Inhibition of Adenosine Triphosphatase Activity from a Plasma Membrane Fraction of Acer pseudoplatanus Cells by 2,2,2-Trichloroethyl 3,4-Dichlorocarbanilate.
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Journal: 2010/July - Plant Physiology
ISSN: 0032-0889
PUBMED: 16664702
Abstract:
2,2,2-Trichloroethyl 3,4-dichlorocarbanilate (SW26) is toxic for Acer pseudoplatanus cell cultures. It inhibited the cellular proton extrusion and depolarized the plasmalemma. In vitro, it inhibited the plasma membrane ATPase. SW 26 was also inhibitory to membrane ATPases of other origins-plant (maize shoot), fungus (Schizosaccharomyces pombe), and animal (dog kidney)-with about the same efficiency (7.5 micromolar < I(50) < 22 micromolar). It did not inhibit the oligomycin-sensitive ATPase from purified plant mitochondria, nor molybdate-sensitive soluble phosphatases. SW26 was more specific for plasma membrane ATPases than diethylstilbestrol or vanadate. A Lineweaver-Burk plot analysis showed that inhibition kinetics were purely noncompetitive (K(i) = 14.7 micromolar) below 20 micromolar. Above this concentration, the inhibition pattern was not consistent with Michaelis-Menten kinetics, and a Hill plot representation revealed a positive cooperativity.
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Plant Physiol 80(3): 782-785
PMID: 16664702

Inhibition of Adenosine Triphosphatase Activity from a Plasma Membrane Fraction of <em>Acer pseudoplatanus</em> Cells by 2,2,2-Trichloroethyl 3,4-Dichlorocarbanilate <sup><a href="#fn1" rid="fn1" class=" fn">1</a>,</sup><sup><a href="#fn2" rid="fn2" class=" fn">2</a></sup>

Abstract

2,2,2-Trichloroethyl 3,4-dichlorocarbanilate (SW26) is toxic for Acer pseudoplatanus cell cultures. It inhibited the cellular proton extrusion and depolarized the plasmalemma. In vitro, it inhibited the plasma membrane ATPase. SW 26 was also inhibitory to membrane ATPases of other origins—plant (maize shoot), fungus (Schizosaccharomyces pombe), and animal (dog kidney)—with about the same efficiency (7.5 micromolar < I50 < 22 micromolar). It did not inhibit the oligomycin-sensitive ATPase from purified plant mitochondria, nor molybdate-sensitive soluble phosphatases. SW26 was more specific for plasma membrane ATPases than diethylstilbestrol or vanadate. A Lineweaver-Burk plot analysis showed that inhibition kinetics were purely noncompetitive (Ki = 14.7 micromolar) below 20 micromolar. Above this concentration, the inhibition pattern was not consistent with Michaelis-Menten kinetics, and a Hill plot representation revealed a positive cooperativity.

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Selected References

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  • Balke NE, Hodges TK. Effect of diethylstilbestrol on ion fluxes in oat roots. Plant Physiol. 1979 Jan;63(1):42–47.[PMC free article] [PubMed] [Google Scholar]
  • Balke NE, Hodges TK. Inhibition of adenosine triphosphatase activity of the plasma membrane fraction of oat roots by diethylstilbestrol. Plant Physiol. 1979 Jan;63(1):48–52.[PMC free article] [PubMed] [Google Scholar]
  • Dulley JR. Determination of inorganic phosphate in the presence of detergents or protein. Anal Biochem. 1975 Jul;67(1):91–96. [PubMed] [Google Scholar]
  • Dupont FM, Burke LL, Spanswick RM. Characterization of a partially purified adenosine triphosphatase from a corn root plasma membrane fraction. Plant Physiol. 1981 Jan;67(1):59–63.[PMC free article] [PubMed] [Google Scholar]
  • Etherton B. Evidence for amino Acid-h co-transport in oat coleoptiles. Plant Physiol. 1978 Jun;61(6):933–937.[PMC free article] [PubMed] [Google Scholar]
  • Gallagher SR, Leonard RT. Effect of vanadate, molybdate, and azide on membrane-associated ATPase and soluble phosphatase activities of corn roots. Plant Physiol. 1982 Nov;70(5):1335–1340.[PMC free article] [PubMed] [Google Scholar]
  • Komor E. Proton-coupled hexose transport in Chlorella vulgaris. FEBS Lett. 1973 Dec 15;38(1):16–18. [PubMed] [Google Scholar]
  • Komor E, Tanner W. The hexose-proton symport system of Chlorella vulgaris. Specificity, stoichiometry and energetics of sugar-induced proton uptake. Eur J Biochem. 1974 May 2;44(1):219–223. [PubMed] [Google Scholar]
  • Leonard RT, Hotchkiss CW. Cation-stimulated Adenosine Triphosphatase Activity and Cation Transport in Corn Roots. Plant Physiol. 1976 Sep;58(3):331–335.[PMC free article] [PubMed] [Google Scholar]
  • LOWRY OH, ROSEBROUGH NJ, FARR AL, RANDALL RJ. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  • MITCHELL P. Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism. Nature. 1961 Jul 8;191:144–148. [PubMed] [Google Scholar]
  • Nagahashi G, Leonard RT, Thomson WW. Purification of plasma membranes from roots of barley: specificity of the phosphotungstic Acid-chromic Acid stain. Plant Physiol. 1978 Jun;61(6):993–999.[PMC free article] [PubMed] [Google Scholar]
Laboratoire des Herbicides et Autres Produits Phytosanitaires, I.N.R.A., BV 1540, 21034 Dijon Cedex (France)
Laboratoire de Chimie Organique et Biologique, E.N.S.A., 145 av de Muret, Toulouse Cedex (France)
Supported by the Institut National de la Recherche Agronomique (Ministère de l'Agriculture and Ministère de la Recherche et de la Technologie); The Institut National Polytechnique de Toulouse (Ministère de l'Education Nationale); and the Société Nationale des Poudres et Explosifs.
All requests about 2,2,2-trichloroethyl 3,4-dichlorocarbanilate should be sent to Dr. Blein or Dr. Scalla.
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Abstract
2,2,2-Trichloroethyl 3,4-dichlorocarbanilate (SW26) is toxic for Acer pseudoplatanus cell cultures. It inhibited the cellular proton extrusion and depolarized the plasmalemma. In vitro, it inhibited the plasma membrane ATPase. SW 26 was also inhibitory to membrane ATPases of other origins—plant (maize shoot), fungus (Schizosaccharomyces pombe), and animal (dog kidney)—with about the same efficiency (7.5 micromolar < I50 < 22 micromolar). It did not inhibit the oligomycin-sensitive ATPase from purified plant mitochondria, nor molybdate-sensitive soluble phosphatases. SW26 was more specific for plasma membrane ATPases than diethylstilbestrol or vanadate. A Lineweaver-Burk plot analysis showed that inhibition kinetics were purely noncompetitive (Ki = 14.7 micromolar) below 20 micromolar. Above this concentration, the inhibition pattern was not consistent with Michaelis-Menten kinetics, and a Hill plot representation revealed a positive cooperativity.
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