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Oligomeric human Aβ1-42 inhibits antigen presentation

ABSTRACT: Oligomeric human Aβ1-42 inhibits antigen presentation

PROVIDER: PRJNA563674 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR10060872.fastq.gz	Fastqsanger.gz
	SRR10060873.fastq.gz	Fastqsanger.gz
	SRR10060874.fastq.gz	Fastqsanger.gz
	SRR10060875.fastq.gz	Fastqsanger.gz
	SRR10060876.fastq.gz	Fastqsanger.gz

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Oligomeric human Aβ1-42 inhibits antigen presentation

Project description:The goal of this study is to investigate the involvement of inflammation in Alzheimer’s disease (AD) and to clarify the signaling pathways involved in the presence of beta-amyloidosis, a hallmark of AD pathogenesis, to help identifying potential targets for therapy. To do that, we isolated bone marrow-derived progenitor cells from femurs, tibiae and hip bones of non-transgenic C57BL/6 mice according to established protocols , and we maturated them with LPS. To obtain an unbiased view of gene regulation in mouse bone marrow-derived dendritic cells (BM-DCs) exposed to pre-aggregated beta-amyloid peptide (Aβ) oligomers, we analyzed the transcriptome of untreated immature control BM-DCs (‘Ctrl’), LPS-treated BM-DCs (’LPS’), Aβ1-42 oligomer-treated BM-DCs (‘Aβ‘) and BM-DCs treated with Aβ1-42 oligomers and LPS (‘Aβ+LPS‘) via explorative RNA-sequencing.

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KDM5A inhibits anti-tumor immune response through downregulation of antigen presentation pathway in ovarian cancer [RNA-seq]

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KDM5A inhibits anti-tumor immune response through downregulation of antigen presentation pathway in ovarian cancer

Project description:KDM5A inhibits anti-tumor immune response through downregulation of antigen presentation pathway in ovarian cancer

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Increased antigen cross-presentation but impaired cross-priming after activation of PPARÎ³

Project description:Increased antigen cross-presentation but impaired cross-priming after activation of PPARÎ³ is mediated by up-regulation of B7H1 Dendritic cells (DCs) are able to take up exogenous antigens and present antigen-derived peptides on MHC class I molecules, a process termed cross-presentation. The mannose receptor (MR), an endocytic receptor expressed on a variety of antigen-presenting cells (APCs), has been demonstrated to target soluble antigens exclusively towards cross-presentation. In this study, we investigated the role of the murine nuclear receptor peroxisome proliferator-activated receptor Î³ (PPARÎ³), a ligand-activated transcription factor with immunomodulatory properties, in MR-mediated endocytosis and cross-presentation of the model antigen ovalbumin (OVA). We could demonstrate both in vitro and in vivo that activation of PPARÎ³ resulted in increased MR expression, which in consequence led to enhanced MR-mediated endocytosis and elevated cross-presentation of soluble OVA. Concomitantly, activation of PPARÎ³ in DCs induced up-regulation of the co-inhibitory molecule B7H1, which, despite enhanced cross-presentation, caused an impaired activation of naive OVA-specific CD8+ T cells and the induction of T cell tolerance. These data provide a mechanistic basis for the immunomodulatory action of PPARÎ³ which might open new possibilities in development of therapeutical approaches aimed at the control of excessive immune responses, e.g. in T cell-mediated autoimmunity. Comparison of murine mannose receptor negative versus mannose receptor positive bone marrow-derived DCs

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