J. Lipid Res. Neurobiology of Lipids (ISSN1683-5506)
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A more recent version of this article appeared on January 1, 2004

Papers In Press, published online ahead of print October 1, 2003
J. Lipid Res., doi:10.1194/jlr.M300279-JLR200
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Submitted on June 24, 2003
Revised on September 3, 2003
Accepted on September 16, 2003

PPARalpha controls the intracellular coenzyme A concentration via regulation of PANK1alpha gene expression

Gayathri Ramaswamy, Mohammad A. Karim, K. Gopal Murti, and Suzanne Jackowski

Infectious Diseases, St. Jude Children's Research Hospital, Memphis, TN 38105-2794

Corresponding Author: suzanne.jackowski{at}stjude.org

Pantothenate kinase (PanK) is thought to catalyze the first rate-limiting step in Coenzyme A (CoA) biosynthesis. The full-length cDNA encoding the human PanK1alpha protein was isolated and the complete human PANK1 gene structure was determined. Bezafibrate, a hypolipidemic drug and a PPARalpha agonist, specifically increased hPANK1alpha mRNA expression in human hepatoblastoma (HepG2) cells as a function of time and dose of the drug, compared to hPANK1alpha , hPANK2 and hPANK3, which did not significantly increase. Four putative PPARalpha response elements were identified in the PANKIalpha promoter and bezafibrate stimulated hPANK1alpha promoter activity, but did not alter the mRNA half-life. Increased hPANK1alpha mRNA resulted in higher hPanK1 protein, localized in the cytoplasm, and elevated PanK enzyme activity. The enhanced hPANK1alpha gene expression translated into increased activity of the CoA biosynthetic pathway and established a higher steady-state CoA level in HepG2 cells. These data are consistent with a key role for PanK1alpha in the control of cellular CoA content and point to the PPARalpha transcription factor as a major factor that governs hepatic CoA levels by specific modulation of PANK1alpha gene expression.


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