Phospholipid analogues: side chain- and polar head group-dependent effects on phosphatidylcholine biosynthesis.
In recent studies we showed that the phospholipid analogue hexadecylphosphocholine inhibits phosphatidylcholine biosynthesis by affecting the translocation of the rate-limiting enzyme of phosphatidylcholine biosynthesis, CTP:phosphocholine cytidylyltransferase (EC 2.7.7.15), to membranes, where it i...
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Format: | Article |
Language: | English |
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Elsevier
1994-04-01
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Series: | Journal of Lipid Research |
Online Access: | http://www.sciencedirect.com/science/article/pii/S0022227520411769 |
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author | C.C. Geilen A. Haase T. Wieder D. Arndt R. Zeisig W. Reutter |
author_facet | C.C. Geilen A. Haase T. Wieder D. Arndt R. Zeisig W. Reutter |
author_sort | C.C. Geilen |
collection | DOAJ |
description | In recent studies we showed that the phospholipid analogue hexadecylphosphocholine inhibits phosphatidylcholine biosynthesis by affecting the translocation of the rate-limiting enzyme of phosphatidylcholine biosynthesis, CTP:phosphocholine cytidylyltransferase (EC 2.7.7.15), to membranes, where it is active (Geilen et al. 1992. J. Biol. Chem. 267: 6719-6724). The present study was performed to investigate the structure-dependency of this effect. It is shown that the inhibitory properties of phospholipid analogues are dependent on their alkyl side chain length (dodecylphosphocholine < tetradecylphosphocholine < hexadecylphosphocholine < heptadecylphosphocholine < octadecylphosphocholine > eicosadecylphosphocholine). Furthermore, it is demonstrated that this inhibition of phosphatidylcholine biosynthesis by phospholipid analogues is also dependent on the polar head group (hexadecylphosphocholine > hexadecylphosphoethanolamine = hexadecylphosphoserine). These effects result from an inhibition of the CTP:phosphocholine cytidylyltransferase and are not due to an inhibition of choline uptake or differences in the cellular uptake of the phospholipid analogues investigated. |
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id | doaj.art-0349bd2374224340a9231a5ba15c4cc2 |
institution | Directory Open Access Journal |
issn | 0022-2275 |
language | English |
last_indexed | 2024-12-17T08:40:36Z |
publishDate | 1994-04-01 |
publisher | Elsevier |
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series | Journal of Lipid Research |
spelling | doaj.art-0349bd2374224340a9231a5ba15c4cc22022-12-21T21:56:21ZengElsevierJournal of Lipid Research0022-22751994-04-01354625632Phospholipid analogues: side chain- and polar head group-dependent effects on phosphatidylcholine biosynthesis.C.C. Geilen0A. Haase1T. Wieder2D. Arndt3R. Zeisig4W. Reutter5Institut für Molekularbiologie und Biochemie der Freien Universität Berlin, Germany.Institut für Molekularbiologie und Biochemie der Freien Universität Berlin, Germany.Institut für Molekularbiologie und Biochemie der Freien Universität Berlin, Germany.Institut für Molekularbiologie und Biochemie der Freien Universität Berlin, Germany.Institut für Molekularbiologie und Biochemie der Freien Universität Berlin, Germany.Institut für Molekularbiologie und Biochemie der Freien Universität Berlin, Germany.In recent studies we showed that the phospholipid analogue hexadecylphosphocholine inhibits phosphatidylcholine biosynthesis by affecting the translocation of the rate-limiting enzyme of phosphatidylcholine biosynthesis, CTP:phosphocholine cytidylyltransferase (EC 2.7.7.15), to membranes, where it is active (Geilen et al. 1992. J. Biol. Chem. 267: 6719-6724). The present study was performed to investigate the structure-dependency of this effect. It is shown that the inhibitory properties of phospholipid analogues are dependent on their alkyl side chain length (dodecylphosphocholine < tetradecylphosphocholine < hexadecylphosphocholine < heptadecylphosphocholine < octadecylphosphocholine > eicosadecylphosphocholine). Furthermore, it is demonstrated that this inhibition of phosphatidylcholine biosynthesis by phospholipid analogues is also dependent on the polar head group (hexadecylphosphocholine > hexadecylphosphoethanolamine = hexadecylphosphoserine). These effects result from an inhibition of the CTP:phosphocholine cytidylyltransferase and are not due to an inhibition of choline uptake or differences in the cellular uptake of the phospholipid analogues investigated.http://www.sciencedirect.com/science/article/pii/S0022227520411769 |
spellingShingle | C.C. Geilen A. Haase T. Wieder D. Arndt R. Zeisig W. Reutter Phospholipid analogues: side chain- and polar head group-dependent effects on phosphatidylcholine biosynthesis. Journal of Lipid Research |
title | Phospholipid analogues: side chain- and polar head group-dependent effects on phosphatidylcholine biosynthesis. |
title_full | Phospholipid analogues: side chain- and polar head group-dependent effects on phosphatidylcholine biosynthesis. |
title_fullStr | Phospholipid analogues: side chain- and polar head group-dependent effects on phosphatidylcholine biosynthesis. |
title_full_unstemmed | Phospholipid analogues: side chain- and polar head group-dependent effects on phosphatidylcholine biosynthesis. |
title_short | Phospholipid analogues: side chain- and polar head group-dependent effects on phosphatidylcholine biosynthesis. |
title_sort | phospholipid analogues side chain and polar head group dependent effects on phosphatidylcholine biosynthesis |
url | http://www.sciencedirect.com/science/article/pii/S0022227520411769 |
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