Incorporation of serine into the phospholipids of phosphatidylethanolamine-depleted Tetrahymena.

Abstract:

:Phosphatidylserine formation and decarboxylation are decreased in Tetrahymena in which phosphatidylethanolamine has been replaced by its isosteric analog 3-aminopropylphosphonolipid (1,2-diacylglyceryl-3-O-(3-aminopropylphosphonate). The combined activity of the phosphatidylethanolamine: serine phosphatidyltransferase/ phosphatidylserine decarboxylase complex in isolated mitochondria from lipid-altered cells [J. D. Smith and D. A. Giegel (1981) Arch. Biochem, Biophys. 206, 420-423] is about 20% of the activity in mitochondria from control cells. The enzyme activity in the lipid-altered mitochondria is stimulated by the addition of exogenous phosphatidylethanolamine to the assay system while the enzymes of the control mitochondria are not. In vivo the lipid-altered cells are able to incorporate radioactivity from [3-14C]- or [3-3H]serine into phosphatidylserine and phosphatidylcholine in amounts comparable to normal cells. Thus, under conditions of "stress" (e.g., the depletion of phosphatidylethanolamine), the phosphatidyltransferase is apparantly capable of utilizing other phospholipids besides its normal substrate phosphatidylethanolamine.

journal_name

Arch Biochem Biophys

authors

Smith JD

doi

10.1016/0003-9861(84)90433-8

subject

Has Abstract

pub_date

1984-05-01 00:00:00

pages

525-32

issue

2

eissn

0003-9861

issn

1096-0384

pii

0003-9861(84)90433-8

journal_volume

230

pub_type

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