PLA1A, also known as phosphatidylserine-specific phospholipase A1-alpha, belongs to the pancreatic lipase family. It specifically hydrolyzes the sn-1 fatty acid of phosphatidylserine (PS) or 1-acyl-lysophosphatidylserine (1-acyl-lysoPS), producing unsaturated lysoPS species. It is involved in multiple biological processes such as the antiviral innate immune response, cholesterol transportation, and the regulation of immune cell maturation and functions [2].

In a mouse model of mannan-induced psoriatic arthritis (MIP), Pla1a−/− mice showed a reduced susceptibility to MIP with less bone erosions and decreased levels of cytokines like IL-17, KC, IP-10, MIP-1β, LIF, and VEGF in hind paw tissues. CD4+ T cells in lymph nodes increased in Pla1a−/− mice, contributing to a higher ratio of CD3+ to CD19+ and CD4+ to CD8+ in the MIP model. This indicates that PLA1A may contribute to MIP through increased lymphocyte activation, potentially those producing IL-17 [1].

In conclusion, PLA1A is crucial in multiple biological processes. The study of Pla1a−/− mouse models has revealed its role in psoriatic arthritis, suggesting that it could be a potential target for treating such inflammatory diseases. Additionally, its functions in immune regulation, antiviral responses, and lipid-related processes make it an important gene for understanding various physiological and pathological conditions [1,2].