Figure 2
From: REG3β modifies cell tumor function by impairing extracellular vesicle uptake
REG3β interacts with EVs through its lectin domain. (a) PKH26-labeled THP1-EVs binding to plates coated with anti-REG3β antibody and saturated with 500 ng/ml of REG3β. The indicated concentrations of EVs were used. Non-specific binding was assessed in the absence of REG3β. Data are depicted as relative expression to saturation (5 ng/µl of EV) (n = 4). (b,c) PKH26-labeled EVs (1 ng/µl of EV protein) binding to plates (b) or magnetic beads (c) coated with anti-REG3β antibody and incubated with the indicated concentrations of REG3β. Data are depicted as relative expression to maximum binding (500 ng/ml of REG3β). (d) Anti-REG3β immunogold labeling of THP1-EVs incubated with REG3β (500 ng/ml). Non-specific binding was tested in the absence of REG3β. Scale bar: 200 nm. (e) Competitive assay of PKH26-labeled THP1-EVs binding to REG3β as in (B), but in the presence of 1 mg/ml mannose, 1 mg/ml mannan or 5 mM of NAG. (n = 4). ***P < 0.001 compared to non-sugar binding (F test). In all panels, data are expressed as mean ± SEM. R 2 represents goodness of fit to the one-site binding hyperbola model.
