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The 37/67 kDa laminin receptor (LR) is a non-integrin protein, which binds both laminin-1 of the extracellular matrix and prion proteins, that hold a central role in prion diseases. The 37/67 kDa LR has been identified as interactor for the prion protein (PrP C ) and to be required for pathological PrP (PrP Sc ) propagation in scrapie-infected neuronal cells, leading to the possibility that 37/67 kDa LR-PrP C  interaction is related to the pathogenesis of prion diseases. A relationship between 37/67 kDa LR and PrP C  in the presence of specific LR inhibitor compounds has not been investigated yet. We have characterized the trafficking of 37/67 kDa LR in both neuronal and non-neuronal cells, finding the receptor on the cell surface and nuclei, and identified the 67 kDa LR as the almost exclusive isoform interacting with PrP C . Here, we show that the treatment with the 37/67 kDa LR inhibitor, NSC47924, affects both the direct 37/67 kDa LR-PrP C  interaction  in vitro  and the formation of the immunocomplex in live cells, inducing a progressive internalization of 37/67 kDa LR and stabilization of PrP C  on the cell surface. These data reveal NSC47924 as a useful tool to regulate PrP C  and 37/67 kDa LR trafficking and degradation, representing a novel small molecule to be tested against prion diseases.

The 37/67kDa laminin receptor (LR) inhibitor, NSC47924, affects 37/67kDa LR cell surface localization and interaction with the cellular prion protein