interleukin-8 and rhein

interleukin-8 has been researched along with rhein* in 2 studies

Other Studies

2 other study(ies) available for interleukin-8 and rhein

ArticleYear
Rhein prevents endotoxin-induced acute kidney injury by inhibiting NF-κB activities.
    Scientific reports, 2015, Jul-07, Volume: 5

    This study aimed to explore the effect and mechanisms of rhein on sepsis-induced acute kidney injury by injecting lipopolysaccharide (LPS) and cecal ligation and puncture (CLP) in vivo, and on LPS-induced HK-2 cells in vitro. For histopathological analysis, rhein effectively attenuated the severity of renal injury. Rhein could significantly decrease concentration of BUN and SCr and level of TNF-α and IL-1β in two different mouse models of experimental sepsis. Moreover, rhein could markedly attenuate circulating leukocyte infiltration and enhance phagocytic activity of macrophages partly impaired at 12 h after CLP. Rhein could enhance cell viability and suppresse the release of MCP-1 and IL-8 in LPS-stimulated HK-2 cells Furthermore, rhein down regulated the expression of phosphorylated NF-κB p65, IκBα and IKKβ stimulated by LPS both in vivo and in vitro. All these results suggest that rhein has protective effects on endotoxin-induced kidney injury. The underlying mechanism of rhein on anti-endotoxin kidney injury may be closely related with its anti-inflammatory and immunomodulatory properties by decreasing NF-κB activation through restraining the expression and phosphorylation of the relevant proteins in NF-κB signal pathway, hindering transcription of NF-κB p65.These evidence suggest that rhein has a potential application to treat endotoxemia-associated acute kidney injury.

    Topics: Acute Kidney Injury; Animals; Anthraquinones; Blood Urea Nitrogen; Cell Line; Creatine; Disease Models, Animal; I-kappa B Kinase; I-kappa B Proteins; Immunohistochemistry; Interleukin-1beta; Interleukin-8; Kidney; Lipopolysaccharides; Macrophages; Mice; Mice, Inbred BALB C; NF-kappa B; NF-KappaB Inhibitor alpha; Phosphorylation; Sepsis; Signal Transduction; Transcription Factor RelA; Transcription, Genetic; Tumor Necrosis Factor-alpha

2015
Effects of rhein on human articular chondrocytes in alginate beads.
    Biochemical pharmacology, 2003, Feb-01, Volume: 65, Issue:3

    This study was designed to investigate the effects of rhein, the active metabolite of diacerhein, on the metabolic functions of human chondrocytes cultured in alginate beads. Enzymatically isolated osteoarthritic (OA) chondrocytes were cultured in alginate beads in a well-defined culture medium for 12 days. Rhein was tested in a range of concentrations comprised between 10(-7) and 4 x 10(-5)M, in the presence or absence of 10(-10)M IL-1beta. Interleukin (IL)-6 and -8, macrophage inflammatory protein (MIP-1beta), stromelysin-1 (MMP-3), aggrecan (AGG), tissue inhibitor of metalloproteinases-1 (TIMP-1), prostaglandin E(2) (PGE(2)) and nitric oxide (NO) productions were assayed. Cyclooxygenase-2 (COX-2) and inducible NO synthase (iNOS) mRNA steady-state levels were also quantified. In the basal condition, 10(-5)M rhein increased by 46.5% the production of AGG, decreased by 17-30% the production of IL-6, MMP-3, NO and MIP-1beta but enhanced by 50% the production of PGE(2). IL-1beta increased IL-6, IL-8, MIP-1beta, NO, PGE(2) and MMP-3 productions, but inhibited AGG and TIMP-1 synthesis. Rhein partially reversed the effect of IL-1beta on TIMP-1 and NO production, had no effect on AGG, IL-6 and MIP-1beta production, but up-regulated the IL-1beta stimulated PGE(2) production. The COX-2 and iNOS mRNA levels and IL-8 production were not modified by rhein.Overall, these results contribute to explain the clinical efficiency of rhein and give new information on its mechanisms of action.

    Topics: Aggrecans; Anthraquinones; Chemokine CCL4; Chondrocytes; Dinoprostone; DNA; Enzyme Inhibitors; Extracellular Matrix Proteins; Humans; Interleukin-6; Interleukin-8; L-Lactate Dehydrogenase; Lectins, C-Type; Macrophage Inflammatory Proteins; Matrix Metalloproteinase 3; Mixed Function Oxygenases; Nitric Oxide; Proteoglycans; Tissue Inhibitor of Metalloproteinase-1

2003