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Impact of asialoglycoprotein receptor and mannose receptor deficiency on murine plasma N-glycome profiles

ABSTRACT: The asialoglycoprotein receptor (ASGPR) and the mannose receptor 1 (MRC1) are C-type lectins that identify and remove glycoproteins from circulation. ASGPR recognizes terminal galactose and N-acetylgalactosamine, whereas MRC1 recognizes terminal mannose, fucose, and N-acetylglucosamine. The effects of ASGPR and MRC1 deficiency on the N-glycosylation of individual circulating proteins have been studied. However, the impact on the homeostasis of the major plasma glycoproteins is debated and their glycosylation has not been mapped with high molecular resolution in this context. Therefore, we evaluated the total plasma N-glycome and plasma proteome of ASGR1 and MRC1 deficient mice.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Blood Plasma

SUBMITTER: Giangiacomo Beretta

LAB HEAD: Giuseppe Danilo Norata

PROVIDER: PXD042269 | Pride | 2023-10-24

REPOSITORIES: Pride

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			Action	DRS
	21P74-ASGR1-KO-01.mzML	Mzml
	21P74-ASGR1-KO-01.mzTab	Mztab
	21P74-ASGR1-KO-01.raw	Raw
	21P74-ASGR1-KO-02.mzML	Mzml
	21P74-ASGR1-KO-02.mzTab	Mztab

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Publications

Impact of Asialoglycoprotein Receptor and Mannose Receptor Deficiency on Murine Plasma N-glycome Profiles.

Svecla M M Nour J J Bladergroen M R MR Nicolardi S S Zhang T T Beretta G G Wuhrer M M Norata G D GD Falck D D

Molecular & cellular proteomics : MCP 20230704 9

The asialoglycoprotein receptor (ASGPR) and the mannose receptor C-type 1 (MRC1) are well known for their selective recognition and clearance of circulating glycoproteins. Terminal galactose and N-Acetylgalactosamine are recognized by ASGPR, while terminal mannose, fucose, and N-Acetylglucosamine are recognized by MRC1. The effects of ASGPR and MRC1 deficiency on the N-glycosylation of individual circulating proteins have been studied. However, the impact on the homeostasis of the major plasma g ...[more]

PMID: 37414249

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Precision structural interpretation of site-specific N-glycans in seminal plasma

Project description:This study is aimed to comprehensively and globally characterize seminal plasma glycoproteins in a site-specific manner with information of N-glycosites and corresponding glycan structures, as well as glycan isomers using mass spectrometry. Furthermore, the function of specific glycan structures is introduced during human reproduction. In addition, site-specific glycoproteins are compared precisely to explored the sub-glycan structure regulation of glycoprotein in human seminal plasma and spermatozoa.

2023-03-04 | PXD030804 | Pride

Human Caco-2 proteome and N-glycome during differentiation

Project description:Park, D, Brune, KA, Mitra, A, Marusina, AI, Maverakis, E, Lebrilla, CB. Characteristic Changes in Cell Surface Glycosylation Accompany Intestinal Epithelial Cell Differentiation: High Mannose Structures Dominate the Cell Surface Glycome of Undifferentiated Enterocytes, Molecular and Cellular Proteomics: submitted.

2015-08-21 | MSV000079264 | MassIVE

Free glycans derived from O-mannosylated glycoproteins suggest the presence of an O-glycoprotein degradation pathway in yeast

Project description:In eukaryotic cells, unconjugated oligosaccharides structurally related to N-glycans (FNGs) are generated either from misfolded N-glycoproteins destined for endoplasmic reticulum (ER)-associated degradation (ERAD), or from lipid-linked oligosaccharides, donor substrates for N-glycosylation of proteins. The mechanism responsible for the generation of FNGs is now well understood, but whether there are other type of free glycans remain unclarified. Here, we report on the accumulation of O-mannosylated free glycans in budding yeast that were cultured in media containing mannose as a carbon source. A structural analysis of these glycans revealed that their structures are identical to those of O-mannosyl glycans that are attached to glycoproteins. Deletion of the cyc8 gene, encoding a general transcription repressor, resulted in the accumulation of excessive amounts of the free O-glycans, concomitant with a severe growth defect, a reduction in the level of cellular O-mannosylated proteins, and compromised cell wall integrity. Our findings provide evidence for a regulated pathway for O-glycoprotein degradation in yeast and offer critical insights into the catabolic mechanisms that control the fate of O-glycosylated proteins.

