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J Biol Chem, Vol. 274, Issue 14, 9400-9408, April 2, 1999
and§
From the Phosphatidylcholine (PtdCho) is the major
membrane phospholipid in mammalian cells, and its synthesis is
controlled by the activity of CDP:phosphocholine cytidylyltransferase
(CCT). Enforced CCT expression accelerated the rate of PtdCho
synthesis. However, the amount of cellular PtdCho did not increase as a
result of the turnover of both the choline and glycerol components of
PtdCho. Metabolic labeling experiments demonstrated that cells
compensated for elevated CCT activity by the degradation of PtdCho to
glycerophosphocholine (GPC). Phospholipase D-mediated PtdCho hydrolysis
and phosphocholine formation were unaffected. Most of the GPC produced
in response to excess phospholipid production was secreted into the
medium. Cells also degraded the excess membrane PtdCho to GPC when
phospholipid formation was increased by exposure to exogenous
lysophosphatidylcholine or lysophosphatidylethanolamine. The
replacement of the acyl moiety at the 1-position of PtdCho with a
non-hydrolyzable alkyl moiety prevented degradation to GPC.
Accumulation of alkylacyl-PtdCho was associated with the inhibition of
cell proliferation, demonstrating that alternative pathways of
degradation will not substitute. GPC formation was blocked by bromoenol
lactone, implicating the calcium-independent phospholipase
A2 as a key participant in the response to excess
phospholipid. Owing to the fact that PtdCho is biosynthetically
converted to PtdEtn, excess PtdCho resulted in overproduction and
exit of GPE as well as GPC. Thus, general membrane phospholipid
homeostasis is achieved by a balance between the opposing activities of
CCT and phospholipase A2.
Department of Biochemistry, St. Jude
Children's Research Hospital, Memphis, Tennessee 38105 and the
§ Department of Biochemistry, University of Tennessee,
Memphis, Tennessee 38163
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