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

FEBS Letters

Nigam, Santosh¹  Schewe, Tankred¹  Chaitidis, Pavlos¹  Kühn, Hartmut²  Sutherland, Mark¹ 

[1] Eicosanoid Research Division, Department of Gynaecology, University Medical Centre Benjamin Franklin, Free University Berlin, D-12200 Berlin, Germany;Institute of Biochemistry, University Clinics Charité, Humboldt University of Berlin, D-10098 Berlin, Germany

关键词: 15-Lipoxygenase;    Phospholipase A2;    Cytosolic phospholipase A2;    Secretory phospholipase A2;    Peroxidized phospholipid;   

DOI  :  10.1016/S0014-5793(98)01024-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown