scholarly journals Biosynthesis of lecithin in brain. Participation of cytidine diphosphate choline and phosphatidic acid

1963 ◽  
Vol 87 (1) ◽  
pp. 128-136 ◽  
Author(s):  
KP STRICKLAND ◽  
D SUBRAHMANYAM ◽  
ET PRITCHARD ◽  
W THOMPSON ◽  
RJ ROSSITER
1971 ◽  
Vol 49 (3) ◽  
pp. 275-281 ◽  
Author(s):  
M. Kates ◽  
C. E. Park ◽  
B. Palameta ◽  
C. N. Joo

The chemical synthesis of 2,3-di-O-phytanyl-sn-1-glycerophosphate was carried out in two ways: (a) by phosphorylation of 2,3-diphytanyl-sn-glycerol with diphenylphosphoryl chloride in pyridine, followed by catalytic hydrogenolysis of the phenyl groups; and (b) by condensation of 1-iodo-2,3-di-O-phytanyl-sn-glycerol with silver di-p-nitrobenzyl phosphate in anhydrous benzene, followed by catalytic hydrogenolysis of the p-nitrobenzyl groups. The free diether phosphatidic acid obtained was converted to the dipotassium and disodium salts. The diether phosphatidic acid was also converted to the diether analogue of cytidine diphosphate diglyceride by condensation with cytidine monophosphate morpholidate in pyridine. The physical properties of these diether analogues are described, as well as their stabilities towards acid hydrolysis.


1962 ◽  
Vol 40 (1) ◽  
pp. 1051-1058 ◽  
Author(s):  
K. P. Strickland ◽  
R. J. Rossiter

When particle preparations from rat or chicken liver were incubated in a suitable medium containing α-glycerophosphate-C14, radioactivity was recovered from lecithin, phosphatidyl inositol, phosphatidic acid, and triglyceride. Whole homogenate and various particle preparations catalyzed the dephosphorylation of a number of phosphatidic acids, with the liberation of inorganic P.It is currently believed that liver preparations are capable of catalyzing the esterification of L-α-glycerophosphate, with the formation of L-α-phosphatidic acid, which subsequently may be dephosphorylated to form D-α,β-diglyceride. The diglyceride so formed may then give rise either to lecithin, by combining with phosphorylcholine from cytidine diphosphate choline, or to triglyceride, by combining with fatty acid from fatty acyl coenzyme A. If these reactions occur in liver particle preparations, it should be possible, by the addition in vitro of unlabelled cytidine diphosphate choline, to divert the synthesis of lipid from the formation of triglyceride to the formation of lecithin. In experiments designed to put this hypothesis to the experimental test, such a diversion of lipid synthesis was achieved.


1972 ◽  
Vol 50 (1) ◽  
pp. 109-109
Author(s):  
M. Kates ◽  
C. E. Park ◽  
B. Palameta ◽  
C. N. Joo

Author(s):  
Manoj G Tyagi ◽  
Dharmendra Singh ◽  
Nirmala Joyce ◽  
Mohammed Amil ◽  
Shyam S Yadav

Phospholipids are basic building-block molecules for biological membranes. Biosynthesis of phospholipids i.e phosphatidylinositol, phosphatidylglycerol and phosphatidylserine requires a central liponucleotide intermediate named cytidine-diphosphate diacylglycerol (CDP-DAG). The CDP-DAG synthase (CDS) is an integral membrane enzyme catalysing the formation of CDP-DAG, an essential step for phosphoinositide recycling during signal transduction. New roles are being ascribed to the CDP-DAG in signalling and pathophysiological conditions. This pathway may also be the target of novel drugs to be used in neuro-psychiatric conditions. Key words: Phospholipids, Cytidine diphosphate, diacylglycerol, phosphatidic acid, phosphatidylglycerol.


1977 ◽  
Vol 55 (11) ◽  
pp. 1153-1158 ◽  
Author(s):  
W. Thompson ◽  
G. MacDonald

Cytidine diphosphate (CDP) diglyceride isolated from pooled rat liver was shown like phosphatidyl inositol to contain stearate and arachidonate as the major fatty acids. On the other hand palmitate and oleate were the predominant fatty acids of total liver phosphatidic acid.Labelling of molecular classes of phosphatidic acid, CDP-diglyceride, and phosphatidyl inositol was examined in liver at various time intervals after either intraportal or intrajugular injections of [3H]glycerol. In general the major flux of radioactivity was through the oligoenoic classes [Δ1 and Δ2] of phosphatidic acid. In contrast the labelling of oligoenoic classes of CDP-diglyceride was less and of polyenoic classes [Formula: see text] significantly enhanced, raising the possibility that there may be some discrimination in selection of species of phosphatidic acid for liponucleotide synthesis. After intrajugular injections of isotope the monoenoic classes of phosphatidyl inositol were most highly labelled but between 5 and 240 min there was a progressive decrease of radioactivity in this class and increase in the tetraenoic species, presumably as a result of deacylation and reacylation reactions. The backflow of radioactivity from phosphatidyl inositol was deemed not a likely explanation for the observed labelling pattern of CDP-diglyceride.The conversion of sonicated dispersions of [3H]phosphatidic acid, labelled in the glycerol moiety, to CDP-diglyceride by rat liver microsomes was examined. There was slightly less label in the oligoenoic classes and slightly more in trienoic and polyenoic (> Δ4) classes of CDP-diglyceride as compared with phosphatidic acid. These differences were much smaller in vitro than those observed in vivo. The in vitro data provide no convincing evidence for a high enough selectivity to explain the differences in arachidonate content between phosphatidic acid and the liponucleotide.


1962 ◽  
Vol 40 (8) ◽  
pp. 1051-1058 ◽  
Author(s):  
K. P. Strickland ◽  
R. J. Rossiter

When particle preparations from rat or chicken liver were incubated in a suitable medium containing α-glycerophosphate-C14, radioactivity was recovered from lecithin, phosphatidyl inositol, phosphatidic acid, and triglyceride. Whole homogenate and various particle preparations catalyzed the dephosphorylation of a number of phosphatidic acids, with the liberation of inorganic P.It is currently believed that liver preparations are capable of catalyzing the esterification of L-α-glycerophosphate, with the formation of L-α-phosphatidic acid, which subsequently may be dephosphorylated to form D-α,β-diglyceride. The diglyceride so formed may then give rise either to lecithin, by combining with phosphorylcholine from cytidine diphosphate choline, or to triglyceride, by combining with fatty acid from fatty acyl coenzyme A. If these reactions occur in liver particle preparations, it should be possible, by the addition in vitro of unlabelled cytidine diphosphate choline, to divert the synthesis of lipid from the formation of triglyceride to the formation of lecithin. In experiments designed to put this hypothesis to the experimental test, such a diversion of lipid synthesis was achieved.


1986 ◽  
Vol 56 (03) ◽  
pp. 260-262 ◽  
Author(s):  
Isabella Roos ◽  
Fabrizia Ferracin ◽  
Alfred Pletscher

SummaryArginine-vasopressin (AVP) in the presence of Mg2+ but not in the absence of bivalent cations led to accumulation of [32P]-phosphatidic acid ([32P]-PA) in human blood platelets. Mg2+ also enhanced the specific binding of [3H]-AVP to intact platelets. The concentrations of the cation which enabled AVP to cause half maximal rise of [32P]-PA and those inducing half maximal [3H]-AVP-binding were of the same order. It is concluded that the stimulation of phosphatidyl inositide breakdown by AVP in presence of Mg2+ is at least partially due to a Mg2+-induced enhancement of specific AVP-binding to the platelet membranes.


1983 ◽  
Vol 50 (02) ◽  
pp. 595-600 ◽  
Author(s):  
Y Watanabe ◽  
M Soda ◽  
N Fukamachi ◽  
B Kobayashi

SummaryThrombin-induced platelet release reaction examined with secretion of calcium and N-acetylglucosaminidase was significantly enhanced in the platelets from reserpine-treated rabbits as compared with the control. On the other hand, 32P-incorporation into phosphatidic acid was suppressed in the reserpinized platelets in activated state. Thrombin induced phosphatidylinositol (PI)- breakdown, which was examined by decreases in radioactivity and content of PI, and an increase in diacylglycerol, was not enhanced in the reserpinized platelets as compared with the control. The phosphorylation of the specific protein coupled to thrombin- induced platelet PI-breakdown was not stimulated in the reserpinized platelets as compared with the control. In contrast to PI, PC-degradation by thrombin was significantly stimulated in the reserpinized platelets. Possible existence of pathway(s) other than that associated with an enhancement of Pl-tumover is conceivable as a mechanism involved in platelet release reaction.


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