Dataset Information

Proteome analysis of serum proteins enriched by MOA and PSL1a

ABSTRACT: We conducted serum protein enrichment using Marasmius oreades agglutinin (MOA) and Polyporus squamosus lectin (PSL1a), followed by analysis using HF-X.

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Yusuke Kawashima

PROVIDER: PXD051875 | JPOST Repository | Wed Apr 30 00:00:00 BST 2025

REPOSITORIES: jPOST

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Dataset's files

Source:

			Action	DRS
	DIA-T60-Serum_MOA.mzML	Mzml
	DIA-T60-Serum_MOA.raw	Raw
	DIA-T60-Serum_PSL1a.mzML	Mzml
	DIA-T60-Serum_PSL1a.raw	Raw
	DIA-T60_37Lectins-TOP14D_report.pg_matrix.tsv	Tabular

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Publications

Proteome Analysis of Serum Purified Using <i>Solanum tuberosum</i> and <i>Lycopersicon esculentum</i> Lectins.

Nakajima Daisuke D Konno Ryo R Miyashita Yasuomi Y Ishikawa Masaki M Ohara Osamu O Kawashima Yusuke Y

International journal of molecular sciences 20240121 2

Serum and plasma exhibit a broad dynamic range of protein concentrations, posing challenges for proteome analysis. Various technologies have been developed to reduce this complexity, including high-abundance depletion methods utilizing antibody columns, extracellular vesicle enrichment techniques, and trace protein enrichment using nanobead cocktails. Here, we employed lectins to address this, thereby extending the scope of biomarker discovery in serum or plasma using a novel approach. We enrich ...[more]

PMID: 38279312

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Project description:Objectives: Hashimoto’s thyroiditis (HT) is one of the most common autoimmune disorders; however, its underlying pathological mechanisms remain unclear. Although aberrant glycosylation has been implicated in the N-glycome of immunoglobulin G (IgG), changes in serum proteins have not been comprehensively characterized. This study aimed to investigate the glycosylation profile of serum samples of HT patients that were depleted of highly abundant proteins by and propose the potential functions of glycoproteins for the further study of pathological mechanisms of HT . Methods: A lectin microarray containing 70 lectins was used to detect and analyze glycosylation of serum proteins using serum samples (N=27 HT; N=26 healthy control [HC]) depleted of abundant proteins. Significant differences in glycosylation status between HT patients and the HC group were verified by lectin blot analysis. A lectin-based pull-down assay combined with mass spectrometry was used to investigate potential glycoproteins combined with differentially present lectins, and an enzyme-linked immunosorbent assay (ELISA) was used to identify the expression of targeted glycoproteins in 131 patients with papillary thyroid carcinoma (PTC), 131 patients with benign thyroid nodules (BTN) patients, 130 patients with HT, and 128 HCs. Results: Compared with the HC group, the majority of the lectin binding signals in HT group were weakened, while the Vicia villosa agglutinin (VVA) binding signal was increased. The difference in VVA binding signals verified by lectin blotting was consistent with the results of the lectin microarray. A total of 113 potential VVA-binding glycoproteins were identified by mass spectrometry and classified by gene ontology (GO) and kyoto encyclopedia of genes and genomes (KEGG) analyses . Using ELISA, we confirmed that lactoferrin (LTF) and mannan-binding lectin-associated serine protease 1 (MASP-1) levels were elevated in the serum of patients with HT and PTC. Conclusions: Following depletion of abundant proteins, remaining serum proteins in HT patients exhibited lower glycosylation levels than those observed in HCs. An increased level of potential VVA-binding glycoproteins may play an important role in HT development. LTF and MASP-1 expression was significantly higher in the serum of HT and PTC patients, suggesting key roles played by glycosylation in pathological mechanisms underlying HT and PTC.