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J. Lipid Res.
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A more recent version of this article appeared on June 1, 2006

Papers In Press, published online ahead of print March 18, 2006
J. Lipid Res., doi:10.1194/jlr.C600004-JLR200
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Submitted on February 22, 2006
Revised on March 14, 2006
Accepted on March 17, 2006

Cloning and characterization of a cDNA encoding human cardiolipin synthase (hCLS1)

Biao Lu, Fred Y. Xu, Yan J. Jiang, Patrick C. Choy, Grant M. Hatch, Carl Grunfeld, and Kenneth R. Feingold

Metabolism 111F, VA Medical Center, San Francisco, CA 94121

Corresponding Author: kfngld{at}itsa.ucsf.edu

Cardioplin (CL) is a phospholipid localized to the mitochondria and its biosynthesis is essential for mitochondrial structure and function. We report here the identification and characterization of a cDNA encoding the first mammalian cardiolipin synthase (CLS1) in humans and mice. This cDNA exhibits sequence homology with members of a CLS gene family that share similar domain structure and chemical properties. Expression of the hCLS1 cDNA in reticulocyte lysates or insect cells led to a marked increase in CLS activity. The enzyme is specific for CL synthesis because no significant increase in phosphatidylglycerol phosphate synthase activity was observed. In addition, CL pool size was increased in hCLS1-overexpressing cells as compared to controls. Furthermore, the hCLS1 gene was highly expressed in tissues such as heart, skeletal muscle, and liver, which have been shown to have high CLS activities. These results demonstrate that hCLS1 encodes an enzyme that synthesizes CL.


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