Lung adenocarcinoma (LUAD) is the most common histological subtype of nonsmall-cell lung cancer. Herein, a multiomics method, which combined proteomic and N-glycoproteomic analyses, was developed to analyze the normal and cancerous bronchoalveolar lavage fluids (BALFs) from six LUAD patients to identify potential biomarkers of LUAD. The data-independent acquisition proteomic analysis was first used to analyze BALFs, which identified 59 differentially expressed proteins (DEPs). The bioinformatic analyses of 59 DEPs have shown that a potential marker protein, beta-1,4-galactosyltransferase 1 (B4GALT1), was consistently downregulated in all cancerous lung lobes (CLLs). As the downregulation of B4GALT1 may indicate changes in protein N-glycosylation, site-specific N-glycoproteome analysis of BALFs from the normal lung lobes (NLLs) and CLLs was further performed by using a fully automated glycopeptide enrichment and separation system. Comparing the glycan structures containing free GlcNAc in BALFs between NLLs and CLLs qualitatively, the percentage of unique glycan structure for free GlcNAc existing only in NLLs was 52.8%, which was significantly higher than the 46.3% existing only in CLLs. Furthermore, the sequential proteomic and N-glycoproteomic analyses allowed us to identify a panel of functionally related potential biomarkers consisting of one protein (B4GALT1) and four glycoproteins (NFKB1, F2, LTF, and DLD).
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1021/acs.jproteome.4c00845 | DOI Listing |
J Proteome Res
January 2025
The First Affiliated Hospital of Ningbo University, Ningbo315010, P.R. China.
Lung adenocarcinoma (LUAD) is the most common histological subtype of nonsmall-cell lung cancer. Herein, a multiomics method, which combined proteomic and N-glycoproteomic analyses, was developed to analyze the normal and cancerous bronchoalveolar lavage fluids (BALFs) from six LUAD patients to identify potential biomarkers of LUAD. The data-independent acquisition proteomic analysis was first used to analyze BALFs, which identified 59 differentially expressed proteins (DEPs).
View Article and Find Full Text PDFJ Proteome Res
December 2024
Department of Chemistry, Yale University, New Haven, Connecticut 06511, United States.
Protein glycosylation is a complex post-translational modification that is generally classified as N- or O-linked. Site-specific analysis of glycopeptides is accomplished with a variety of fragmentation methods, depending on the type of glycosylation being investigated and the instrumentation available. For instance, collisional dissociation methods are frequently used for N-glycoproteomic analysis with the assumption that one N-sequon exists per tryptic peptide.
View Article and Find Full Text PDFPhenomics
June 2024
Mass Spectrometry Engineering Technology Research Center, Center for Advanced Measurement Science, National Institute of Metrology, Beijing, 102206 China.
Glycobiology
September 2024
Department of Laboratory Medicine and Pathology, Mayo Clinic, 200 First Street SW, Rochester, Minnesota 55905, United States.
SRD5A3-CDG is a congenital disorder of glycosylation (CDG) resulting from pathogenic variants in SRD5A3 and follows an autosomal recessive inheritance pattern. The enzyme encoded by SRD5A3, polyprenal reductase, plays a crucial role in synthesizing lipid precursors essential for N-linked glycosylation. Despite insights from functional studies into its enzymatic function, there remains a gap in understanding global changes in patient cells.
View Article and Find Full Text PDFPoult Sci
December 2024
Institute for Egg Science and Technology, School of Food and Biological Engineering, Chengdu University, Chengdu, 610106, China. Electronic address:
Chicken egg yolk plasma (EYP), the supernatant fraction of egg yolk obtained by water dilution and centrifugation, is a rich source of various bioactive substances and a significant bearer of yolk-emulsifying properties. This study utilized proteomics to conduct a comprehensive and in-depth analysis of both common and modified EYP proteins (phosphorylated proteins and N-glycosylated proteins). Total of 208 proteins were identified in EYP, including 42 phosphorylated proteins with 137 phosphorylation sites and 150 N-glycoproteins with 332 N-glycosylation sites.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!