Molecular species of choline glycerophospholipids and ethanolamine glycerophospholipids in goat liver

1989 ◽  
Vol 34 (1) ◽  
pp. 71-78
Author(s):  
Young K. Yeo ◽  
Ryun B. Tak ◽  
Bernadette C. Celi
Keyword(s):  
Molecular Species ◽  
Ethanolamine Glycerophospholipids ◽  
Choline Glycerophospholipids

scholarly journals Oestradiol-induced changes in the composition of phospholipid classes of quail oviduct: specific replacement of arachidonic acid by docosahexaenoic acid in alkenylacyl-glycerophosphoethanolamine

1994 ◽  
Vol 301 (2) ◽  
pp. 361-366 ◽  
Author(s):  
B E Felouati ◽  
J F Pageaux ◽  
J M Fayard ◽  
M Lagarde ◽  
C Laugier
Keyword(s):  
Cell Proliferation ◽  
Arachidonic Acid ◽  
Molecular Species ◽  
Phospholipid Composition ◽  
Oestrogen Treatment ◽  
Ethanolamine Glycerophospholipids ◽  
Striking Result ◽  
Choline Glycerophospholipids ◽  
Phospholipid Classes ◽  
Induced Changes

The phospholipid composition and the molecular species of the major subclasses of ethanolamine and choline glycerophospholipids were determined during the natural or oestradiol-induced development of the quail oviduct. The phospholipid concentration increased significantly during oviduct development, and the proportion of ethanolamine glycerophospholipids (EPL) remained constant while that of choline glycerophospholipids increased. The immature oviduct contained the majority of its endogenous arachidonic acid mass (71%) in EPL, mainly in alkenylacyl-glycerophosphoethanolamine (alkenylacyl-GPE) (49% of the total). Oestrogen treatment induced the depletion of 20:4,n-6 specifically from this pool, which indicates the biological importance of 20:4,n-6 molecular species in alkenylacyl-GPE as substrates for the oviduct phospholipases activated by oestradiol, and suggests that this EPL subclass is involved in the oestrogen-induced cell proliferation. Another striking result was the marked increase in 22:6,n-3 EPL molecular species following the oestradiol treatment and more particularly the strict substitution of 20:4,n-6 by 22:6,n-3 in alkenylacyl-GPE. We speculate that alkenylacyl-GPE molecular species containing 22:6,n-3 may participate in the arrest of oestrogen-induced proliferation.

scholarly journals Roles of various phospholipases A2 in providing lysophospholipid acceptors for fatty acid phospholipid incorporation and remodelling

2002 ◽  
Vol 364 (3) ◽  
pp. 695-702 ◽  
Author(s):  
Jesús BALSINDE
Keyword(s):  
Fatty Acid ◽  
Phospholipase A2 ◽  
Group Iv ◽  
Group Vi ◽  
Ethanolamine Glycerophospholipids ◽  
Phospholipases A2 ◽  
Cytosolic Phospholipase ◽  
Choline Glycerophospholipids ◽  
Bromoenol Lactone ◽  
Strong Candidate

In the present study the lysophospholipid sources for arachidonic (AA) and eicosapentaenoic acid (EPA) incorporation into and redistribution within the phospholipids of phorbol-ester-differentiated U937 cells was investigated. Initially, AA incorporated primarily into choline glycerophospholipids (PC), whereas EPA incorporated mainly into ethanolamine glycerophospholipids (PE). Bromoenol lactone (BEL), an inhibitor of the Group VI Ca2+-independent phospholipase A2 (iPLA2), diminished both lysophosphatidylcholine levels and the incorporation of AA into phospholipids. However BEL had little effect on EPA incorporation. In concanavalin A-activated cells, EPA, but not AA, incorporation was also affected by methyl arachidonyl fluorophosphonate (MAFP), suggesting an additional role for the group IV cytosolic phospholipase A2. In the activated cells AA and EPA did not compete with each other for incorporation, indicating that the pathways for AA and EPA incorporation are partially different. The AA and EPA initially incorporated into PC slowly moved to PE in a process that took several hours. The transfer of AA and EPA from PC to PE was not inhibited by BEL, MAFP or LY311727 [3-(3-acetamide 1-benzyl-2-ethylindolyl-5-oxy)propanesulphonic acid], raising the possibility that an as-yet-undetermined phospholipase A2 may be involved in fatty acid phospholipid remodelling. A strong candidate to be involved in these reactions is a novel Ca2+-independent phospholipase A2 that, unlike all known iPLA2s, is resistant to inhibition by BEL and also to MAFP and LY311727. The enzyme activity cleaves both PC and PE and is thus able to provide the lysoPC and lysoPE acceptors required for the fatty acid acylation reactions.

scholarly journals The stimulation by synaptic transmitters of the incorporation of oleate into the phospholipid of synaptic membranes

1975 ◽  
Vol 148 (3) ◽  
pp. 557-565 ◽  
Author(s):  
R J Gullis ◽  
C E Rowe
Keyword(s):  
Initial Rate ◽  
Optimum Concentration ◽  
Synaptic Membranes ◽  
Gamma Aminobutyric Acid ◽  
Response Curves ◽  
Ethanolamine Glycerophospholipids ◽  
Sodium Phosphate Buffer ◽  
Choline Glycerophospholipids ◽  
Hydrolysis Of ◽  
Guinea Pig Brain

Noradrenaline stimulated the incorporation of oleate into choline glycerophospholipids of guinea-pig brain synaptic membranes incubated in sodium phosphate buffer. In the presence of 1 mm-NaF, noradrenaline stimulated the incorporation of oleate into the choline glycerophospholipids, phosphatidylinositol, ethanolamine glycerophospholipids, phosphatidylserine and phosphatidic acid of synaptic membranes incubated in 10 mm-Tris-HCl buffer. In Tris-CHl containing 1 mm-NaF, stimulation of incorporation of oleate into choline glycerophospholipids by noradrenaline was enhanced by ATP, CaCl2, MgCl2 and CoA plus dithiothreitol. The optimum concentration of CaCl2 for stimulation by 10 mum-noradrenaline was 10 mum. In the presence of CaCl2, the optimum concentration of ATP-2MgCl2 was in the range 0.1-1 mm. Acetylcholine, carbamoylcholine, 5-hydroxytryptamine, dopamine, histamine and gamma-aminobutyric acid also stimulated the incorporation of oleate into choline glycerophospholipids of synaptic membranes. Sigmoidal dose-response curves were obtained, similar to those obtained previously for stimulation by the same agonists of the hydrolysis of phosphatidylcholine by phospholipase A2 (Gullis & Rowe, 1975a). The initial rate of transfer of oleate from oleoyl-CoA to choline glycerophospholipid was similar to the initial rate of transfer from oleate-albumin, stimulated by noradrenaline. Transfer of oleate from oleoyl-CoA was not appreciably stimulated by noradrenaline, but was stimulated by ATP and MgCl2.

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