Retracted: Emodin relieved lipopolysaccharide‐evoked inflammatory damage in WI‐38 cells by up‐regulating taurine up‐regulated gene 1

Abstract

Background: Neonatal pneumonia (NP) has a high fatality rate in neonatal illness. This research investigated the functions of emodin on lipopolysaccharide (LPS)-evoked inflammatory injury in WI-38 cells. Methods: Cell counting kit-8 (CCK-8) assay and flow cytometry were utilized for examining the impacts of LPS and emodin on viability and apoptosis, respectively. Taurine up-regulated gene 1 (TUG1) level was altered through cell transfection and investigated by reverse transcription quantitative polymerase chain reaction (RT-qPCR). Moreover, RT-qPCR, western blot and enzyme-linked immunosorbent assay (ELISA) were utilized for investigating expressions of monocyte chemoattractant protein-1 (MCP-1) and interleukin (IL)-6. Western blot was carried out for investigating the levels of Bcl-2, Bax, pro-Caspase-3, cleaved-Caspase-3 and NF-κB and p38MAPK pathway-related proteins. Results: LPS treatment restrained cell viability, enhanced apoptosis, and expressions of inflammation-related IL-6 and MCP-1. Emodin alleviated LPSevoked inflammatory injury and restrained the NF-κB and p38MAPK pathways. Furthermore, emodin positively regulated TUG1 expression and TUG1 silencing could reverse the efficacy of emodin on IL-6 and MCP-1 expressions. Finally, TUG1 regulates the expression of inflammatory factors through NF-κB and p38MAPK pathways. Conclusion: Emodin alleviated LPS-evoked inflammatory injury by raising TUG1 expression via NF-κB and p38MAPK pathways in WI-38 cells. K E Y W O R D S emodin, inflammatory damage, NF-κB and p38MAPK pathways, neonatal pneumonia, TUG1 1 | INTRODUCTION Neonatal pneumonia (NP) is the most familiar respiratory diseases in the neonatal stage. Most NP is caused by lung infections which are caused by inhalation of

Glaucocalyxin A alleviates lipopolysaccharide‑induced inflammation and apoptosis in pulmonary microvascular endothelial cells and permeability injury by inhibiting STAT3 signaling

“…*** P<0.001 vs. LPS (-) + GLA (µM) (-); ### P<0.001 vs. LPS (+) + GLA (µM) (-) + Colivelin (µM) (-). ∆∆ P<0.01 and ∆∆∆ P<0.001 vs. LPS (+) + GLA (µM) ( 10 ) + Colivelin (µM) (-).…”

“…(C) Protein expression level of VE-cadherin, ZO-1 and claudin 5 in LPS-induced hPMVECs co-treated with GLA and colivelin was analyzed using western blot analysis. *** P<0.001 vs. LPS (-) + GLA (µM) (-); ### P<0.001 vs. LPS (+) + GLA (µM) (-) + Colivelin (µM) (-); ∆ P<0.05, ∆∆ P<0.01 and ∆∆∆ P<0.001 vs. LPS (+) + GLA (µM) ( 10 ) + Colivelin (µM) (-). hPMVECs, human pulmonary microvascular endothelial cells; GLA, glaucocalyxin A; LPS, lipopolysaccharide; VE-cadherin, vascular endothelial cadherin; ZO-1, zonula occludens-1.…”

“…The protein expression level of p-STAT3, STAT3 and ERS-related protein expression in LPS-induced hPMVECs co-treated with GLA and colivelin was analyzed using western blot analysis and subsequently quantified using densitometry. *** P<0.001 vs. LPS (-) + GLA (µM) (-); ### P<0.001 vs. LPS (+) + GLA (µM) (-) + Colivelin (µM) (-); ∆∆ P<0.01, ∆∆∆ P<0.001 vs. LPS (+) + GLA (µM) ( 10 ) + Colivelin (µM) (-). hPMVECs, human pulmonary microvascular endothelial cells; GLA, glaucocalyxin A; LPS, lipopolysaccharide; p, phosphorylated, ERS, endoplasmic reticulum stress; ATF6, activating transcription factor 6; CHOP, C/EBP-homologous protein; STAT3, signal transducer and activator of transcription 3; GRP78, glucose regulated protein 78.…”

“…Thus, current research should focus on the mechanisms underlying the inflammatory response and aim to identify novel treatment options for pneumonia. Emerging evidence has indicated that inflammation-related proteins, including TNF-α, IL-1β and IL-6, as well as apoptosis-related proteins Bcl-2 and Bax, were associated with LPS-induced acute pneumonia (7)(8)(9)(10).…”

Advances in the study of emodin: an update on pharmacological properties and mechanistic basis

“…Additionally, the down-regulated expressions of Notch 1, Notch 2, Notch3, and the repressed phosphorylation of p65 and NF-κB induced by emodin were markedly reversed after TUG1 knockdown by transfection with sh-TUG1, which further consolidated the argument [ 33 ]. A most recent study in human fibroblasts cell line (WI-38) further demonstrated that emodin (5–20 μM) enhanced TUG1 expression and alleviated the LPS-evoked inflammatory damage via restraining the NF-κB and p38MAPK pathways [ 34 ].…”