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| dc.contributor.author | Sulistyowati, Erna | |
| dc.contributor.author | Lee, Mei-Yueh | |
| dc.contributor.author | Wu, Lin-Chi | |
| dc.contributor.author | Hsu, Jong-Hau | |
| dc.contributor.author | Dai, Zen-Kong | |
| dc.contributor.author | Wu, Bin-Nan | |
| dc.contributor.author | Lin, Ming-Chung | |
| dc.contributor.author | Yeh, Jwu-Lai | |
| dc.date.accessioned | 2021-10-14T01:47:23Z | |
| dc.date.available | 2021-10-14T01:47:23Z | |
| dc.date.issued | 2018-08-23 | |
| dc.identifier.uri | https://www.mdpi.com/1420-3049/23/9/2124 | |
| dc.identifier.uri | http://repository.unisma.ac.id/handle/123456789/2034 | |
| dc.description | [ARCHIVES] Copyright Article from: MDPI journals | en_US |
| dc.description.abstract | Heat shock cognate protein 70 (HSC70), a molecular chaperone, is constitutively expressed by mammalian cells to regulate various cellular functions. It is associated with many diseases and is a potential therapeutic target. Although HSC70 also possesses an anti-inflammatory action, the mechanism of this action remains unclear. This current study aimed to assess the anti-inflammatory effects of HSC70 in murine macrophages RAW 264.7 exposed to lipopolysaccharides (LPS) and to explain its pathways. Mouse macrophages (RAW 264.7) in 0.1 µg/mL LPS incubation were pretreated with recombinant HSC70 (rHSC70) and different assays (Griess assay, enzyme-linked immune assay/ELISA, electrophoretic mobility shift assay/EMSA, gelatin zymography, and Western blotting) were performed to determine whether rHSC70 blocks pro-inflammatory mediators. The findings showed that rHSC70 attenuated the nitric oxide (NO) generation, tumor necrosis factor α (TNF-α) and interleukin 6 (IL-6) expressions in LPS-stimulated RAW264.7 cells. In addition, rHSC70 preconditioning suppressed the activities and expressions of matrix metalloproteinase-2 (MMP-2) and MMP-9. Finally, rHSC70 diminished the nuclear translocation of nuclear factor-κB (NF-κB) and reduced the phosphorylation of extracellular-signal regulated kinases 1/2 (ERK1/2), c-Jun N-terminal kinase (JNK), p38 mitogen-activated protein kinases (MAPK), and phosphatidylinositol-3-kinase (PI3K/Akt). We demonstrate that rHSC70 preconditioning exerts its anti-inflammatory effects through NO production constriction; TNF-α, and IL-6 suppression following down-regulation of inducible nitric oxide synthase (iNOS), cyclooxygenase 2 (COX-2), and MMP-2/MMP-9. Accordingly, it ameliorated the signal transduction of MAPKs, Akt/IκBα, and NF-κB pathways. Therefore, extracellular HSC70 plays a critical role in the innate immunity modulation and mechanisms of endogenous protective stimulation. | en_US |
| dc.language.iso | en | en_US |
| dc.publisher | MDPI journals | en_US |
| dc.relation.ispartofseries | MDPI journals;Vol.23, Issue 9, Page 1-13 | |
| dc.subject | Heat Shock Protein | en_US |
| dc.subject | Llipopolysaccharide | en_US |
| dc.subject | Inflammation | en_US |
| dc.subject | RAW264.7 Macrophages | en_US |
| dc.subject | Matrix Metalloproteinases | en_US |
| dc.title | Exogenous Heat Shock Cognate Protein 70 Suppresses LPS-Induced Inflammation by Down-Regulating NF-κB through MAPK and MMP-2/-9 Pathways in Macrophages | en_US |
| dc.type | Article | en_US |
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