Fodrin Inhibits Phospholipases A2, C, and D by Decreasing Polyphosphoinositide Cell Content
| Autor: | Sandra Lukowski, Jean-Paul Mira, Alain Zachowski, Blandine Geny |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
Phosphatidylinositol 4
5-Diphosphate Cell Biophysics HL-60 Cells Nerve Tissue Proteins Phospholipase Biology Biochemistry Phospholipases A Cofactor law.invention chemistry.chemical_compound Phosphatidylinositol Phosphates law Phospholipase D medicine Humans Spectrin Phosphatidylinositol Enzyme Inhibitors Molecular Biology Microfilament Proteins Cell Biology Recombinant Proteins Cell biology Enzyme Activation Phospholipases A2 stomatognathic diseases Cytosol medicine.anatomical_structure chemistry Type C Phospholipases Recombinant DNA biology.protein lipids (amino acids peptides and proteins) Streptolysin Guanosine Triphosphate Carrier Proteins |
| Zdroj: | Biochemical and Biophysical Research Communications. 248:278-284 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.1998.8942 |
| Popis: | Brain fodrin inhibited in a dose dependent manner the GTPγS-stimulated cytosolic PLA 2 (cPLA 2 ), PLC, and PLD activities in differentiated HL-60 cells permeabilized with streptolysin O. cPLA 2 and PLD were inhibited by the same concentrations of fodrin (IC 50 =1.5–2 nM) but PLC was inhibited by lower concentrations (IC 50 =0.3 nM). Moreover, the rates of inhibition were different between the phospholipases. Spectrin, which shares 50% homology with fodrin, had similar effects on the three phospholipases. However, using cytosol-depleted cells or recombinant PLD1, we showed that fodrin was not a direct inhibitor. Studying the potential mechanisms of these inhibitions, we demonstrated that a major decrease in membrane phosphatidylinositol 4-monophosphate (PtdIns(4)P) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P 2 ) amounts was induced by fodrin. Exogenous PtdIns(4,5)P 2 partly reversed fodrin inhibition of GTPγS-stimulated phospholipase C activity. Hence, inhibition of PLC, cPLA 2 , and PLD activities observed with fodrin could be related to the decrease of PtdIns(4,5)P 2 , substrate of PLC, a cofactor of PLD and an enhancer of cPLA2 activity. |
| Databáze: | OpenAIRE |
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