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14-kDa Phosphohistidine Phosphatase is a Potential Therapeutic Target for Liver Fibrosis

ABSTRACT: 14-kDa Phosphohistidine Phosphatase is a Potential Therapeutic Target for Liver Fibrosis

PROVIDER: PRJNA662894 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR12623444_1.fastq.gz	Fastqsanger.gz
	SRR12623444_2.fastq.gz	Fastqsanger.gz
	SRR12623445_1.fastq.gz	Fastqsanger.gz
	SRR12623445_2.fastq.gz	Fastqsanger.gz
	SRR12623446_1.fastq.gz	Fastqsanger.gz

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14-kDa Phosphohistidine Phosphatase is a Potential Therapeutic Target for Liver Fibrosis

Project description:Liver fibrosis, a major cause of morbidity and mortality worldwide, leads to liver damage, seriously threatening human health. In our previous study, we demonstrated that 14-kDa phosphohistidine phosphatase (PHP14) was upregulated in fibrotic liver tissue and involved in the migration and lamellipodia formation of hepatic stellate cells (HSCs). In this study, we evaluated PHP14 as a therapeutic target for liver fibrosis and investigated the mechanism by which it mediates liver fibrosis. AAV-Phpt1 administration significantly attenuates CCl4-induced liver fibrosis in mice. In particular, fibrosis-associated inflammatory infiltration was significantly suppressed after PHP14 knockdown. Mechanistically, PHP14 regulated macrophage recruitment, infiltration and migration by affecting podosome formation of macrophages. Inhibition of PHP14 decreased the expression of the fibrogenic signature at the early stage of liver fibrogenesis and the activation of HSCs in vivo. Thus, PHP14 can be considered a potential therapeutic target for liver fibrosis.

2021-07-01 | GSE157814 | GEO

Transcription profiling of IMR32 cells expressing 69-kDa or 82-kDa CHAT proteins

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A novel role for 14-kDa phosphohistidine phosphatase in lamellipodia formation.

Project description:Cell migration involves dynamic regulation of the actin cytoskeleton, which exhibits rapid actin polymerization at the leading edge of migrating cells. This process relies on regulated recruitment of actin nucleators and actin-binding proteins to the leading edge to polymerize new actin filaments. Many of these proteins have been identified, including the actin-related protein (Arp) 2/3 complex, which has emerged as the core player in the initiation of actin polymerization. However, the functional coordination of these proteins is unclear. Previously, we have demonstrated that the 14-kDa phosphohistidine phosphatase (PHP14) is involved in cell migration regulation and affects actin cytoskeleton reorganization. Here, we show that PHP14 may regulate actin remodeling directly and play an important role in dynamic regulation of the actin cytoskeleton. We observed a colocalization of PHP14 with Arp3 and F-actin at the leading edge of migrating cells. Moreover, PHP14 was recruited to the actin remodeling sites in parallel with Arp3 during lamellipodia formation. Furthermore, PHP14 knockdown impaired Arp3 localization at the leading edge of lamellipodia, as well as lamellipodia formation. Most importantly, we found that PHP14 was a novel F-actin-binding protein, displaying an Arp2/3-dependent localization to the leading edge. Collectively, our results indicated a crucial role for PHP14 in the dynamic regulation of the actin cytoskeleton and cell migration.

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