J. Lipid Res. Did you know there is a large type edition? Click here.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on April 1, 2005

Papers In Press, published online ahead of print February 1, 2005
J. Lipid Res., doi:10.1194/jlr.M400364-JLR200
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
M400364-JLR200v1
46/4/727    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Liu, D.
Right arrow Articles by Zoeller, R. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Liu, D.
Right arrow Articles by Zoeller, R. A.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Submitted on September 23, 2004
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

Dailan Liu, Narasimhan Nagan, Wilhelm W. Just, Claus Rodemer, Thanh-Phuong Thai, and Raphael A. Zoeller

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.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
R. Zufferey and C. B. Mamoun
Leishmania major Expresses a Single Dihydroxyacetone Phosphate Acyltransferase Localized in the Glycosome, Important for Rapid Growth and Survival at High Cell Density and Essential for Virulence
J. Biol. Chem., March 24, 2006; 281(12): 7952 - 7959.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Journal of Biological Chemistry 
 Molecular and Cellular Proteomics   ASBMB Today 
Copyright © 2005 by the American Society for Biochemistry and Molecular Biology.