Enzymes
UniProtKB help_outline | 2 proteins |
Reaction participants Show >> << Hide
- Name help_outline a sphingomyelin Identifier CHEBI:17636 Charge 0 Formula C24H48N2O6PR SMILEShelp_outline O=P(OCC[N+](C)(C)C)(OC[C@H](NC(*)=O)[C@@H](/C=C/CCCCCCCCCCCCC)O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 16 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:39727 | RHEA:39728 | RHEA:39729 | RHEA:39730 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Targeted mutation of plasma phospholipid transfer protein gene markedly reduces high-density lipoprotein levels.
Jiang X.C., Bruce C., Mar J., Lin M., Ji Y., Francone O.L., Tall A.R.
It has been proposed that the plasma phospholipid transfer protein (PLTP) facilitates the transfer of phospholipids and cholesterol from triglyceride-rich lipoproteins (TRL) into high-density lipoproteins (HDL). To evaluate the in vivo role of PLTP in lipoprotein metabolism, we used homologous rec ... >> More
It has been proposed that the plasma phospholipid transfer protein (PLTP) facilitates the transfer of phospholipids and cholesterol from triglyceride-rich lipoproteins (TRL) into high-density lipoproteins (HDL). To evaluate the in vivo role of PLTP in lipoprotein metabolism, we used homologous recombination in embryonic stem cells and produced mice with no PLTP gene expression. Analysis of plasma of F2 homozygous PLTP-/-mice showed complete loss of phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol, sphingomyelin, and partial loss of free cholesterol transfer activities. Moreover, the in vivo transfer of [3H]phosphatidylcholine ether from very-low-density proteins (VLDL) to HDL was abolished in PLTP-/-mice. On a chow diet, PLTP-/-mice showed marked decreases in HDL phospholipid (60%), cholesterol (65%), and apo AI (85%), but no significant change in non-HDL lipid or apo B levels, compared with wild-type littermates. On a high-fat diet, HDL levels were similarly decreased, but there was also an increase in VLDL and LDL phospholipids (210%), free cholesterol (60%), and cholesteryl ester (40%) without change in apo B levels, suggesting accumulation of surface components of TRL. Vesicular lipoproteins were shown by negative-stain electron microscopy of the free cholesterol- and phospholipid-enriched IDL/LDL fraction. Thus, PLTP is the major factor facilitating transfer of VLDL phospholipid into HDL. Reduced plasma PLTP activity causes markedly decreased HDL lipid and apoprotein, demonstrating the importance of transfer of surface components of TRL in the maintenance of HDL levels. Vesicular lipoproteins accumulating in PLTP-/-mice on a high-fat diet could influence the development of atherosclerosis. << Less
J. Clin. Invest. 103:907-914(1999) [PubMed] [EuropePMC]
This publication is cited by 6 other entries.
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Molecular and macromolecular specificity of human plasma phospholipid transfer protein.
Rao R., Albers J.J., Wolfbauer G., Pownall H.J.
Phospholipid transfer protein (PLTP), also known as lipid transfer protein 2 (LTP-2), mediates a transfer of phospholipids between high-density lipoproteins (HDL). The molecular and macromolecular specificities of recombinant human PLTP were studied using a fluorometric assay based on the excimer ... >> More
Phospholipid transfer protein (PLTP), also known as lipid transfer protein 2 (LTP-2), mediates a transfer of phospholipids between high-density lipoproteins (HDL). The molecular and macromolecular specificities of recombinant human PLTP were studied using a fluorometric assay based on the excimer fluorescence of pyrenyl lipids. To determine lipoprotein specificity of PLTP, donor very low density lipoproteins (VLDL), low-density lipoproteins (LDL), and HDL were labeled with 1-palmitoyl-2-[10-(1-pyrenyl)decanoyl]phosphatidylcholine (PPyDPC) and incubated with unlabeled acceptor VLDL, LDL, and HDL in every pairwise combination. The highest rate of PPyDPC transfer mediated by PLTP occurred between donor HDL and acceptor HDL. Reassembled HDL (rHDL) consisting of 1-palmitoyl-2-oleoylphosphatidylcholine, apolipoprotein A-I, and pyrene lipids (100:1:4) were used to demonstrate that PLTP transfers diacylglyceride > phosphatidic acid > sphingomyelin > phosphatidylcholine (PC) > phosphatidylglycerol > cerobroside > phosphatidylethanolamine. Thus, PLTP transfers a variety of lipids with two carbon chains and a polar head group. Unsaturation of one PC acyl chain greatly increased transfer rate, whereas increasing chain length and exchanging sn-1/sn-2 position had only small effects. The rate of PPyDPC transfer by PLTP decreases with increasing free cholesterol content in rHDL and with decreasing HDL size. In contrast to spontaneous transfer, PLTP mediates the accumulation of PC in small rHDL particles. PLTP may be important in vivo in the recycling of PC from mature HDL to nascent HDL, the latter of which are the initial acceptors of cholesterol from peripheral tissue for reverse cholesterol transport to the liver. << Less
Biochemistry 36:3645-3653(1997) [PubMed] [EuropePMC]
This publication is cited by 5 other entries.