title: 15-Lipoxygenation of phospholipids may precede the sn-2 cleavage by phospholipases A2: reaction specificities of secretory and cytosolic phospholipases A2 towards native and 15-lipoxygenated arachidonoyl phospholipids.
abstract: Reticulocyte-type 15-lipoxygenase is known to dioxygenate phospholipids without preceding action of phospholipases A2 (PLA2). Therefore we studied the reaction of the secretory PLA2s (sPLA2) from pancreas and snake venom, and of the human cytosolic PLA2 (cPLA2) with 1-palmitoyl-2-arachidonoyl phosphatidylcholine (PAPC) and their 15-lipoxygenated species (PAPC-OOH and PAPC-OH) either alone or as equimolar mixtures. These PLA2s cleaved PAPC-O(O)H with higher (sPLA2) or similar rates (cPLA2) as compared with native PAPC. In mixtures, however, PAPC proved to be the preferred, albeit not exclusive substrate for all three PLA2s. Thus, partial 15-lipoxygenation of phospholipids may also trigger liberation of arachidonic acid.
authors.affiliation: Department of Gynaecology, University Medical Centre Benjamin Franklin, Free University Berlin, Germany.
authors.forename: P
authors.initials: P
authors.lastname: Chaitidis
authors.forename: T
authors.initials: T
authors.lastname: Schewe
authors.forename: M
authors.initials: M
authors.lastname: Sutherland
authors.forename: H
authors.initials: H
authors.lastname: Kühn
authors.forename: S
authors.initials: S
authors.lastname: Nigam
mesh_terms: D001093:Arachidonate 15-Lipoxygenase / Q000378:metabolism*; D016718:Arachidonic Acid / Q000378:metabolism; D003435:Crotalid Venoms / Q000201:enzymology; D003600:Cytosol / Q000201:enzymology; D006801:Humans; D006868:Hydrolysis; D010741:Phospholipases A / Q000378:metabolism*; D054467:Phospholipases A2; D010743:Phospholipids / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D003435:Crotalid Venoms; D010743:Phospholipids; D016718:Arachidonic Acid; D001093:Arachidonate 15-Lipoxygenase; D010741:Phospholipases A; D054467:Phospholipases A2