Dataset Information

Binding proteins for the GA-modified proteins in mouse serum.

ABSTRACT: We determined if the glycolaldehyde (GA)-modified proteins could show an affinity with serum proteins. The mouse serum was incubated with the ligand-coupled beads for 1 h at room temperature. The ligands used were BSA and GA-treated BSA (GA-BSA). The proteins bound to the beads were eluted and separated by SDS-PAGE. Seven unique bands detected in the pull-down with the GA-BSA ligands were processed for tryptic digestion and LC-MS/MS analysis.

ORGANISM(S): Mus Musculus (mouse)

SUBMITTER: Koji Uchida

PROVIDER: PXD018423 | JPOST Repository | Wed Apr 08 00:00:00 BST 2020

REPOSITORIES: jPOST

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Dataset's files

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			Action	DRS
	190416chika01_0419DS60_2ul.mzML	Mzml
	190416chika01_0419DS60_2ul.raw	Raw
	190416chika01_0419DS60_2ul_uMM17_pSTY_PSM.xlsx	Xlsx
	190416chika02_0419DS60_2ul.mzML	Mzml
	190416chika02_0419DS60_2ul.raw	Raw

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Publications

Glycolaldehyde is an endogenous source of lysine N-pyrrolation.

Chikazawa Miho M Yoshitake Jun J Lim Sei-Young SY Iwata Shiori S Negishi Lumi L Shibata Takahiro T Uchida Koji K

The Journal of biological chemistry 20200423 22

Lysine N-pyrrolation converts lysine residues to Nϵ-pyrrole-l-lysine (pyrK) in a covalent modification reaction that significantly affects the chemical properties of proteins, causing them to mimic DNA. pyrK in proteins has been detected in vivo, indicating that pyrrolation occurs as an endogenous reaction. However, the source of pyrK remains unknown. In this study, on the basis of our observation in vitro that pyrK is present in oxidized low-density lipopr ...[more]

PMID: 32332094

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Project description:The receptors engaged during phagocytic particle uptake determine the signaling events that occur during phagosome formation and maturation. However, pathogens generally have multiple ligands, making it difficult to dissect the roles of individual receptors in these processes. Here, we used latex beads coupled to single ligands, focusing on IgG, mannan, LPS and avidin, and monitored phagocytic uptake rates, phago-lysosomal fusion events, macrophage gene expression and the proteomic composition of isolated phagosomes. The pattern of gene expression and the protein composition of isolated phagosomes showed that each bead ligand altered a distinct pattern of genes and led to a different composition of phagosomes. These data argue that activation of each receptor initiates a specific signature of signaling events that last many hours and influences several phagocytosis functions. All samples and controls were carried out in triplicates. J774.A1 cells (mouse macrophage-like cell line) were seeded onto 6-well plates one day before the experiment. Subsequently, cells were incubated with serum-free DME medium containing 0.01 % latex beads of 1 Âµm diameter coupled to the following ligands: avidin (Av), the Fc fragment of mouse IgG (Fc), lipopolysaccharides from Klebsiella pneumoniae (LPS) and mannan from Saccharomyces cerevisae (Man) for 30 and 60 minutes. After incubation, samples as well as untreated controls were washed twice in PBS and total RNA was extracted using RNeasy kit (Qiagen) following manufacturer's instructions. Each sample was hybridized to CodeLink Mouse whole genome bioarray slides (Amersham). This study was intended to analyze the role of receptor-ligand interactions on phagosome maturation and gene expression after receptor-mediated phagocytosis in macrophages. CodeLink EXP v4.0-processed data are represented in the Sample tables, GeneSpring-processed data are linked as a supplementary files to the matrix table, additional results available as a supplementary file on the Series record. http://www.biologie.uni-rostock.de/tierphysiologie/agkuznetsov.html

Dataset Information

Binding proteins for the GA-modified proteins in mouse serum.

Dataset's files

Publications

Glycolaldehyde is an endogenous source of lysine <i>N</i>-pyrrolation.

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