kavain and Inflammation

kavain has been researched along with Inflammation* in 2 studies

Other Studies

2 other study(ies) available for kavain and Inflammation

ArticleYear
The involvement of Kav001 in inhibition of LPS/P. gingivalis-induced.
    Journal of cellular biochemistry, 2018, Volume: 119, Issue:7

    TNF-a is an important cytokine mediator of inflammation which suggests that inhibition of TNF activity may provide potential for clinical application. Recent data indicated that treatment of both human and mouse cells with Kavain significantly modulates P. gingivalis- and LPS-induced TNF-α expression. In order to obtain a selective analog with optimized biological activity and structural physico-chemical properties of Kavain, Kavain analogs were designed and synthesized and found one Kavain analogue (named Kav001) that is similar to Kavain but soluble and does not induce a significant toxicity. Both studies in vitro and in vivo treatment by Kav001 showed stronger biological function as compared to Kavain. Furthermore, most mouse bone marrow macrophages up-regulated Bcl-6 while down-regulating LITAF expression after treatment with Kav001 for 36 h. Consequently, this led to an extension of macrophage pseudopods due to its immune response to P.g. infection/LPS stimulation.

    Topics: Animals; Anticonvulsants; Arthritis, Experimental; Bacteroidaceae Infections; Cytokines; Inflammation; Lipopolysaccharides; Macrophages, Peritoneal; Male; Mice; Mice, Inbred C57BL; Porphyromonas gingivalis; Pyrones; Tumor Necrosis Factor-alpha

2018
Microsphere-based flow cytometry protease assays for use in protease activity detection and high-throughput screening.
    Current protocols in cytometry, 2010, Volume: Chapter 13

    This protocol describes microsphere-based protease assays for use in flow cytometry and high-throughput screening. This platform measures a loss of fluorescence from the surface of a microsphere due to the cleavage of an attached fluorescent protease substrate by a suitable protease enzyme. The assay format can be adapted to any site or protein-specific protease of interest and results can be measured in both real time and as endpoint fluorescence assays on a flow cytometer. Endpoint assays are easily adapted to microplate format for flow cytometry high-throughput analysis and inhibitor screening.

    Topics: Animals; Biotinylation; Flow Cytometry; Fluorescence Resonance Energy Transfer; Green Fluorescent Proteins; High-Throughput Screening Assays; Humans; Inflammation; Kinetics; Microspheres; Peptide Hydrolases; Peptides; Reproducibility of Results; Temperature

2010