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Aspirin inhibits phospholipase C

descriptionPublicationkeyboard_double_arrow_right Article 01 Aug 1986Publisher:Elsevier BVJournal:Biochemical and Biophysical Research Communications, volume 139, pages 115-121 (issn: 0006-291X,

Authors: Mike A. Clark; John S. Bomalaski; Fusao Hirata;

doi: 10.1016/s0006-291x(86)80087-0

pmid: 2945550

Aspirin inhibits phospholipase C

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Abstract

We have shown previously that aspirin (ASA) ingestion by normal human volunteers inhibits peripheral blood monocyte phospholipase C (PLC) activities ex vivo. In order to explore further the mechanism of action of ASA, normal human monocytes and differentiated human U937 cells were treated with ASA and other salicylates. Cells preincubated with ASA were found to have decreased PLC activities. Phospholipase A2 activities were not affected by salicylates. Sodium salicylate and salicylic acid, nonacetylated relatives of ASA also inhibited PLC activity. This effect was dose and time dependent and addition of cycloheximide or actinomycin D to the preincubation mixture abrogated the inhibitory effect of salicylates on PLC. This PLC inhibitory protein induced by ASA appears distinct from lipocortin, a phospholipase A2 inhibitory protein inducible by corticosteroids.

Related Organizations

Smith, Kline & French
United Kingdom
Johns Hopkins University
United States
University of Pennsylvania
United States

Keywords

Aspirin, Annexins, Type C Phospholipases, Indomethacin, Dactinomycin, Humans, Cycloheximide, Salicylates, Glycoproteins

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