Lipocortin inhibition of extracellular and intracellular phospholipases A2 is substrate concentration dependent

80Citations
Citations of this article
6Readers
Mendeley users who have this article in their library.

Abstract

Hydrolysis of Escherichia coli membrane phospholipids by pancreatic phospholipase A2 was inhibited by lipocortin from human monocytes in a substrate dependent manner. Inhibition was completely overcome at substrate concentrations above 250 μM. Lipocortin also inhibited partially purified preparations of two intracellular phospholipases A2, isolated from rat liver mitochondria and rat platelets when these enzymes were assayed at low micromolar concentrations of phosphatidylethanolamine. Inhibition gradually decreased with increasing substrate concentrations both for pancreatic and platelet phospholipase A2 and became completely abolished above 15 and 50 μM phosphatidylethanolamine, respectively. © 1987.

Cite

CITATION STYLE

APA

Aarsman, A. J., Mynbeek, G., van den Bosch, H., Rothhut, B., Prieur, B., Comera, C., … Russo-Marie, F. (1987). Lipocortin inhibition of extracellular and intracellular phospholipases A2 is substrate concentration dependent. FEBS Letters, 219(1), 176–180. https://doi.org/10.1016/0014-5793(87)81212-7

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free