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Interleukin-1 promotes autoimmune neuroinflammation by suppressing endothelial heme oxygenase-1 at the blood-brain barrier

ABSTRACT: Interleukin-1 promotes autoimmune neuroinflammation by suppressing endothelial heme oxygenase-1 at the blood-brain barrier

PROVIDER: PRJNA610270 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR11237212.fastq.gz	Fastqsanger.gz
	SRR11237213.fastq.gz	Fastqsanger.gz
	SRR11237214.fastq.gz	Fastqsanger.gz
	SRR11237215.fastq.gz	Fastqsanger.gz
	SRR11237216.fastq.gz	Fastqsanger.gz

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Interleukin-1 promotes autoimmune neuroinflammation by suppressing endothelial heme oxygenase-1 at the blood-brain barrier.

Project description:The proinflammatory cytokine interleukin 1 (IL-1) is crucially involved in the pathogenesis of multiple sclerosis (MS) and its animal model experimental autoimmune encephalomyelitis (EAE). Herein, we studied the role of IL-1 signaling in blood-brain barrier (BBB) endothelial cells (ECs), astrocytes and microglia for EAE development, using mice with the conditional deletion of its signaling receptor IL-1R1. We found that IL-1 signaling in microglia and astrocytes is redundant for the development of EAE, whereas the IL-1R1 deletion in BBB-ECs markedly ameliorated disease severity. IL-1 signaling in BBB-ECs upregulated the expression of the adhesion molecules Vcam-1, Icam-1 and the chemokine receptor Darc, all of which have been previously shown to promote CNS-specific inflammation. In contrast, IL-1R1 signaling suppressed the expression of the stress-responsive heme catabolizing enzyme heme oxygenase-1 (HO-1) in BBB-ECs, promoting disease progression via a mechanism associated with deregulated expression of the IL-1-responsive genes Vcam1, Icam1 and Ackr1 (Darc). Mechanistically, our data emphasize a functional crosstalk of BBB-EC IL-1 signaling and HO-1, controlling the transcription of downstream proinflammatory genes promoting the pathogenesis of autoimmune neuroinflammation.

| S-EPMC7498485 | biostudies-literature

Interleukin-1 promotes autoimmune neuroinflammation by suppressing endothelial heme oxygenase-1 at the blood-brain barrier

Project description:The goal of this study is to study endothelial cell Il1r1 signaling in EAE (multiple scleroris)

2020-09-23 | GSE146378 | GEO

Malaria parasites require a divergent heme oxygenase for apicoplast biogenesis

Project description:Affinity purification data for Heme Oxygenase from Plasmodium falciparum

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Heme oxygenase-1 knocked down rat mesangial cells treated with hydrogen peroxide

Project description:HO-1 cells denote the cultured rat mesangial cells with heme oxygenase-1 knocked down by RNA interference (using lentiviral vector). GFP cells denote the cultured rat mesangial cells that are transfected with empty lentiviral vector containing GFP cassette. Cells are treated with hydrogen peroxide 100 micromolar for 2 hours, or without. RNA are then harvested for array analysis. Biological replicates are performed (two independent experiment sets). GFP cell and HO-1 cell are untreated, or treated with hydrogen peroxide (100 micromolar for 2 hours).

2014-01-10 | E-GEOD-53953 | biostudies-arrayexpress

The heme regulatory motifs of heme oxygenase-2 function to transfer heme to the catalytic site for degradation

Project description:Heme regulatory motifs (HRMs) are found in a variety of proteins that are involved in diverse biological functions. In the C-terminal tail region of human heme oxygenase-2 (HO2), there are two HRMs whose cysteines form a disulfide bond; when reduced, these cysteines are available to bind Fe3+-heme. Heme binding to the HRMs is independent of the HO2 catalytic active site in the core of the protein, where heme binds with high affinity and is degraded to biliverdin. Here, we describe the reversible, protein-mediated transfer of heme between the HRMs and the core of HO2. Using HDX-MS to monitor the dynamics of HO2 with and without Fe3+-heme bound to the HRMs and to the core, we detected conformational changes in the catalytic core only in one state of the catalytic cycle – when Fe3+-heme is bound to the HRMs and the core is in the apo state. The conformational changes detected are consistent with transfer of heme between binding sites. Indeed, Fe3+-heme bound to the HRMs is transferred to the apo-core upon either independently expressing the core and a construct spanning the HRM-containing tail or after single turnover of heme at the core. In addition, we observed transfer of heme from the core to the HRMs and equilibration of heme between the core and HRMs. We thus propose a Fe3+-heme transfer model in which heme bound to the HRMs is readily transferred to the catalytic site for degradation to facilitate turnover but can also equilibrate between the sites to maintain heme homeostasis.

2020-03-18 | PXD017538 | Pride

Heme oxygenase-1 knocked down rat mesangial cells treated with hydrogen peroxide

2014-01-10 | GSE53953 | GEO

Identification of Cytoprotective Small Molecule Inducers of Heme Oxygenase-1

Project description:Identification of Cytoprotective Small Molecule Inducers of Heme Oxygenase-1

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Heme oxygenase-1 and carbon monoxide suppress autoimmune neuroinflammation.

Project description:Heme oxygenase-1 (HO-1, encoded by HMOX1) dampens inflammatory reactions via the catabolism of heme into CO, Fe, and biliverdin. We report that expression of HO-1 dictates the pathologic outcome of experimental autoimmune encephalomyelitis (EAE), a model of multiple sclerosis (MS). Induction of EAE in Hmox1(-/- )C57BL/6 mice led to enhanced CNS demyelination, paralysis, and mortality, as compared with Hmox1(+/+) mice. Induction of HO-1 by cobalt protoporphyrin IX (CoPPIX) administration after EAE onset reversed paralysis in C57BL/6 and SJL/J mice and disease relapse in SJL/J mice. These effects were not observed using zinc protoporphyrin IX, which does not induce HO-1. CoPPIX protection was abrogated in Hmox1(-/-) C57BL/6 mice, indicating that CoPPIX acts via HO-1 to suppress EAE progression. The protective effect of HO-1 was associated with inhibition of MHC class II expression by APCs and inhibition of Th and CD8 T cell accumulation, proliferation, and effector function within the CNS. Exogenous CO mimicked these effects, suggesting that CO contributes to the protective action of HO-1. In conclusion, HO-1 or exposure to its end product CO counters autoimmune neuroinflammation and thus might be used therapeutically to treat MS.

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Counteraction of myocardial ferritin heavy chain deficiency by heme oxygenase-1

Project description:Counteraction of myocardial ferritin heavy chain deficiency by heme oxygenase-1

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Heme oxygenase-1 orchestrates the immunosuppressive program of tumor-associated macrophages

Project description:Heme oxygenase-1 orchestrates the immunosuppressive program of tumor-associated macrophages

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