English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Lysophosphatidic acid (LPA), a metabolite of phosphatidic acid (PA) by phospholipases of the A2 type, markedly inhibited the synaptic membrane (Na+ + K+)-ATPase activity from rat cerebral cortices in incubation media containing free Ca2+ concentrations below 4.7 x 10(-6) M. This effect of LPA was dose-dependent, and the minimum effective concentration was 10(-6) g/ml. The inhibitory action of LPA was more potent than that of PA. Lysophosphatidylinositol (LPI) and lysophosphatidylethanolamine (LPE) at 10(-5) g/ml had little or no effect on this enzyme activity. These results suggest that LPA may partly play a role in the depolarization and/or increase in intracellular calcium concentrations in the brain.

Inhibition of synaptosomal (Na++K+)-ATPase activity by lysophosphatidic acid: Its possible role in membrane depolarization.