4.7 Article Proceedings Paper

Acetylcholinesterase inhibitors neostigmine and physostigmine inhibit induction of alpha-amylase activity during seed germination in barley, Hordeum vulgare var. Jyoti

Journal

LIFE SCIENCES
Volume 80, Issue 24-25, Pages 2386-2388

Publisher

PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.lfs.2007.02.018

Keywords

acetylcholine; acetylcholinesterase; alpha-amylase; AMO-1618; gibberellic acid; neostigmine; physostigmine; quaternary ammonium compounds; non-neuronal

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Acetylcholine (ACh) is an important neurotransmitter whose non-neuronal biological roles are being widely accepted. ACh and components of its metabolism are present in plants. ACh and some inhibitors of acetylcholinesterase (AChE) share structural similarity (quaternary ammonium group) with some inhibitors of biosynthesis of a plant hormone, gibberellic acid (GA); e.g., 2-Isopropyl-4-dimethylamino-5-methylphenyl-l-piperidine carboxylate methyl chloride (AMO-1618) inhibits GA biosynthesis as well as AChE. The present study explores the possibility that ACh and antiAChE may inhibit GA biosynthesis. Seeds of barley var. Jyoti were germinated in the presence of ACh, its breakdown products choline and acetate, and two antiAChE - neostigmine and physostigmine (all 10(-5) M). Alpha amylase activity in germinating seeds was measured as a reliable indicator of the level of GA biosynthesis. Alpha amylase activity in barley seeds was significantly reduced after 72 h of treatment with antiChE but not by ACh or its breakdown products. Since germinating barley seeds contain AChE, much of the ACh may have been broken down before its uptake. Quaternary ammonium antiChE neostigmine was more effective (50% inhibition at 10(-5) M) as compared to tertiary ammonium physostigmine (15% inhibition at 10(-5) M). ACh, choline, acetate, neostigmine and physostigmine (all 10(-5) M) did not affect formation of starch-iodine complex or activity of alpha-amylase per se. Our results indicate that quaternary ammonium inhibitors of AChE may inhibit GA biosynthesis. (c) 2007 Elsevier Inc. All rights reserved.

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