogenesis.
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
