Annexin II inhibits calcium‐dependent phospholipase A1 and lysophospholipase but not triacyl glycerol lipase activities of rat liver hepatic lipase

FEBS Letters

Bohn, Ernst²  Löffler, Bernd-Michael¹  Gerke, Volker¹  Kunze, Hans²  Kresse, Hans² 

[1]Max-Planck-Institut für biophysikalische Chemie, Am Faβberg 11, D-3400 Göttingen, Germany

[2]Max-Planck-Institut für experimentelle Medizin, Hermann-Rein-Straβe 3 Am Faβberg 11, D-3400 Göttingen, Germany

关键词: Hepatic lipase;    Annexin;    Phospholipase A1;    Lysophospholipase;    Triacyl glycerol lipase;    HL;    hepatic lipase;    [14C]PC;    1;    2-di[1-14C]palmitoyl-sn-glycero-3-phosphorylcholine;    [14C]LPC;    1-[1-14C]palmitoyl-sn-glycero-3-phosphorylcholine;    [14C]PS;    1;    2-dioleoyl-sn-glycero-3-phosphoryl-l-[3-14C]serine;    [14C]LPS;    1-oleoyl-sn-glycero-3-phosphoryl-l-[3-14C]serine;    [3H]TO;    glycerol tri[9;    10(n)-3H]oleate;   

DOI  :  10.1016/0014-5793(92)80294-Q

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A member of the annexin family (the heterotetrameric annexin II₂pl 1₂ complex purified from porcine intestinal epithelium) was tested for its ability to affect different calcium-dependent intrinsic lipolytic activities of rat liver hepatic lipase (HL). Whereas annexin II in the presence of calcium failed to interfere with HL triacyl glycerol lipase (EC 3.1.1.3) activity, it inhibited HL phospholipase A₁ (EC 3.1.1.32) and lysophospholipase (EC 3.1.1.5) activities. Inhibition could be overcome by increasing the substrate concentration. Under phospholipase A₁ assay conditions, annexin II did not bind to the purified HL enzyme. These results therefore suggest that only inhibitor/substrate interactions lead to inhibition of HL phospholipase A₁ and lysophospholipase activities, an obviously general mechanism of phospholipase inhibition by annexins. Possible implications of HL inhibition in vivo by annexins are discussed.

【 授权许可】

Unknown