Human platelets have cholesteryl ester hydrolytic activity resulting in esterification of [1-14C]oleate to individual phospholipids of platelets.

摘要: Human platelet cholesteryl ester hydrolytic (CEH) activity was determined toward [1-14C]oleate resulting in esterification of to individual phospholipids: choline-containing phospholipids (PC); ethanolamine-containing (PE); phosphatidylserine (PS); phosphatidylinositol (PI); and sphingomyelin (SPH). Liberation enhanced by 100 nM iloprost (a stable analogue prostacyclin that increases cyclic adenosine monophosphate (c-AMP)), inhibited 30 microM H-89 (N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide)) specific c-AMP dependent protein kinase (CADPK) inhibitor) 500 2',5' dideoxyadenosine (DDA) (an inhibitor iloprost-induced rise c-AMP), but unaffected 150 mM choloroquine diphosphate. These observations suggest the CEH is mediated a CADPK phosphorylation an enzyme with phosphorylated state representing active form extralysosomal.