Lysophosphatidic acid (LPA) is a lipid mediator that induces various cellular responses including proliferation, migration and inhibition of apoptosis in numerous types of cells via its specific G protein-coupled receptors. At least 5 LPA G-protein coupled receptors (GPCRs) have been identified so far. LPA mediates its effects predominantly by interacting with members of the endothelial differentiation gene (EDG) subfamily of GPCRs: LPA1/EDG2, LPA2/EDG4, and LPA3/EDG7¹. LPA2 couples to three distinct families of heterotrimeric GTP binding proteins, including G_αq, G_αi, and G_α12/13².

LPA2 spans the plasma membrane seven times and contains three extracellular loops and three intracellular loops. LPA2 is unique from the other LPA receptors as it contains two distinct protein-protein interaction domains in the carboxyl-terminal tail (aa 296-351). In the proximal region, LPA2 contains a di-leucine motif and several putative palmitoylated cysteine residues. This region is responsible for associating with zinc-finger proteins^3.

LPA2 mRNA is expressed in a variety of tissues including human testis, leukocytes, prostate, spleen, thymus, pancreas, and bone marrow³.

LPA2-null mice do not show any obvious phenotypic aberrations⁵. On the other hand, LPA2 expression is increased in ovarian and thyroid cancers and inflammation, suggesting that the main function of LPA2 could become evident under pathophysiological conditions⁶.