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Updated: Jul 4, 2026

Site-Directed Immobilization of Bone Morphogenetic Protein 2 to Solid Surfaces by Click Chemistry
Published on: March 29, 2018
Site-Specific Analysis of Bone Morphogenetic Protein Receptor Type 2 N‑Glycosylation Reveals High Heterogeneity at
Valeria Nazaire1, Alejandro Garcia1, Carlos H Pavan1
1Translational Glycobiology Institute, Department of Cellular and Molecular Medicine, Herbert Wertheim College of Medicine, Florida International University, Miami, Florida 33199, United States.
Abstract:
The bone morphogenetic protein receptor type 2 (BMPR2) is expressed in multiple cell types, including endothelial cells, and mediates cell signaling via binding of transforming growth factor β (TGF-β) family ligands, contributing to balanced cell proliferation, apoptosis, and angiogenesis. BMPR2 N-glycosylation reportedly influences ligand binding. Here, we sought to develop a bottom-up nanoliquid chromatography-tandem mass spectrometry method to obtain evidence of site-specific N-glycosylation of human BMPR2. To optimize the observation of all three predicted N-glycosylation sites, three protease combinations were tested. Trypsin-Glu-C N-glycopeptides spanning all three putative BMPR2 N-glycosylation sites (N29, N84, and N100) were observed. Analyses of N-glycosylation site occupancy revealed that sites N29 and N84 are highly occupied, while a minor but detectable proportion of BMPR2 is not glycosylated at site N100. Glycopeptide analyses revealed N-glycan compositions consistent with hybrid and complex glycoforms with abundant fucosylation and sialylation. The nLC-MS/MS method established here will facilitate the study of BMPR2 N-glycosylation and its function in homeostasis and disease. Data are available via ProteomeXchange with identifier PXD066494.
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