Serine Base Exchange Enzyme Activity Is Modulated by Sphingosine and Other Amphiphilic Compounds: Possible Role of Positive Charge in Increasing the Synthesis of Phosphatidylserine
| Autor: | M. Czarny, Wiktorek-Wójcik M, Jolanta Barańska, Banasiak M, Dariusz Stępkowski |
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| Rok vydání: | 1997 |
| Předmět: |
PLCD3
Thapsigargin Nitrogenous Group Transferases Phosphorylcholine Biophysics Phosphatidylserines Biochemistry Serine chemistry.chemical_compound Sphingosine Microsomes Amphiphile Tumor Cells Cultured Animals Molecular Biology Protein Kinase C Protein kinase C biology Chemistry Glioma Cell Biology Phosphatidylserine Enzyme assay Rats Kinetics Microsomes Liver biology.protein Tetradecanoylphorbol Acetate Cholesterol Esters |
| Zdroj: | Biochemical and Biophysical Research Communications. 241:73-78 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.1997.7774 |
| Popis: | It has been found that sphingosine and sphingosylphosphorylcholine (amphiphilic cations) have a stimulatory, and cholesterol 3-sulfate (an amphiphilic anion), an inhibitory, effect on [14C]serine incorporation into phosphatidylserine in glioma C6 and rat liver microsomes. In glioma intact cells sphingosine stimulates phosphatidylserine synthesis in a process independent of protein kinase C, but suppressed by thapsigargin. We suggest that the stimulation of the enzyme occurs by the interaction of amphiphilic cations with the membrane cosubstrate phospholipids, leading to a charge redistribution on their phosphate groups, and hence facilitating the enzyme action. A new hypothesis concerning the mechanism of the serine base exchange reaction is discussed. |
| Databáze: | OpenAIRE |
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