PRIM2A Activators

PRIM2A Activators encompass a range of compounds that, while not directly interacting with PRIM2A, can create cellular conditions that enhance its functional activity. Aphidicolin and Hydroxyurea, by inhibiting DNA polymerase and ribonucleotide reductase respectively, create a cellular environment where the demand for primase activity, and thereby PRIM2A function, is increased. This indirect enhancement could arise due to the need for compensatory mechanisms in DNA replication. Similarly, DNA damaging agents like Camptothecin, Etoposide, and Cisplatin could indirectly augment PRIM2A activity. By increasing DNA supercoiling, entanglements, and adducts, these compounds create a scenario where enhanced initiation of DNA replication, a process involving PRIM2A, is required for DNA repair and replication continuity.

Olaparib along with VE-821 and the CHK1 inhibitor, disrupt key DNA damage response pathways. This disruption might lead to an increased need for DNA replication initiation mechanisms, indirectly enhancing PRIM2A activity. Lastly, ATR inhibitors like AZD6738, by affecting DNA damage response and replication stress, could create conditions necessitating increased PRIM2A-mediated replication initiation.