Protease-activated receptor 1 (PAR1), a thrombin-responsive G protein-coupled receptor (GPCR), is implicated in promoting metastasis in multiple tumor types, including both sarcomas and carcinomas, but the molecular mechanisms responsible remain largely unknown.
Finally, a reduction was observed in the expression of integrin α5 (ITGA5) upon heterodimerization, supported by decreased cell adhesion to extracellular matrices <i>in vitro</i> Taken together, the data identify a novel pharmacologic mechanism for the modulation of tumor cell migration and invasion in the context of metastatic disease.<b>Implications:</b> This study investigates a signaling mechanism by which GPCR heterodimerization inhibits cancer cell migration.<i></i>.
Signaling activated by binding of the C<i>X</i>C motif chemokine ligand 12 (CXCL12) to its cognate G protein-coupled receptor (GPCR), chemokine C<i>X</i>C motif receptor 4 (CXCR4), is linked to metastatic disease.
Notably, HRG treatment upregulates surface expression levels of CXCR4, a G protein-coupled receptor (GPCR) implicated in breast cancer metastasis and an indicator of poor prognosis in breast cancer patients.
This review focuses on the recent report of a mouse melanoma model, TG-3, which has implicated the ectopic expression of the metabotropic glutamate receptor 1 (Grm1), a G protein coupled receptor (GPCR), in melanomagenesis and metastasis.