As a result, such receptors (e.g., LRP -1 and -6 and Fz) can modulate transcription through multiple mechanisms.
Considering the lack of molecular knowledge about LRP-1 in the cancer field, we investigated the intracellular signaling network connecting LRP-1 thethe aggressive behavior of tumor cells.
Importantly, both cell lines express LRP-1.
As shown in Fig. 3, we were able to successfully immunoprecipitate LRP-1 β-chain with an antibody raised against the extracellular LRP-1 α-chain.
However, despite the existence of a molecular interaction between Src and LRP-1, a specific Src-inhibitor did not affect the LRP-1-mediated control of cell invasion.
LRP-1 thus appeared as an attractive receptor for targeting the invasive behavior of malignant cells.
Co-immunoprecipitation experiments revealed that LRP-1 constitutes an intracellular docking site for MAPK containing complexes.
We recently described a key role for LRP-1 in tumor progression [17].
As expected, an increased amount of talin was observed in LRP-1-deficient cells.
As such, LRP-1 may represent a crucial actor in the epithelial-to-mesenchymal transition.
In agreement, immunoprecipitation assays revealed various protein phosphatases associated with the LRP-1-ICD (Fig. 10A).
