Fig. 3: Endogenous NRP1 localizes at intercellular contacts and interacts with cell adhesion receptors in ECs. | Nature Communications

Fig. 3: Endogenous NRP1 localizes at intercellular contacts and interacts with cell adhesion receptors in ECs.

From: Neuropilin 1 and its inhibitory ligand mini-tryptophanyl-tRNA synthetase inversely regulate VE-cadherin turnover and vascular permeability

Fig. 3

a, b NRP1 co-localizes with VE-cadherin and PECAM1 at endothelial intercellular contacts. Confocal microscopy analysis of endogenous NRP1 (magenta) and VE-cadherin (a) and PECAM1 (b) (green) in cultured ECs. Scale bar is 10 µm. c, d NRP1 co-immunoprecipitates with VE-cadherin and PECAM1 intercellular adhesion receptors. Co-immunoprecipitation of endogenous NRP1 and VE-cadherin (c) and PECAM1 (d) from lysates of cultured ECs that were previously incubated live with the mouse mAb (R&D Systems—MAB3870) recognizing the extracellular domain of human NRP1 or control mouse IgGs (Ctrl). A representative experiment out of five (c) or four (d) is shown. e Pull-down experiments further confirm VE-cadherin as a NRP1 binding partner. Representative western blot analysis (out of three biological replicates) of in vitro pull-down assay in which NRP1-Fc-tagged bound to an agarose-conjugated anti-NRP1 antibody was incubated with recombinant VE-cadherin-Fc-tagged or Fc alone. Source data are provided as Source Data file.

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