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Papers In Press, published online ahead of print February 1, 2005
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Department of Physiology and Biophysics, Boston University, Boston, MA 02118
Corresponding Author: rzoeller{at}bu.edu
The variant Chinese hamster ovary (CHO-K1) cell line, NRel-4, is unable to synthesize plasmalogens due to a severe reduction in dihydroxyacetonephosphate acyltransferase (DHAPAT) activity [Nagan, N. et al. (1998) Biochem. J. 332, 273-279]. Northern analysis demonstrated that the loss of this activity was due to a severe reduction in mRNA levels for DHAPAT. Transfection of NRel-4 cells with a plasmid bearing the human DHAPAT cDNA recovered DHAPAT activity and plasmalogen biosynthesis. Examination of clonal isolates from the transfected population showed that recovery of as little as 10% of wild type DHAPAT activity restored plasmalogen levels to 55% of normal while in one isolate, NRel-4.15, which over-expressed DHAPAT activity 6-fold over wild-type cells, plasmalogen levels were returned only to wild-type values. While the rate of plasmenylethanolamine biosynthesis was restored in NRel-4.15, the biosynthesis of non-ether glycerolipids was either decreased or unaffected suggesting that peroxisomal DHAPAT does not normally contribute to non-ether glycerolipid biosynthesis. The data demonstrate that a defect in the gene that codes for peroxisomal DHAPAT is the primary lesion in the NRel-4 cell line and that the peroxisomal DHAPAT is essential for the biosynthesis of plasmalogens in animal cells.
Revised on January 13, 2005
Accepted on January 19, 2005
Role of dihydroxyacetonephosphate acyltransferase in the biosynthesis of plasmalogens and non-ether glycerolipids: Studies using a plasmalogen-deficient CHO-K1 variant
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