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Prolyl endopeptidase-mediated transcriptional regulation in quiescent and activated bone marrow-derived macrophages

ABSTRACT: Prolyl endopeptidase-mediated transcriptional regulation in quiescent and activated bone marrow-derived macrophages

PROVIDER: PRJNA878832 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR21505700_1.fastq.gz	Fastqsanger.gz
	SRR21505700_2.fastq.gz	Fastqsanger.gz
	SRR21508127_1.fastq.gz	Fastqsanger.gz
	SRR21508127_2.fastq.gz	Fastqsanger.gz
	SRR21508128_1.fastq.gz	Fastqsanger.gz

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Prolyl endopeptidase-mediated transcriptional regulation in quiescent and activated bone marrow-derived macrophages (CUT&Tag)

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Prolyl endopeptidase-mediated transcriptional regulation in quiescent and activated bone marrow-derived macrophages (Bulk RNA-seq)

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Prolyl endopeptidase-mediated transcriptional regulation in quiescent and activated bone marrow-derived macrophages (CUT&Tag)

Project description:Liver fibrosis, a pathogical change commonly existing in various chronic liver diseases, can ultimately develop into life-threatening liver cirrhosis, but effective antifibrotic therapy is absent due to limited understanding of fibrogenic process. The characteristic fibrotic scar in fibrosis is stiff and disorganized extracellular matrix (ECM) yielded by ECM remodeling, a pathogenic process with vigorous participation of aberrantly activated macrophages. Prolyl endopeptidase (PREP) is a dipeptidyl peptidase that possess both proteolytic and non-proteolytic functions. Using Prep knockout mouse, we found aggravated liver fibrosis in a NASH-related fibrosis murine model, as well as significantly altered transcriptome by in vitro M1/M2 polarization in primary macrophages after PREP ablation. Most importantly, a PREP-mediated direct transcriptional regulation to active cis-regulatory genomic regions was identified for the first time as a novel non-proteolytic function of PREP, based on significant nuclear localization of PREP and CUT&Tag-seq results. Among the PREP-downstream genes, Ctsb and Ctsd, genes encoding ECM remodeling-related profibrogenic cathepsin B and D respectively, were excessively expressed in PREP-ablated macrophages in vitro and in vivo. Our results indicates that PREP is a newly found transcriptional regulator in macrophage, and is a promising therapeutic target for fibrosis-related aberrant macrophage activation.

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Prolyl endopeptidase-mediated transcriptional regulation in quiescent and activated bone marrow-derived macrophages (Bulk RNA-seq)

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Prolyl endopeptidase-mediated transcriptional regulation in quiescent and activated bone marrow-derived macrophages

Project description:This SuperSeries is composed of the SubSeries listed below.

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Bone Marrow Transplantation in Treating Patients With Hematologic Cancer

Project description:RATIONALE: Radiation therapy uses high-energy x-rays to damage cancer cells. Drugs used in chemotherapy use different ways to stop cancer cells from dividing so they stop growing or die. Combining chemotherapy with bone marrow transplantation may allow the doctor to give higher doses of chemotherapy drugs and kill more tumor cells. PURPOSE: Phase II trial to study the effectiveness of bone marrow transplantation in treating patients who have hematologic cancer.

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Quiescent vs. Activated Endothelial Cell-Derived Extracellular Vesicles

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Induced-fit mechanism for prolyl endopeptidase.

Project description:Prolyl peptidases cleave proteins at proline residues and are of importance for cancer, neurological function, and type II diabetes. Prolyl endopeptidase (PEP) cleaves neuropeptides and is a drug target for neuropsychiatric diseases such as post-traumatic stress disorder, depression, and schizophrenia. Previous structural analyses showing little differences between native and substrate-bound structures have suggested a lock-and-key catalytic mechanism. We now directly demonstrate from seven structures of Aeromonus punctata PEP that the mechanism is instead induced fit: the native enzyme exists in a conformationally flexible opened state with a large interdomain opening between the beta-propeller and alpha/beta-hydrolase domains; addition of substrate to preformed native crystals induces a large scale conformational change into a closed state with induced-fit adjustments of the active site, and inhibition of this conformational change prevents substrate binding. Absolute sequence conservation among 28 orthologs of residues at the active site and critical residues at the interdomain interface indicates that this mechanism is conserved in all PEPs. This finding has immediate implications for the use of conformationally targeted drug design to improve specificity of inhibition against this family of proline-specific serine proteases.

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