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Effect of acetylcholine and acetylcholinesterase on the activity of contractile vacuole of Amoeba proteus

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Abstract

Acetylcholine (ACh, 1 μM) stimulates the activity of contractile vacuole of the amoeba Amoeba proteus. The ACh action is not reproduced by ACh analogs carbacholine and 5-methylfurmethide that are not hydrolized by acetylcholinesterase (AChE). The ACh effect is not blocked by M-cholinolytics (atropine and metylone), but is suppressed by the N-cholynolytic tubocurarine (0.01 μM). The AChE inhibitors eserine (0.001 μM) and armine (0.01 μM) suppress action of ACh on the amoeba contractile vacuole. ACh does not affect the contractile vacuole activation produced by arginine-vasopressin (AVP, 1 μM), but blocks the contractile vacuole activation caused by the ligand of opioid receptors dynorphin A (1–13) at a concentration of 0.1 μM. Based on comparison of the obtained results with literature data, the conclusion is drawn that, in the described ACh effects, the enzyme AChE plays the role of synergist, but not of antagonist. Regulation of the contractile vacuole activity and, hence, the water-salt homeostasis of A. proteus is provided by three independent mechanisms through receptors of the AVP, ACh, and opioid systems.

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Abbreviations

AVP:

arginine-vasopressin

ADH:

antidi-uretic hormone

Ach:

acetylcholine

AchE:

acetylcholinesterase

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Authors and Affiliations

  1. Sechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, St. Petersburg, Russia

    Ya. Yu. Bagrov & N. B. Manusova

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  1. Ya. Yu. Bagrov
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  2. N. B. Manusova
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Correspondence to N. B. Manusova.

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Bagrov, Y.Y., Manusova, N.B. Effect of acetylcholine and acetylcholinesterase on the activity of contractile vacuole of Amoeba proteus . Cell Tiss. Biol. 5, 619–624 (2011). https://doi.org/10.1134/S1990519X11060022

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