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Retinoids Inhibit Human Epidermal Keratinocyte RNase P Activity
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E. Papadimou
Published/Copyright:
June 1, 2005
Abstract
Ribonuclease P (RNase P) is a ubiquitous and essential enzyme that endonucleolytically cleaves all tRNA precursors to produce the mature 5'-end. We have investigated the effect of synthetic rertinoids (all-trans retinoic acid, acitretin) and arotinoids (Ro 13-7410, Ro 15-0778, Ro, 13-6298 and Ro 15-1570) on RNase P activity isolated for the first time from normal human epidermal keratinocytes (NHEK). All tested compounds but one (Ro 15-1570) revealed a dose-dependent inhibition of RNase P activity, indicating that they may have a direct effect on tRNA biogenesis. Detailed kinetic analysis showed that all retinoids behave as classic competitive inhibitors. On the basis of the Ki values Ro 13-7410 was found to be the strongest inhibitor among all compounds tested.
:
Published Online: 2005-06-01
Published in Print: 2003-03-14
Copyright © 2003 by Walter de Gruyter GmbH & Co. KG
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- Recombinant RNase Z Does Not Recognize CCA as Part of the tRNA and Its Cleavage Efficieny Is Influenced by Acceptor Stem Length
- HIV-1 TAR as Anchoring Site for Optimized Catalytic RNAs
- Transcription of Different Exons 1 of the Human Neuronal Nitric Oxide Synthase Gene Is Dynamically Regulated in a Cell- and Stimulus- Specific Manner
- Hepatitis B Virus Core Antigen: Enhancement of Its Production in Escherichia coli, and Interaction of the Core Particles with the Viral Surface Antigen
- Determinants of Enzymatic Specificity in the Cys-Met-Metabolism PLP-Dependent Enzyme Family: Crystal Structure of Cystathionine γ-Lyase from Yeast and Intrafamiliar Structure Comparison
- In vitro Uptake and Stability Study of pVEC and Its All-D Analog
- Calpastatin Exon 1B-Derived Peptide, a Selective Inhibitor of Calpain: Enhancing Cell Permeability by Conjugation with Penetratin
- Structure-Activity Relationships of Glucose-Dependent Insulinotropic Polypeptide (GIP)
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