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Cell lines LS180 vs U937

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Extensive heterogeneity of glycopeptides in plasma revealed by deep glycoproteomic analysis

Project description:A number of plasma glycoproteins are clinically useful as biomarkers in a variety of diseases. Although thousands of proteins are present in plasma, >95% of the plasma proteome by mass is represented by only 22 proteins. This necessitates strategies to deplete the abundant proteins and enrich other subsets of proteins. Although glycoproteins are abundant in plasma, in routine proteomic analyses, glycopeptides are not often investigated. Traditional methods such as lectin-based enrichment of glycopeptides followed by deglycosylation have helped understand the glycoproteome, but they lack any information about the attached glycans. Here, we apply size-exclusion chromatography (SEC) as a simple strategy to enrich intact glycopeptides based on their larger size which achieves broad selectivity regardless of the nature of attached glycans. Using this approach, we identified 1,317 glycopeptides belonging to 266 glycosylation sites on 154 plasma glycoproteins. The deep coverage achieved by this approach was evidenced by extensive heterogeneity that was observed. For instance, 20-100 glycopeptides were observed per protein for the top 15 glycoproteins. Overall, we found 615 novel glycopeptides of which 39 glycosylation sites (from 38 glycoproteins) are not including in protein databases such as Uniprot and GlyconnectDB. We also identified 12 novel glycopeptides containing di-sialic acid, which is a rare glycan epitope. Thus, SEC allows for efficient LC-MS/MS-based deep glycoproteomics from low amounts (~1 l) of human plasma. Overall, the SEC-based method described here is a simple, rapid and high-throughput strategy for characterization of the glycoproteome.

2021-08-18 | PXD025414 | Pride

Probing Blood Plasma Protein Glycosylation with Infrared Spectroscopy

Project description:The health state of an individual is closely linked to the glycosylation patterns of their blood plasma proteins. However, obtaining this information requires cost- and time-efficient analytical methods. We put forward infrared spectroscopy, which allows label-free analysis of protein glycosylation, but so far has only been applied to analyses of individual proteins. Although spectral information does not directly provide the molecular structure of the glycans, it is sensitive to changes therein and covers all types of glycosidic linkages. Combining single-step ion exchange chromatography with infrared spectroscopy, we developed a workflow that enables separation and analysis of major protein classes in blood plasma. Our results demonstrate that infrared spectroscopy can identify different patterns and global levels of glycosylation of intact plasma proteins. To showcase the strengths and limitations of the proposed approach, we compare the glycoforms of human and bovine alpha-1-acid glycoproteins, which exhibit highly variable global levels of glycosylation. To further independently evaluate our conclusions, the glycan moieties of human alpha-1-acid glycoprotein were further analyzed using established glycomics workflow. Importantly, the chromatographic separation of blood plasma improves the detection of aberrant glycoforms of a given protein, as compared to infrared spectroscopy of bulk plasma. The presented approach allows time-efficient comparison of glycosylation patterns of multiple plasma proteins, opening new avenues for biomedical probing.

2024-02-26 | PXD046796 | Pride

Glyco-CPLL: an integrated method for in-depth and comprehensive N-glycoproteome profiling of human plasma

Project description:N-glycoproteins are involved in various biological processes. Certain distinctive glycoforms on specific glycoproteins enhance the specificity and/or sensitivity of cancer diagnosis. Therefore, the characterization of plasma N-glycoproteome is essential for new biomarker discovery. Absence of suitable analytical methods for in-depth and large-scale analyses of low-abundance plasma glycoproteins make it challenging to investigate the role of glycosylation. In this study, we developed an integrated method termed Glyco-CPLL, which integrates combinatorial peptide ligand libraries, high-pH reversed-phase pre-fractionation, hydrophilic interaction chromatography, trypsin and PNGase F digestion, shotgun proteomics, and various analysis software (MaxQuant and pGlyco2.0) for the low-abundance plasma glycoproteomic profiling. Then, we utilized the method to perform a comparative study and to explore papillary thyroid carcinoma-related proteins and glycosylations with reference to healthy controls. Finally, a large and comprehensive human plasma N-glycoproteomic database was established, containing 786 proteins, 369 N-glycoproteins, 862 glycosites, 171 glycan compositions, and 1644 unique intact N-glycopeptides. Additionally, several low-abundance plasma glycoproteins were identified, including SVEP1 (~0.54 ng/mL), F8 (~0.83 ng/mL), ADAMTS13 (~1.2 ng/mL). These results suggest that this method will be useful for analyzing plasma intact glycopeptides in future studies. Besides, the Glyco-CPLL method has a great potential to be translated to clinical applications.

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Project description:N-linked glycosylation is an important type of post-translational modification. This modification plays important roles in many cellular functions including cell-cell and receptor-ligand interactions, immune response, apoptosis, and pathogenesis of many diseases. Seminal plasma is a mixture of secretions from several male accessory glands. Glycoproteins in seminal plasma can reflect the states of reproductive organs or diseases. Using isotope labeling and high-resolution mass spectrometry, we identified 720 N-glycosylated sites on 372 N-glycosylated proteins, corresponding to 365 genes. Analysis of variations among five individuals revealed similar compositions of N-glycosylated proteins in seminal plasma. Consistent composition of N-linked glycoproteins in human seminal plasma provides evidences that seminal plasma glycoproteins are of significant value to be candidates of biomarkers. Bioinformatics annotation of the identified seminal plasma glycoproteins showed that more than 43.0% of these glycoproteins are known secreted proteins according to UniProt. Such a high proportion of secreted glycoproteins in seminal plasma may play important roles in seminal plasma function such as making sure for sperm nutrition and function.

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