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Image Search Results
Journal: The Journal of Biological Chemistry
Article Title: Matrix metalloproteinases inactivate the proinflammatory functions of secreted moonlighting tryptophanyl-tRNA synthetase
doi: 10.1074/jbc.RA119.009584
Figure Lengend Snippet: WRS increases MMP activity in macrophage-conditioned media by a TNFα-dependent pathway. PMA-differentiated THP1-derived macrophages were treated for 24 h with recombinant human WRS (100 nm), Δ1–47 WRS (100 nm) as an analog of the MMP7 and MMP8 cleavage product, TNFα (40 ng/ml), or buffer with or without a mAb inhibitor of TNFα (infliximab (IN)) (100 ng/ml). MMPs in 20-fold–concentrated conditioned media were activated with 1 mm APMA, and cleavage of the quenched fluorescence peptide substrate Mca-Pro-Leu-Gly↓Leu-Dpa-Ala-Arg-NH2 was measured (scatter plots show means ± S.D., n = 3) in N = 3 independent experiments. Statistical significance was determined against buffer + infliximab using a one-way ANOVA with Dunnett's multiple comparison posttests. ***, p < 0.001; ns, not significant. Error bars represent S.D.
Article Snippet: To assess MMP activity in conditioned medium, THP1 M0 cells were cultured in phenol red–free, serum-free growth medium for 24 h with 10 μg/ml polymyxin B plus 100 n m WRS, TNFα 40 μg/ml, or PBS ± 100 μg/ml
Techniques: Activity Assay, Derivative Assay, Recombinant, Fluorescence, Comparison