High-Throughput Screening Assay for Sphingosine Kinase Inhibitors in Whole Blood Using RapidFire® Mass Spectrometry
| Autor: | Olga V. Nemirovskiy, Jaime L. Masferrer, Grace E. Munie, William A. LaMarr, Maureen K. Highkin, John W. Rains, Marek M. Nagiec, Matthew P. Yates |
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| Rok vydání: | 2011 |
| Předmět: |
Sphingosine metabolism
High-throughput screening Sphingosine kinase Aminophenols Mass spectrometry Biochemistry Mass Spectrometry Analytical Chemistry chemistry.chemical_compound Sphingosine High-Throughput Screening Assays Humans Enzyme Inhibitors Whole blood Chromatography Dose-Response Relationship Drug Kinetics Phosphotransferases (Alcohol Group Acceptor) Thiazoles chemistry Homogeneous Molecular Medicine lipids (amino acids peptides and proteins) Lysophospholipids Signal Transduction Biotechnology |
| Zdroj: | SLAS Discovery. 16:272-277 |
| ISSN: | 2472-5552 |
| Popis: | To facilitate discovery of compounds modulating sphingosine-1-phosphate (S1P) signaling, the authors used high-throughput mass spectrometry technology to measure S1P formation in human whole blood. Since blood contains endogenous sphingosine (SPH) and S1P, mass spectrometry was chosen to detect the conversion of an exogenously added 17-carbon-long variant of sphingosine, C17SPH, into C17S1P. The authors developed procedures to achieve homogeneous mixing of whole blood in 384-well plates and for a method requiring minimal manipulations to extract S1P from blood in 96- and 384-well plates prior to analyses using the RapidFire(®) mass spectrometry system. |
| Databáze: | OpenAIRE |
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