Phosphorylated Heat Shock Protein 27 Inhibits Lipopolysaccharide-Induced Inflammation in Thp1 Cells by Promoting TLR4 Endocytosis, Ubiquitination, and Degradation

Li, Jinfei; Qi, Xiaowen; Jiang, Baolin; Huang, Ting‐Hsiang; Luo, Lan; Liu, Shixiang; Yin, Zhimin

doi:10.1007/s10753-019-01041-x

Cited by 12 publications

(8 citation statements)

References 45 publications

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“…These data suggest that TLR4 is regulated by post-translational modifications, such as ubiquitylation Abbreviations: HCC, hepatocellular carcinoma; MyD88, myeloid differentiation primary response gene 88; NF-κB, nuclear factor-κB; TLR4, toll-like receptor 4; USP13, ubiquitin specific peptidase 13. and deubiquitylation. Heat shock protein 27 (HSP27) has been identified as a regulator in facilitating endocytosis, ubiquitination, and degradation of TLR4 (Li et al, 2019). US7 and US8, which are encoded by human cytomegalovirus (HCMV), contribute to ubiquitination-mediated degradation of TLR3 and TLR4 (Park et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

Hypoxia-Inducible Ubiquitin Specific Peptidase 13 Contributes to Tumor Growth and Metastasis via Enhancing the Toll-Like Receptor 4/Myeloid Differentiation Primary Response Gene 88/Nuclear Factor-κB Pathway in Hepatocellular Carcinoma

Gao

Chen

et al. 2020

Front. Cell Dev. Biol.

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Section: Introductionmentioning

confidence: 99%

Hypoxia-Inducible Ubiquitin Specific Peptidase 13 Contributes to Tumor Growth and Metastasis via Enhancing the Toll-Like Receptor 4/Myeloid Differentiation Primary Response Gene 88/Nuclear Factor-κB Pathway in Hepatocellular Carcinoma

Gao

Chen

et al. 2020

Front. Cell Dev. Biol.

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“…Further investigations were performed to determine whether the phosphorylation state of HSP27 plays a role in PRRSV replication. KRIBB3 was used, which is a specific inhibitor that can inhibit HSP27 phosphorylation [ 19 ]. We first tested the cytotoxicity of KRIBB3 on MARC-145 cells and PAMs to determine the optimal concentration using a CCK-8.…”

Section: Resultsmentioning

confidence: 99%

HSP27 Interacts with Nonstructural Proteins of Porcine Reproductive and Respiratory Syndrome Virus and Promotes Viral Replication

et al. 2023

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Heat shock protein 27 (HSP27) is a multifunctional protein and belongs to the small HSP family. It has been shown that HSP27 is involved in viral replication as a cellular chaperone, but the function of HSP27 during porcine reproductive and respiratory syndrome virus (PRRSV) infections remains unexplored. Here, we found that PRRSV replication can induce HSP27 expression and phosphorylation in vitro. HSP27 overexpression promoted PRRSV replication, whereas its knockdown reduced PRRSV proliferation. Additionally, suppressing HSP27 phosphorylation reduced PRRSV replication and the level of viral double-stranded RNA (dsRNA), a marker of the viral replication and transcription complexes (RTCs). Furthermore, HSP27 can interact with multiple viral nonstructural proteins (nsps), including nsp1α, nsp1β, nsp5, nsp9, nsp11 and nsp12. Suppressing the phosphorylation of HSP27 almost completely disrupted its interaction with nsp1β and nsp12. Altogether, our study revealed that HSP27 plays an important role in PRRSV replication.

