Interaction of prostaglandin E₁ with human high density lipoproteins

Abstract

Prostaglandin El has been shown to interact with serum high density lipoproteins (HDL) in a manner resembling the interaction of a ligand with a high affinity binding site. The presence of 10-12-10-'o M prostaglandin El induces a rearrangement of the HDL surface lipids and probably influences the biological functions of the lipoproteins. Fluorescent phospholipid probe High density lipoprotein Prostaglandin EI

Influence of prostaglandins on the lipid transfer between human high density and low density lipoproteins

“…Since PGE~ enhances both the spontaneous and protein-mediated transfer in a similar manner, it seems likely that the effect is due to reorganization of the lipoprotein surface by the prostaglandin rather than to interaction of PGE~ with the LEP. That PGE1 induces a rearrangement of the HDL surface has been demonstrated previously using fluorescence measurements [5]. The results of that fluorescence study correlate with those of the present work because in both studies PGE1 was active, whereas the closely related PGE2 was not.…”

“…It was found that PGE~ significantly stimulated spontaneous and protein-mediated lipid transfer from HDL to LDL, whereas PGE2 was inactive. These differences correlated with the results of our previous study [5], which demonstrated that PGE~ at low concentration was able to induce a rearrangement of the HDL surface lipids, while PGE2 was not.…”

“…We have recently discovered that small amounts of PGs can substantially change the surface structure of serum lipoproteins and that these changes appear to be mediated by PG-apoprotein interaction [2]. Lipids, particularly phosphatidylcholine and cholesterol esters, are known to exchange between Correspondence address: G.I.…”

The interaction of prostaglandin E1 with serum lipoproteins possible role in cholesterol homeostasis

“…Using ASM-or APC-labeled high density (HDL2, HDL 3, apo-A1 recombinants) and low density lipoproteins, we observed that in all these lipoproteins both the fluorescence polarization (P) and the efficiency of the tryptophane-to-probe energy transfer (E) were sensitive to the presence of small amounts of PGE~ ( Fig. 5) (13)(14)(15). The effects of PGE~ appeared to be caused by its interaction with protein rather than with lipid at the lipoprotein surface because no changes in P and E were observed upon addition of the prostaglandin to APC-or ASM-labeled liposomes with a lipid composition resembling that of the lipoprotein surface (14,15).…”