PMID: 7540662Jul 1, 1995Paper

Phospholipase A2 down-regulates the affinity of [3H]AMPA binding to rat cortical membranes

Journal of Neurochemistry
K K DevJ M Henley

Abstract

The effects of exogenous phospholipase A2 on the binding of alpha-[3H]amino-3-hydroxy-5-methylisoxazole-4-propionate ([3H]AMPA) to rat cortical membranes in the presence of the chaotrope potassium thiocyanate were assessed. Pretreatment of membranes with secretory phospholipase A2 (sPLA2) elicited a concentration-dependent decrease in specific [3H]AMPA binding due mainly to a decrease in affinity (KD). This observation, together with protease inhibitor and western blot evidence, suggest that the sPLA2 effect is not due to proteolysis. The sPLA2-evoked decrease was temperature and calcium dependent. Inclusion of the specific inhibitor oleoyloxyethyl phosphocholine or preincubation of the enzyme with reducing agents to degrade its secondary structure significantly reduced the sPLA2 inhibition. These results suggest that the effects of sPLA2 arise from an enzymatic action rather than a competitive interaction at the AMPA binding site. However, arachidonic acid, a major metabolite of sPLA2 action, did not cause a similar decrease in the affinity of [3H]AMPA binding. In contrast to the effects on [3H]AMPA binding, sPLA2 caused an increase in [3H]CNQX binding, which is in accordance with the functionality of the AMPA receptor complex...Continue Reading

Citations

Feb 5, 2003·International Journal of Developmental Neuroscience : the Official Journal of the International Society for Developmental Neuroscience·Silvia OliveraDaniel Rodriguez-Ithurralde
Jan 15, 1999·Molecular Neurobiology·K K Dev, J M Henley
Dec 5, 1997·Brain Research. Molecular Brain Research·K K DevJ M Henley

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