Bioactivatable, Membrane-Permeant Analogs of Cyclic Nucleotides as Biological Tools for Growth Control of C6 Glioma Cells
-
M. Bartsch
Abstract
In the present study, the cAMP analogs 8-bromocAMP (8-Brc-AMP), N6-2'O-dibutyryl-cAMP (DBcAMP) and 8-parachlorophenylthio-cAMP (8-CPT-cAMP), as well as the corresponding cAMP-acetoxymethyl (AM)-ester-prodrugs were tested in a HPLC study for their membrane permeability, intracellular accumulation and biotransformation. Antiproliferative activities of these compounds were studied in the rat C6 glioma cell line. Chromatographic analysis revealed that the AM-ester analogs of the cyclic nucleotides penetrate quantitatively into rat C6 glioma cells and generate high amounts of their parent cyclic nucleotides intracellularly within 60 min; however, longterm growth inhibition tested in C6 cells is only slightly enhanced with the AM-ester prodrugs of 8-Br-cAMP or DBcAMP.
Copyright © 2003 by Walter de Gruyter GmbH & Co. KG
Articles in the same Issue
- Paper of the Year 2002
- Terminal Differentiation of Epithelia
- Use of Detergents to Study Membrane Rafts: The Good, the Bad, and the Ugly
- Protein Structure Similarity as Guiding Principle for Combinatorial Library Design
- The Making of a Professional Secretory Cell: Architectural and Functional Changes in the ER during B Lymphocyte Plasma Cell Differentiation
- No Superoxide Dismutase Activity of Cellular Prion Protein in vivo
- A Nucleosome-Free dG-dC-Rich Sequence Element Promotes Constitutive Transcription of the Essential Yeast RIO1 Gene
- Phosphatidylinositol-3,5-Bisphosphate Is a Potent and Selective Inhibitor of Acid Sphingomyelinase
- Function and Structure of N-Terminal and C-Terminal Domains of Calcineurin B Subunit
- Verification of the Interaction of a Tryparedoxin Peroxidase with Tryparedoxin by ESI-MS/MS
- Kinin-B1 Receptors in Ischaemia-Induced Pancreatitis: Functional Importance and Cellular Localisation
- Bioactivatable, Membrane-Permeant Analogs of Cyclic Nucleotides as Biological Tools for Growth Control of C6 Glioma Cells
- Human Cathepsin H: Deletion of the Mini-Chain Switches Substrate Specificity from Aminopeptidase to Endopeptidase
- Nitridergic Platelet Pathway Activation by Hementerin, a Metalloprotease from the Leech Haementeria depressa
Articles in the same Issue
- Paper of the Year 2002
- Terminal Differentiation of Epithelia
- Use of Detergents to Study Membrane Rafts: The Good, the Bad, and the Ugly
- Protein Structure Similarity as Guiding Principle for Combinatorial Library Design
- The Making of a Professional Secretory Cell: Architectural and Functional Changes in the ER during B Lymphocyte Plasma Cell Differentiation
- No Superoxide Dismutase Activity of Cellular Prion Protein in vivo
- A Nucleosome-Free dG-dC-Rich Sequence Element Promotes Constitutive Transcription of the Essential Yeast RIO1 Gene
- Phosphatidylinositol-3,5-Bisphosphate Is a Potent and Selective Inhibitor of Acid Sphingomyelinase
- Function and Structure of N-Terminal and C-Terminal Domains of Calcineurin B Subunit
- Verification of the Interaction of a Tryparedoxin Peroxidase with Tryparedoxin by ESI-MS/MS
- Kinin-B1 Receptors in Ischaemia-Induced Pancreatitis: Functional Importance and Cellular Localisation
- Bioactivatable, Membrane-Permeant Analogs of Cyclic Nucleotides as Biological Tools for Growth Control of C6 Glioma Cells
- Human Cathepsin H: Deletion of the Mini-Chain Switches Substrate Specificity from Aminopeptidase to Endopeptidase
- Nitridergic Platelet Pathway Activation by Hementerin, a Metalloprotease from the Leech Haementeria depressa
