Comprehensive analysis of platelet glycoprotein Ibα ectodomain glycosylation.

ABSTRACT:

Background

Platelet glycoprotein (GP) Ibα is the major ligand-binding subunit of the GPIb-IX-V complex that binds von Willebrand factor. GPIbα is heavily glycosylated, and its glycans have been proposed to play key roles in platelet clearance, von Willebrand factor binding, and as target antigens in immune thrombocytopenia syndromes. Despite its importance in platelet biology, the glycosylation profile of GPIbα is not well characterized.

Objectives

The aim of this study was to comprehensively analyze GPIbα amino acid sites of glycosylation (glycosites) and glycan structures.

Methods

GPIbα ectodomain that was recombinantly expressed or that was purified from human platelets was analyzed by Western blot, mass spectrometry glycomics, and mass spectrometry glycopeptide an

SUBMITTER: Hollenhorst MA 

PROVIDER: S-EPMC10065957 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature