Cyclic AMP-dependent protein kinases (protein kinase A) are activated by the signal cascade originated by the activation of the G protein Gs by the LHCG-receptor. Activated Gs binds the enzyme adenylate cyclase and this leads to the production of cyclic AMP (cAMP). Cyclin AMP-dependent protein kinases are present as tetramers with two regulatory subunits and two catalytic subunits. Upon binding of cAMP to the regulatory subunits, the catalytic units are released and initiate the phosphorylation of proteins leading to the physiologic action. Cyclic AMP is degraded by phosphodiesterase and release 5’AMP. One of the targets of protein kinase A is the Cyclic AMP Response Element Binding Protein, CREB, which binds DNA in the cell nucleus via direct interactions with specific DNA sequences called cyclic AMP response elements (CRE); this process results in the activation or inactivation of gene transcription.
The signal is amplified by the involvement of cAMP and the resulting phosphorylation. The process is modified by prostaglandins. Other cellular regulators that participate are the intracellular calcium concentration regulated by phospholipase C activation, nitric oxide, and other growth factors.
Other pathways of signaling exist for the LHCGR.