PARP (Poly ADP-ribose Polymerase) Family in Health and Disease.
Level 5 - mechanism / opinion, no new human data
Narrative review of mechanism and drug targets without primary human data or systematic methodology.
PubMed 40904702 · doi:10.1002/mco2.70314
What was done
This narrative review summarizes the structural and functional classification of the 17-member poly(ADP-ribose) polymerase (PARP) family of NAD⁺-dependent enzymes. It describes their enzymatic activities in poly(ADP-ribosyl)ation and mono(ADP-ribosyl)ation across DNA repair, metabolic regulation, telomere maintenance, and immune responses, alongside therapeutic advances and challenges in oncology and non-oncological diseases.
What was found
The abstract reports no quantitative experimental data or statistical metrics. It details the structural classification of PARPs into DNA-dependent PARPs, Tankyrases, CCCH-type PARPs, MacroPARPs, and atypical PARPs, noting their roles in base excision repair and homologous recombination. While PARP inhibitors are established in oncology, their therapeutic utility in neurodegenerative diseases, cardiovascular disorders, and viral infections remains poorly defined.
Why it matters
The review outlines the structural diversity and functional breadth of the PARP family, highlighting mechanistic targets to inform drug development and explore expanding PARP inhibitors beyond oncology.
Limits
The abstract reports no primary empirical findings, systematic search protocols, or meta-analytic data. As a broad narrative overview, it does not assess study quality or risk of bias in the cited literature. The therapeutic relevance for non-oncological indications remains largely undefined and unproven in clinical trials.
Cited by
- supports The PARP enzyme superfamily contains approximately 16 to 17 members, many of which modify proteins with single ADP-ribose units rather than synthesizing ADP-ribose polymers.