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PMID: 3597406 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Inhibition of lecithin-cholesterol acyltransferase by diphytanoyl phosphatidylcholine.

The Journal of biological chemistry ·Vol. 262 ·No. 19 ·1987-07-05 ·Pages 9033-6

Pownall HJ, Pao Q, Brockman HL, Massey JB

Abstract

Model high density lipoproteins containing human apolipoprotein A-I, cholesterol, and a variety of phosphatidylcholines (PCs) have been prepared and tested. The PCs included 1-palmitoyl-2-oleoyl PC (POPC) and its diether analog 1-O-hexadecyl-2-oleyl PC (POPC ether), 1,2-diphytanoyl PC (DPhPC), 1-palmitoyl-2-phytanoyl PC, and 1-phytanoyl-2-palmitoyl PC. All ester PCs were good acyl donors for the transesterification of cholesterol catalyzed by human lecithin-cholesterol acyltransferase except DPhPC, which showed no reactivity. The PCs containing one phytanoyl chain donated an acyl chain to cholesterol as fast as non-branched fatty acyl chains. However, the competitive inhibition of lecithin-cholesterol acyltransferase by POPC ether and DPhPC was similar, and both lipids formed a macromolecular matrix that supported the reactivity of other ester PC substrates. The bulk of physicochemical properties of model high density lipoproteins composed of DPhPC were indistinguishable from those of POPC ether. These properties included 1) alpha-helical content of the apoprotein as assessed by circular dichroism, 2) microviscosity as determined from the fluorescence polarization and lifetime of the probe 1,6-diphenyl-1,3,5-hexatriene, 3) macromolecular weight based upon analytical gel filtration chromatography, and 4) surface polarity revealed by the fluorescence of 6-propionyl-2(dimethylamino)naphthalene. The only major difference in a physicochemical property was that the molecular surface area of DPhPC (area = 69 A2 at collapse pressure) determined by monolayer methods was 17 A2 greater than that of POPC (area = 53 A2 at collapse pressure) at all surface pressures measured. We suggest that the properties of DPhPC in being enzymatically nonreactive but a competitive inhibitor are due to its much larger size and that the active site of lecithin-cholesterol acyltransferase cannot bind phospholipid substrates in a catalytically productive way if they have surface areas of 70 A2 or more.

MeSH Terms
Kinetics Lipoproteins, HDL/metabolism Phosphatidylcholine-Sterol O-Acyltransferase/antagonists & inhibitors Phosphatidylcholines/metabolism,pharmacology
Chemicals
Lipoproteins, HDL Phosphatidylcholines 1,2-diphytanoylphosphatidylcholine Phosphatidylcholine-Sterol O-Acyltransferase 1-palmitoyl-2-oleoylphosphatidylcholine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Pownall H J
Pao Q
Brockman H L
Massey J B
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1987-07-05
Pages
9033-6
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NHLBI NIH HHS · HL-23003 · United States
NHLBI NIH HHS · HL-30913 · United States
NHLBI NIH HHS · HL-30914 · United States
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