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Phospholipase A2 group IIF (PLA2G2F) is a secretory, calcium-dependent enzyme of the sPLA2 family that hydrolyzes the sn-2 ester bond of extracellular phospholipids, preferentially targeting phosphatidylglycerols, phosphatidylethanolamines, and—especially in the epidermis—DHA-containing plasmalogen-PE. It is distinguished by an extra C-terminal sequence with a unique cysteine residue. Unlike other sPLA2s, PLA2G2F is active at mildly acidic pH and is predominantly expressed in suprabasal layers of the skin, where it modulates local lipid mediators involved in inflammation and immune response. Disease associations include plantar fascial fibromatosis and potentially other inflammatory or infectious conditions, though direct drug targeting is still experimental with no specific inhibitors approved for clinical use. Therapeutic development is challenged by the need for selective inhibition among highly homologous sPLA2 subgroups.
Small molecule inhibition of secretory phospholipase A2 activity (by blocking the active site); Modulation of inflammatory mediator production via inhibition of arachidonic acid release (in theory; not specific to this subgroup)
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