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Single-cell transcriptomics reveals natural product Shi-Bi-Man promotes hair regeneration

ABSTRACT: Single-cell transcriptomics reveals natural product Shi-Bi-Man promotes hair regeneration

PROVIDER: PRJNA806791 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR18013587.fastq.gz	Fastqsanger.gz
	SRR18013588.fastq.gz	Fastqsanger.gz
	SRR18013589.fastq.gz	Fastqsanger.gz
	SRR18013590.fastq.gz	Fastqsanger.gz
	SRR18013591.fastq.gz	Fastqsanger.gz

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Single-cell transcriptomics reveals natural product Shi-Bi-Man promotes hair regeneration

Project description:Purpose: This study aimed to explore the mechanism of SBM to promote hair regeneration through single-cell transcriptomics Methods: Supplementation with intragastric administration or smear administration of SBM in artificially shaved C57BL/6 mice to observe its hair growth. Single-cell RNA sequencing were performed to explore the role of SBM for hair regeneration. Results: SBM significantly induced hair growth compared with control treatment.The results of single-cell sequencing revealed that after SBM treatment, the number of hair follicle stem cells (HFSCs) and dermal papilla cells (DPCs) increased significantly. Cell interactions and volcano maps show that interaction of FGF signaling pathway was significantly enhanced, in which FGF7 expression was especially upregulated in DPCs. In addition, Wnt signaling pathway also had a partially enhanced effect on the interactions between various cells in the skin. Network pharmacology study showed that the promotion of FGF and Wnt pathways by SBM was also enriched in alopecia diseases. Conclusion: We report that SBM has a potential effect on the promotion of hair growth by mainly activating FGF signaling pathway. The use of SBM may be a novel therapeutic option for hair loss.

2023-02-14 | GSE196677 | GEO

Natural product Shi-Bi-Man ameliorates psoriasis via inhibiting IL-23/Th17 axis and CXCL16-mediated endothelial activation

Project description:Natural product Shi-Bi-Man ameliorates psoriasis via inhibiting IL-23/Th17 axis and CXCL16-mediated endothelial activation

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Natural product Shi-Bi-Man ameliorates psoriasis via inhibiting IL-23/Th17 axis and CXCL16-mediated endothelial activation

Project description:Purpose: We aimed to find a potential for psoriasis and to explore the mechanism of SBM to relieve psoriasis-like skin inflammation in mice. Methods: Supplementation with smear administration of SBM in the imiquimod-induced murine model, record the weight change and psoriasis Area and Severity Index (PASI) score during the whole process. Using hematoxylin-eosin staining to obverse to skin structure. Performing single-cell RNA sequencing to explore the mechanism of SBM in influencing psoriasis-like phenotype. Immunofluorescence were conducted for verification. Results: SBM remarkably alleviated the psoriasis-like phenotype. Single-cell RNA sequencing analysis shown the expression of Il17 and Il23 was diminished in keratinocytes and T cells, accompanied by a reduction in the proportion of Th17 cells. Meanwhile, endothelial cell activation was inhibited along with the expression of Cxcl16. Conclusion: In this work, we found that natural product SBM inhibited the IL-23/Th17 axis and CXCL16-mediated endothelial activation and had a good therapeutic effect on psoriasis in mice model. This work suggests the potential therapeutic value of SBM in psoriatic patients.

2023-11-21 | GSE232568 | GEO

Glycine max cultivar:Shi-shi

Project description:Glycine max cultivar:Shi-shi Raw sequence reads

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Repo-Man/PP1 regulates heterochromatin formation in interphase

Project description:Repo-Man chromatin binding sites were obtained by expression of GST:Repo-Man and incubation with nucleosomes extracted from HeLa cells (GST alone signal was used as a negative control and subtracted from the GST:Repo-Man chromatin bound fraction)

2016-11-23 | GSE84035 | GEO

Ficus religiosa isolate:SHI

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Project description:Disulfiram and niclosamide were identified as drugs that induced depletion of an MLL-AF9-luciferase fusion protein in THP-1 AML cells, in a bioluminescence sreen. MLL-fusion protein depletion was confirmed in AML and ALL cell lines expressing different MLL-fusion proteins. Combination of disulfiram with niclosamide was found to enhance depletion of MLL-fusion proteins. To investigate whether this enhanced depletion resulted in increased suppression of downstream target genes. MLL-AF6 expressing SHI-1 cells were exposed to disulfiram/copper, nciclosamide or combined drugs. SHI-1 cells were treated for 16 hours with 0.3uM disulfiram / 1uM copper, 5uM niclosamide or combined drugs and RNAseq performed on isolated RNA.

2024-07-03 | GSE262673 | GEO

Nucleocytoplasmic O-Man glycoproteome

Project description:Dynamic cycling of N-Acetylglucosamine (GlcNAc) on serine (Ser) and threonine (Thr) residues (O-GlcNAcylation) is an essential process in all eukaryotic cells except yeast, e.g Saccharomyces cerevisiae. O-GlcNAcylation modulates signaling and cellular processes in an intricate interplay with protein phosphorylation, and serves as a key sensor of nutrients by linking the hexosamine biosynthetic pathway (HBP) to cellular signaling. A longstanding conundrum has been how yeast survives without O-GlcNAcylation in light of its similar phosphorylation signaling system. We previously developed a sensitive lectin enrichment and mass spectrometry workflow for identification of the human O-Mannose (O-Man) glycoproteome, and used this to identify a pleothora of O-linked mannose glycoproteins in human cell lines including the large family of cadherins and protocadherins. Here, we applied the workflow to yeast with the aim to characterize the yeast O-Man glycoproteome, and doing so we discovered hitherto unknown O-Man glycosites on nuclear, cytoplasmic and mitochondrial proteins in Saccharomyces cerevisiae. The type of nucleocytoplasmic proteins and the localization of identified O-Man residues mirrors that of the O-GlcNAc glycoproteome in other eukaryotic cells, indicating that the two different types of O-glycosylations serve the same important biological functions. The discovery opens for exploration of the enzyme machinery that is predicted to regulate the discovered nucleocytoplasmic O-Man glycosylation. It is likely that manipulation of this type of O-Man glycosylation will have wide applications for yeast bioprocessing.

2015-12-08 | PXD002924 | Pride

C-Man peptide pulldowns from Brain

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2020-11-16 | PXD020336 | Pride

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