de Potas_1993_Comp.Biochem.Physiol.C_106_561

Reference

Title : Phosphoinositide phosphorylation and shape changes produced by phosmet- oxon in human erythrocytes - de Potas_1993_Comp.Biochem.Physiol.C_106_561
Author(s) : de Potas GM , de DAAM
Ref : Comparative Biochemistry & Physiology C , 106 :561 , 1993
Abstract :

1. "In vitro" incubation of red blood cells with phosmetoxon induced crenated and invaginated forms. 2. [32P] phosphate incorporation was greater in membranes from erythrocytes exposed to 300 nM phosmetoxon for 10 min than in control cells. 3. The highest incorporation was for phosphatidylinositol (PI), followed by phosphatidylinositol phosphate (PIP) and phosphatidylinositolbiphosphate (PIP2). 4. An activation of phosphatidylinositol (PI) kinase was detected with 150 and 300 nM of the pesticide, while there was no change in poliphosphoinositides (PPI) phosphodiesterase activity. 5. Results suggest an association between changes in PI kinase activity, the phosphorylation cycle of phosphatidylinositols and alterations in erythrocyte morphology induced by phosmetoxon.

PubMedSearch : de Potas_1993_Comp.Biochem.Physiol.C_106_561
PubMedID: 7904927

Related information

Inhibitor Phosmetoxon

Citations formats

de Potas GM, de DAAM (1993)
Phosphoinositide phosphorylation and shape changes produced by phosmet- oxon in human erythrocytes
Comparative Biochemistry & Physiology C 106 :561

de Potas GM, de DAAM (1993)
Comparative Biochemistry & Physiology C 106 :561