HDL-induced cardiac prostacyclin synthesis: relative contribution of HDL apoprotein and lipid.
The objective of this study was to determine if the apoprotein or lipid constituents of high density lipoproteins (HDL) mediate HDL-induced prostacyclin synthesis in the Langendorff-perfused rabbit heart. Acetylation, acetoacetylation, or partial removal by trypsin digestion of HDL apoprotein did not reduce the ability of the lipoprotein to stimulate cardiac prostacyclin synthesis. Delipidated apoproteins were less effective in stimulating cardiac prostacyclin synthesis in comparison to intact HDL. In contrast, protein-free lipid vesicles, made from HDL lipids, caused a pronounced stimulation of cardiac prostacyclin synthesis. These results suggest that HDL apoproteins, in their native state, are not essential for HDL-induced cardiac prostacyclin synthesis. The stimulation of cardiac prostacyclin synthesis by HDL may depend on the lipoprotein's lipid rather than on its apoprotein constituents.
D015121:6-Ketoprostaglandin F1 alpha / Q000378:metabolism; D000818:Animals; D001053:Apolipoproteins / Q000378:metabolism*; D011464:Epoprostenol / Q000096:biosynthesis*; D006321:Heart / Q000187:drug effects; D050356:Lipid Metabolism; D008075:Lipoproteins, HDL / Q000378:metabolism / Q000494:pharmacology*; D008297:Male; D009206:Myocardium / Q000378:metabolism*; D011817:Rabbits; D014357:Trypsin / Q000378:metabolism
D001053:Apolipoproteins; D008075:Lipoproteins, HDL; D015121:6-Ketoprostaglandin F1 alpha; D011464:Epoprostenol; D014357:Trypsin