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ARS Home » Midwest Area » Peoria, Illinois » National Center for Agricultural Utilization Research » Crop Bioprotection Research » Research » Publications at this Location » Publication #76051

Title: ASPIRIN INHIBITION AND ACETYLATION OF THE PLANT CYTOCHROME P450, ALLENE OXIDE SYNTHASE, RESEMBLES THAT OF ANIMAL PROSTAGLANDIN ENDOPEROXIDE H SYNTHASE

Author
item PAN, ZHIQIANG
item CAMARA, BILAL
item Gardner, Harold
item BACKHAUS, RALPH

Submitted to: Journal of Biological Chemistry
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 5/1/1998
Publication Date: N/A
Citation: N/A

Interpretive Summary: It is known that salicylic acid has an important role in the defense of plants from pathogens, but the manner by which it functions is little known. It was demonstrated in this work that salicylic acid and acetylsalicylate (aspirin) inhibit a lipid signalling pathway involved in defense from pathogens as well as initiation of plant aging. Interestingly, the inhibition of lipid signalling by aspirin is similar to the inhibition of lipid signalling in animals These results may explain why aspirin has been used to prolong the life of cut flowers, and this may suggest other uses in the treatment of plants.

Technical Abstract: Aspirin causes a time-dependent inhibition and acetylation of the plant enzyme, allene oxide synthase (AOS), by a reaction that resembles cyclooxygenase inactivation of prostaglandin endoperoxide synthase (PGHS) in animals. AOS initiates the synthesis of 12-oxo-phytodienoic acid, an octadecanoid lipid signalling intermediate that is known to regulate transcription of defense genes in plants. As with PGHS in animals, the formation of plant autacoids is suppressed by the competitive inhibition of AOS with salicyclic acid and the irreversible inhibition with aspirin. However, because AOS is a cytochrome P450, this represents a new mechanism of action for aspirin, suggesting that this and related nonsteroidal anti-inflammatory drugs might inhibit other P450s having catalytic domains similar to AOS.