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“…Figure 2 shows a interaction model between e Hsp and inflammatory cytokines in both healthy pregnant patients and in the development of preeclampsia. Li et al 61 have shown that in human mononuclear cells (Thp1) transfected with the phosphorylated form of Hsp‐27 reduces the concentration of TNFα, IL‐1β and IL‐6 induced by LPS (500 ng/ml) in a dose‐dependent manner and that this effect is mediated by the inhibition of the MyD88 and IRF3 signalling pathway. 61 …”

Section: Discussionmentioning

confidence: 99%

“… 18 This environment promotes deregulation between e Hsp‐60, e Hsp‐70 and e Hsp‐27 (Figure 1 ). The importance of Hsp has been shown by cells transfected with phosphorylated form Hsp‐27 (pho‐Hsp‐27) reduced the IL‐1β and TNFα signalling pathway, 61 and by the small interfering RNA degrades Hsp‐27 mRNA increasing IL‐1 β concentration. 62 …”

Section: Discussionmentioning

confidence: 99%

“…58 Figure 2 shows a interaction model between eHsp and inflammatory cytokines in both healthy pregnant patients and in the development of preeclampsia. Li et al 61 have shown that in human mononuclear cells (Thp1) transfected with the phosphorylated form of Hsp-27 reduces the concentration of TNFα, IL-1β and IL-6 induced by LPS (500 ng/ml) in a dose-dependent manner and that this effect is mediated by the inhibition of the MyD88 and IRF3 signalling pathway. 61 Using peripheral blood mononuclear cells (PBMC), Hadadi et al 62 have shown that by inhibiting the expression of Hsp-27 with small interfering RNA the secretion of IL-1β increases up to twofold compared with the control group.…”

Section: áLvarez-cabrera Et Al Have Shown a Relationship Between Ehsp-mentioning

confidence: 99%

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First‐trimester plasma extracellular heat shock proteins levels and risk of preeclampsia

Robellada-Zárate

Luna-Palacios

Caballero

et al. 2023

J Cellular Molecular Medi

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Preeclampsia (PE) occurs annually in 8% of pregnancies. Patients without risk factors represent 10% of these. There are currently no first‐trimester biochemical markers that accurately predict PE. An increase in serum 60‐ and 70‐KDa extracellular heat shock proteins (eHsp) has been shown in patients who developed PE at 34 weeks. We sought to determine whether there is a relationship between first‐trimester eHsp and the development of PE. This was a prospective cohort study performed at a third level hospital in Mexico City from 2019 to 2020. eHsp levels were measured during the first‐trimester ultrasound in singleton pregnancies with no comorbidities. First‐trimester eHsp levels and biochemical parameters of organ dysfunction were compared between patients who developed preeclampsia and those who did not. All statistical analyses and model of correlation (r) between eHsp and clinical parameter were performed using bootstrapping R‐software. p‐values <0.05 were considered significant. The final analysis included 41 patients. PE occurred in 11 cases. eHsp‐60 and eHsp−70 were significantly higher at 12 weeks in patients who developed PE (p = 0.001), while eHsp‐27 was significantly lower (p = 0.004). Significant differences in first‐trimester eHsp concentration suggest that these are possible early biomarkers useful for the prediction of PE.

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Phosphorylated Heat Shock Protein 27 Inhibits Lipopolysaccharide-Induced Inflammation in Thp1 Cells by Promoting TLR4 Endocytosis, Ubiquitination, and Degradation

Cited by 12 publications

References 45 publications

Hypoxia-Inducible Ubiquitin Specific Peptidase 13 Contributes to Tumor Growth and Metastasis via Enhancing the Toll-Like Receptor 4/Myeloid Differentiation Primary Response Gene 88/Nuclear Factor-κB Pathway in Hepatocellular Carcinoma

Hypoxia-Inducible Ubiquitin Specific Peptidase 13 Contributes to Tumor Growth and Metastasis via Enhancing the Toll-Like Receptor 4/Myeloid Differentiation Primary Response Gene 88/Nuclear Factor-κB Pathway in Hepatocellular Carcinoma

HSP27 Interacts with Nonstructural Proteins of Porcine Reproductive and Respiratory Syndrome Virus and Promotes Viral Replication

First‐trimester plasma extracellular heat shock proteins levels and risk of preeclampsia

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