Colocalization of the novel plasminogen receptor, Plg‐RKT, with the epithelial sodium channel (ENaC)

TL;DRAbstract

Binding of plasminogen (Plg) to cells via specific receptors markedly enhances Plg activation, and localizes the proteolytic activity of plasmin (P) on cell surfaces. Exposure of kidney tubular cells to P results in cleavage and activation of ENaC leading to increased Na + uptake, and Na + retention in nephrotic syndrome in which Plg is present in urine. We recently isolated a novel transmembrane Plg receptor, Plg‐R KT , from macrophages. Here, we examined kidney cells for the presence and subcellular localization of Plg‐R KT as a potential component of the mechanism in which P processes ENaC. Human kidney sections were stained with specific monoclonal anti‐Plg‐R KT . Strong staining was observed in distal tubular epithelium (intensity=200–256) > proximal tubular cells (intensity=140–199) ≫ glomeruli (intensity=80–139). In western blotting of MDCK cells and M1 mouse collecting duct cells Plg‐R KT was highly expressed in membrane fractions, but was not detected in cytoplasm. Using co

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