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LPS-induced systemic inflammation is suppressed by the PDZ motif peptide of ZO-1 via regulation of macrophage M1/M2 polarization

ABSTRACT: LPS-induced systemic inflammation is suppressed by the PDZ motif peptide of ZO-1 via regulation of macrophage M1/M2 polarization

PROVIDER: PRJNA1152345 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR30397312_1.fastq.gz	Fastqsanger.gz
	SRR30397312_2.fastq.gz	Fastqsanger.gz
	SRR30397313_1.fastq.gz	Fastqsanger.gz
	SRR30397313_2.fastq.gz	Fastqsanger.gz
	SRR30397314_1.fastq.gz	Fastqsanger.gz

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LPS-induced systemic inflammation is suppressed by the PDZ motif peptide of ZO-1 via regulation of macrophage M1/M2 polarization

Project description:The gram-negative bacterium lipopolysaccharide (LPS) is frequently administered to generate models of systemic inflammation. In particular, both kidney and lung are more sensitive to acute injury caused by LPS-induced systemic inflammation. However, there are several side effects and no effective treatment for LPS-induced systemic inflammation. PEGylated PDZ peptide was based on the first PDZ domain of the zonula occludens-1 (ZO-1) protein. PEGylated PDZ peptide was analyzed for effects on systemic inflammation induced by LPS. PDZ peptide administration led to restoration of tissue injuries (kidney, liver, and lung) and prevented alterations in biochemical plasma markers. The production of pro-inflammatory cytokines was significantly decreased in the plasma and lung BALF in the PDZ-administered mice. Flow cytometry analysis revealed the PDZ peptide significantly inhibited inflammation, mainly by decreasing the population of M1 macrophages, neutrophils (immature and mature), and increasing M2 macrophages. Using RNA sequencing analysis, the expression levels of the NF-κB-related proteins were lower in PDZ-treated cells than in LPS-treated cells. In addition, wild-type PDZ peptide significantly increased mitochondrial membrane integrity and decreased LPS-induced mitochondria fission. Interestingly, PDZ peptide dramatically could reduce LPS-induced NF-κB signaling, ROS production, and the expression of M1 macrophage marker proteins, but increased the expression of M2 macrophage marker proteins. These results indicated that PEGylated PDZ peptide inhibits LPS-induced systemic inflammation, reducing tissue injuries and reestablishing homeostasis and may be a therapeutic candidate against systemic inflammation.

2024-09-15 | GSE275635 | GEO

LPS-induced systemic inflammation is suppressed by the PDZ motif peptide of ZO-1 <i>via</i> regulation of macrophage M1/M2 polarization.

Project description:The gram-negative bacterium lipopolysaccharide (LPS) is frequently administered to generate models of systemic inflammation. However, there are several side effects and no effective treatment for LPS-induced systemic inflammation. PEGylated PDZ peptide based on zonula occludens-1 (ZO-1) was analyzed for its effects on systemic inflammation induced by LPS. PDZ peptide administration led to the restoration of tissue injuries (kidney, liver, and lung) and prevented alterations in biochemical plasma markers. The production of pro-inflammatory cytokines was significantly decreased in the plasma and lung BALF in the PDZ-administered mice. Flow cytometry analysis revealed the PDZ peptide significantly inhibited inflammation, mainly by decreasing the population of M1 macrophages, and neutrophils (immature and mature), and increasing M2 macrophages. Using RNA sequencing analysis, the expression levels of the NF-κB-related proteins were lower in PDZ-treated cells than in LPS-treated cells. In addition, wild-type PDZ peptide significantly increased mitochondrial membrane integrity and decreased LPS-induced mitochondria fission. Interestingly, PDZ peptide dramatically could reduce LPS-induced NF-κB signaling, ROS production, and the expression of M1 macrophage marker proteins, but increased the expression of M2 macrophage marker proteins. These results indicated that PEGylated PDZ peptide inhibits LPS-induced systemic inflammation, reducing tissue injuries and reestablishing homeostasis, and may be a therapeutic candidate against systemic inflammation.

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[SUPPRESSED]

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Potential peptide drug with LCCL core motif differentiating M1 macrophage

Project description:Cochlin, encoded by the COCH gene, mediates innate immunity against bacterial infections by segregating pathogens and recruiting immune cells through its N-terminal LCCL domain. This domain is cleaved and secreted to attract macrophages and neutrophils, but its core motif has remained unclear. Here, we identified a 62–amino acid core LCCL (cLCCL) containing conserved structural elements. RNA-seq in RAW264.7 cells showed that both LCCL and cLCCL peptides induced M1 polarization, with upregulation of TICAM2, CD40, and CD86. Thus, cLCCL drives pro-inflammatory macrophage polarization and represents a promising candidate for antibacterial peptide therapeutics

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Gene expression profile associated with the PDZ ligand-motif of HPV16-E6 oncoprotin in the skin of transgenic mice models

Project description:The K14E6 transgenic mice developskin hyperplasia,benign tumors and skin cancer. The tumor formation capacity diminishes when E6 lacks its PDZ ligand-motif. This study aims to compare the transciptional profiles of transgenic K14E6 mice with K14E6 Δ146-151 (lacking the PDZ domain) in order to explore the role of PDZ in early skin carcinogenesis. Skin tissue from three different strains of mice were dissected for RNA extraction, processing and hybridization in Affymetrix Mouse Genome 430 2,0 array. We processed three biological replicates per strain. 3 mice were used for each replicate pool for a final RNA concentration of 3 micrograms. The arrays were analyzed using Partek Genomics suite software.

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Potential peptide drug with LCCL core motif differentiating M1 macrophage

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p120 RasGAP and ZO-2 promote the tumor suppressor function of p190A RhoGAP

Project description:ARHGAP35 encoding p190A RhoGAP (p190A) was identified by GWAS as a major human cancer gene. Our published studies have determined that p190A is a tumor suppressor that activates the canonical Hippo pathway. To elucidate how p190A signals in this context, we performed mass spectrometry to identify p190A binding proteins. Two interactors were identified significantly more frequently than others: p120 RasGAP (p120) and ZO-1. Originally p190A was cloned via its direct binding to p120, hence validating our approach. In addition, we found that p190A also binds to ZO-2. The interaction of p190A with ZO-2 is dependent on p120, thus suggesting formation of a ternary complex. Next, we determine that both p120 and ZO-2, but not ZO-1, are necessary for p190A to activate LATS kinases and suppress tumorigenesis in a xenograft mouse model. Moreover, the interactions with p120 and ZO-2 are essential for transcriptional modulation by p190A, including the CDH1 gene encoding E-cadherin, which we previously have demonstrated is essential for p190A signaling. Collectively, this work identifies a novel tumor suppressor interactome of p190A, which includes ZO-2, an established constituent of the Hippo pathway, and p120, which in spite of its strong association with Ras signaling, is essential for p190A to activate LATS kinases.

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