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Papers In Press, published online ahead of print September 8, 2005
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Department of Metabolism Section, 111F, University of California San Francisco, San Francisco, CA 94121
Corresponding Author: yanjennyjiang{at}yahoo.com
LXRs and PPARs are potent regulators of keratinocyte proliferation, differentiation and epidermal permeability barrier homeostasis. Cholesterol sulfotransferase, isoform 2B1b (SULT2B1b), is a key enzyme in the synthesis of cholesterol sulfate, a critical regulator of keratinocyte differentiation and desquamation, as well as a precursor of a portion of the cholesterol that mediates barrier homeostasis. In this study, we assessed the effect of activators of LXR, PPARa, PPARß/d and PPAR on SULT2B1b gene expression and enzyme activity in cultured human keratinocyte (CHK). Our results demonstrate that PPAR and LXR activators increase SULT2B1b mRNA levels, with the most dramatic effect (26-fold increase) induced by the PPAR activator, ciglitazone. Ciglitazone up-regulates SULT2B1b mRNA in a dose- and time-dependent manner. Moreover, the stimulation of SULT2B1b gene expression by LXR and PPARs activators occurs in both undifferentiated and differentiated CHK. The up-regulation of SULT2B1b by ciglitazone appears to occur at a transcriptional level, since the degradation of SULT2B1b is not accelerated by ciglitazone. In addition, cycloheximide almost completely blocks the ciglitazone-induced increase in SULT2B1b mRNA, indicating that the translation of SULTB1b mRNA is dependent on new protein synthesis. Finally, LXR and PPAR activators also increased the activity of cholesterol sulfotransferase activity. Thus, LXR and PPAR activators regulate the expression of SULT2B1b, the key enzyme in the synthesis of cholesterol sulfate, which is a potent regulator of epidermal differentiation and corneocyte desquamation.
Revised on August 26, 2005
Accepted on September 1, 2005
LXR and PPAR activators stimulate cholesterol sulfotransferase (SULT2B1b) in human keratinocytes
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