Disco-interacting protein 2 homolog A (DIP2A) (DIP2A)

Disco-interacting protein 2 homolog A (DIP2A) is a cell surface receptor that serves as a primary mediator for the signaling of Follistatin-like 1 (FSTL1), a secreted glycoprotein with potent cardioprotective properties. In the context of cardiovascular health, the binding of FSTL1 to DIP2A activates the PI3K/Akt/mTOR signaling pathway, which is essential for enhancing cardiomyocyte survival and reducing apoptosis following ischemic events like myocardial infarction. The pathway's effect is highly dependent on the post-translational modification of the ligand; glycosylated FSTL1 typically promotes survival, whereas non-glycosylated forms have been shown to induce the proliferation of adult cardiomyocytes, a rare and highly sought-after effect for cardiac regeneration. Beyond its cardiac functions, DIP2A is also involved in angiogenesis and has been implicated in neurodevelopmental processes, including axonal patterning and synaptic transmission. Therapeutic development focusing on this pathway includes the use of recombinant FSTL1 proteins and bioengineered epicardial patches designed to deliver the ligand directly to damaged heart tissue. However, challenges remain due to the dual role of FSTL1, which can promote beneficial repair in the acute phase but may contribute to pathological fibrosis in chronic disease states.

Other names

C21orf106DIP2KIAA0184Follistatin-like 1 receptorDisco-interacting protein 2 homolog A

Follistatin-like 1 (FSTL1) binds to the DIP2A receptor on the surface of cardiomyocytes and endothelial cells, triggering the activation of the PI3K/Akt/mTOR signaling pathway. This cascade promotes cell survival by inhibiting pro-apoptotic factors and, in specific contexts such as with non-glycosylated FSTL1, stimulates cardiomyocyte proliferation and angiogenesis to facilitate cardiac repair.