TY - JOUR
T1 - Phospholipids chiral at phosphorus
T2 - Synthesis of dioleoylthiophosphatidylcholine and stereospecificity of lecithin-cholesterol acyltransferase
AU - Rosario-Jansen, Theresa
AU - Pownal, Henry
AU - Jiang, Ru Tai
AU - Tsai, Ming Daw
N1 - Funding Information:
’ This is Paper 22 in the series “Phospholipids Chiral at Phosphorus.” This work was supported by Grant GM 30327 from National Institutes 2 To whom correspondence should be addressed. 3 Abbreviations used: DMPA, 4-(N,N-dimethylamino)pyridine; DOPC, 1,2-dioleoyl-sn-glycero-3-phosphocholine; DOPsC, 1,2-dioleoyl-sn-glycero-3-thiophosphocholine; DPPC, l,Zdipalmitoyl-sn-glycero-3-phosphocholine; DPPsC, 1,2-dipalmitoyl-sn-glycero-3-thiophosphocholine; GPsC, sn-glycero-3-thiophosphocholine; LCAT, lecithin-cholesterol acyltransferase; MOPsC, l-oleoyl-sn-glycero-3-thiophosphocholine; MPPsC, l-palmitoyl-sn-glycero-3-thiophosphocholine; PLA2, phospholipase AZ; apo A-I, apolipoprotein A-I; POPC ether, 1-palmityl-2-oleyl-sn-glycero-3-phosphocholine; TLC, thin-layer chromatography.
Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1990/6
Y1 - 1990/6
N2 - Chiral 1,2-dioleoyl-sn-glycero-3-thiophosphocholine (DOPsC) was synthesized from chiral 1,2-dipalmitoyl-sn-glycero-3-thiophosphocholine (DPPsC) via hydrolysis to sn-glycero-3-thiophosphatidylcholine followed by reacylation. Both DOPsC and DPPsC were used to probe the stereochemical requirement in the enzyme-substrate recognition of lecithincholesterol acyltransferase (LCAT) from human plasma. In contrast to phospholipase A2, LCAT is totally insensitive to sulfur substitution or configuration at phosphorus and gives indistinguishable Km and Vmax values to Rp and Sp isomers of DOPsC and DPPsC and the corresponding natural substrates. The results suggest lack of stereospecific interaction between LCAT and the phosphate group of phospholipids.
AB - Chiral 1,2-dioleoyl-sn-glycero-3-thiophosphocholine (DOPsC) was synthesized from chiral 1,2-dipalmitoyl-sn-glycero-3-thiophosphocholine (DPPsC) via hydrolysis to sn-glycero-3-thiophosphatidylcholine followed by reacylation. Both DOPsC and DPPsC were used to probe the stereochemical requirement in the enzyme-substrate recognition of lecithincholesterol acyltransferase (LCAT) from human plasma. In contrast to phospholipase A2, LCAT is totally insensitive to sulfur substitution or configuration at phosphorus and gives indistinguishable Km and Vmax values to Rp and Sp isomers of DOPsC and DPPsC and the corresponding natural substrates. The results suggest lack of stereospecific interaction between LCAT and the phosphate group of phospholipids.
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U2 - 10.1016/0045-2068(90)90040-C
DO - 10.1016/0045-2068(90)90040-C
M3 - Article
AN - SCOPUS:0025003523
VL - 18
SP - 179
EP - 184
JO - Bioorganic Chemistry
JF - Bioorganic Chemistry
SN - 0045-2068
IS - 2
ER -