PARP-2 was initially identified in connection with DNA repair mechanisms. It is involved in the base excision repair (BER) pathway, a critical process for repairing single-strand breaks in DNA . PARP-2 catalyzes the transfer of ADP-ribose units from NAD+ to target proteins, a process known as poly (ADP-ribosyl)ation . This modification is essential for recruiting and activating other proteins involved in DNA repair.
PARP-2 has been implicated in several physiological and pathophysiological processes, including:
Human recombinant PARP-2 is produced using recombinant DNA technology, which involves inserting the PARP-2 gene into a suitable expression system, such as bacteria or yeast. This allows for the large-scale production of the enzyme for research and therapeutic purposes.
PARP-2 has gained significant attention in the field of cancer research. Inhibitors targeting PARP enzymes, including PARP-2, have shown promise in treating cancers with defects in DNA repair pathways, such as BRCA1/2-mutated breast and ovarian cancers . These inhibitors work by exploiting the concept of synthetic lethality, where the inhibition of PARP activity leads to the accumulation of DNA damage and cell death in cancer cells deficient in other DNA repair mechanisms.