Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
Gewählte Publikation:
Gorges, R; Hofer, G; Sommer, A; Stütz, H; Grillhofer, H; Kostner, GM; Paltauf, F; Hermetter, A.
Transfer of phospholipase A-resistant pyrene-dialkyl-glycerophosphocholine to plasma lipoproteins: differences between Lpa and LDL.
J Lipid Res. 1995; 36(2):251-259
Doi: 10.1016/S0022-2275(20)39901-6
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- Co-Autor*innen der Med Uni Graz
- Kostner Gerhard
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- Abstract:
- 1-O-Hexadecyl-2-O-pyrenedecanyl-sn-glycero-3-phosphocholine, a non-hydrolyzable fluorescent diether analog of phosphatidylcholine (PC), was synthesized as a probe for studying phospholipid transfer to different lipoprotein classes with potential phospholipase activities. After incubation of total human plasma with the new probe at 37 degrees C for 4.5 h, a characteristic partition between the main lipoprotein fractions was observed. The fluorescent lipid was not degraded under these conditions and, therefore, served as a measure for choline glycerophospholipid distribution between plasma lipoproteins. In low density lipoprotein (LDL) and high density lipoprotein-3 (HDL3) the fluorescent PC analog showed only monomer fluorescence, whereas in Lp[a] and HDL2 monomer and excimer fluorescence were observed, indicating that the fluorescent phosphatidylcholine analog was incorporated into the respective lipoproteins to a different extent. According to the increased pyrene excimer fluorescence in Lp[a] compared with LDL the labeled phosphatidylcholine must be enriched and/or clustered in Lp[a]. Data from phospholipid and total fluorescence analyses are compatible with the assumption of higher label concentration in Lp[a]. On the other hand, transfer rates for serum protein-catalyzed lipid transport into isolated Lp[a] were slower as compared to LDL. It is suggested that slower lipid transfer to Lp[a] under these conditions is due to the decreased lipid mobility in the Lp[a] surface, whereas the higher extent of label partition into Lp[a] as observed in total plasma might be due to the higher affinity of apolipoproteins for phosphatidylcholine in Lp[a] (Sommer, A., et al. 1992. J. Biol. Chem. 267: 24217-24222). The use of a fluorescent dialkyl- instead of diacyl-glycerophosphocholine for transfer studies was mandatory, as we found that lipoproteins contained phospholipase A2 activity toward long-chain phosphatidylcholine. The lipoprotein-associated phospholipase A2 was three times more active in Lp[a] than in LDL. The degradation products formed by the phospholipase, fatty acids, and lyso-PC may add to the high atherogenic potential of Lp[a].
- Find related publications in this database (using NLM MeSH Indexing)
- Biological Transport -
- Fluorescent Dyes -
- Glycerylphosphorylcholine - metabolism
- Humans - metabolism
- Lipoprotein(a) - metabolism
- Lipoproteins, LDL - metabolism
- Phosphatidylcholines - chemical synthesis
- Phospholipases A - metabolism
- Pyrenes - chemical synthesis
- Find related publications in this database (Keywords)
- Atherosclerosis
- Fluorescent Human Serum Lipoproteins
- Fluorescent Ether Phospholipids
- Phospholipid Transfer
- High Density Lipoproteins
- Pyrene-PC
- Nbd-PC
- Apolipoprotein B