Twonew classes of inhibitors of LpPLA2 have been identified in fermentations ofPseudomonasfluorescens. The two structurally isomeric series differ in the geometry of closure of the bicyclic carbamate and comprise a range of compounds varying only in length of their lipophilic sidechain. The most abundant species were extracted from the cells and purified by silica and C18 chromatography. Membersof the more stable class were shown to be potent and selective competitive inhibitors of LpPLA2.Lipoprotein-associated phospholipase A2 (LpPLA2) is responsible for the conversion of phosphatidylcholine to lysophosphatidylcholine and oxidised free fatty acids during the conversion of low density lipoprotein to its oxidised form1^Both products are potent chemoattractants for circulating monocytes.2) Lysophosphatidylcholine results in rnacrophage proliferation3} and the endolithial dysfunction4'5) observed in patients with atherosclerosis.
Lipoprotein associated phospholipase A2 (LpPLA2) is responsible for the conversion of phosphatidylcholine to lysophosphatidylcholine and oxidised free fatty acids, both of which are potent chemoattractants for circulating monocytes. 1?2) Build-up of lysophosphatidylcholine results in macrophage proliferation^and endolithial dysfunction4>5) and so inhibition of LpPLA2provides an attractive strategy
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