J. Fotheringham et al., Lysophosphatidylethanolamine acyltransferase activity is elevated during cardiac cell differentiation, BBA-MOL C B, 1485(1), 2000, pp. 1-10
Citations number
46
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS
We examined if elevation in lysophosphatidylethanolamine acyltransferase ac
tivity was associated with elevation in phosphatidylethanolamine content du
ring differentiation of P19 teratocarcinoma cells into cardiac myocytes. P1
9 cells were induced to undergo differentiation into cardiac myocytes by th
e addition of 1% dimethylsulfoxide to the medium. Immunofluorescence micros
copy revealed the presence of striated myosin at 8 days post-dimethylsulfox
ide addition confirming differentiation into cardiac cells. The content of
phosphatidylethanolamine was increased 2.1-fold (P < 0.05) in differentiate
d cells compared to undifferentiated cells, whereas the content of phosphat
idylcholine was reduced 29% (P < 0.05). There were no alterations in the po
ol sizes of other phospholipids, including cardiolipin. The relative abunda
nce of fatty acids in phospholipids of P19 cells was 18:1 > 18:0 > 16:1 = 1
8:2 > 16:0 = 14:0 > 20:4 and differentiation did not affect the relative am
ounts of these fatty acids within individual phospholipids. When cells were
incubated with [1,3-H-3] glycerol, radioactivity incorporated into phospha
tidylethanolamine was elevated 5.8-fold, whereas radioactivity incorporated
into phosphatidylcholine was unaltered. Ethanolaminephosphotransferase, ch
olinephosphotransferase and membrane CTP:phosphocholine cytidylyltransferas
e activities were elevated in differentiated cells compared to undifferenti
ated cells, whereas membrane and cytosolic phospholipase A? activities were
unaltered. Lysophosphatidylethanolamine acyltransferase activities were el
evated 2.4-fold (P < 0.05). Lysophosphatidylcholine acyltransferase, monoly
socardiolipin acyltransferase, acyl-Coenzyme A synthetase and acyl-Coenzyme
A hydrolase activities were unaltered in differentiated cells compared to
undifferentiated cells. We postulate that during cardiac cell differentiati
on, the observed elevation in lysophosphatidylethanolamine acyltransferase
activity accompanies the elevation in phosphatidylethanolamine mass, possib
ly to maintain the fatty acyl composition of this phospholipid within the m
embrane. (C) 2000 Elsevier Science B,V. All rights reserved.