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Histone functions as a cell-surface receptor for AGEs

ABSTRACT: Histone functions as a cell-surface receptor for AGEs

PROVIDER: PRJNA801243 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR17786607_1.fastq.gz	Fastqsanger.gz
	SRR17786607_2.fastq.gz	Fastqsanger.gz
	SRR17786608_1.fastq.gz	Fastqsanger.gz
	SRR17786608_2.fastq.gz	Fastqsanger.gz
	SRR17786609_1.fastq.gz	Fastqsanger.gz

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Histone functions as a cell-surface receptor for AGEs

Project description:Reducing sugars can covalently react with proteins to generate a heterogeneous and complex group of compounds called advanced glycation end products (AGEs). AGEs are generally considered as pathogenic molecules, mediating a pro-inflammatory response and contributing to the development of a number of human diseases. However, the intrinsic function of AGEs remains to be elucidated. We now provide multiple lines of evidence showing that AGEs can specifically bind a cell-surface protein and regulate its functions. To identify cellular binding partners for AGEs, we used dehydroascorbic acid (DHA)-modified serum albumins as one of the AGEs to screen for binding proteins in the lipid raft fraction prepared from mouse splenocytes and identified histone localized on the cell-surface as an AGE-binding protein. Histone ubiquitously recognized AGEs, including proteins modified with glucose and its metabolites. AGEs inhibited the binding of plasminogen to the histone component H2B which functions as a cell-surface plasminogen receptor on monocytes/macrophages. Moreover, AGEs regulated the recruitment of monocytes/macrophage to the site of inflammation. Our discovery of histone as a cell-surface receptor for AGEs suggests that, beside our common concept of AGEs as danger-associated molecular patterns mediating a pro-inflammatory response, they may also be involved in the homeostatic response via binding to histone.

2022-03-31 | GSE195558 | GEO

Histone functions as a cell-surface receptor for AGEs.

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Project description:C1QTNF4 is a secreted protein that is structurally unique within the C1QTNF family, a family of proteins that have structural homology with both complement C1q and the tumor necrosis factor superfamily. The role of C1QTNF4 in immunity and inflammation remains poorly defined and a cell surface receptor has yet to be identified. Here we performed co-immunoprecipitation with subsequent mass spectrometric analysis in order to identify a cell surface receptor of C1QTNF4. We report identification of nucleolin as a cell surface binding partner of C1QTNF4. Nucleolin may serve as a docking molecule for C1QTNF4 and act in a context-dependent manner through co-receptors. Having identified nucleolin as a cell surface receptor is a further step to understanding C1QTNF4’s function in the healthy immune system.

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Potential Functions of Histone H3.3K56 Acetylation in Mammals

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Lysine-Specific Demethylase 1 Has Dual Functions as a Major Regulator of Androgen Receptor Transcriptional Activity

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