Changes in the Acetylcholine Titre of Senescing Cotyledons

Lees, George; Lahue, Robert; Thompson, John E.

doi:10.1093/jxb/29.5.1117

Cited by 8 publications

(3 citation statements)

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“…Meanwhile, ACh has been recently identified in a number of non-neuronal tissues in animals, fungi, bacteria, and plants (Wessler et al, 2001;Horiuchi et al, 2003). Although plants lack a nervous system, both ACh and ACh-hydrolyzing activity have been widely recognized in the plant kingdom (Evans, 1972;Jaffe, 1974a, 1974b;Hartmann and Kilbinger, 1974;Verbeek and Vendrig, 1977;Lees et al, 1978;Momonoki and Momonoki, 1991). The ACh-hydrolyzing activities in plant tissues can be measured by the appearance of radioactive acetate following [1][2][3][4][5][6][7][8][9][10][11][12][13][14] C]ACh hydrolysis (Momonoki, 1992), by the appearance of thiol group following acetylthiocholine (ASCh) hydrolysis (Momonoki, 1997), and by histochemical detection of ASCh hydrolysis (Momonoki, 1997;Momonoki et al, 1998).…”

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confidence: 99%

Molecular Characterization of Maize Acetylcholinesterase. A Novel Enzyme Family in the Plant Kingdom

et al. 2005

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Acetylcholinesterase (AChE) has been increasingly recognized in plants by indirect evidence of its activity. Here, we report purification and cloning of AChE from maize (Zea mays), thus providing to our knowledge the first direct evidence of the AChE molecule in plants. AChE was identified as a mixture of disulfide-and noncovalently linked 88-kD homodimers consisting of 42-to 44-kD polypeptides. The AChE hydrolyzed acetylthiocholine and propyonylthiocholine, but not S-butyrylthiocholine, and the AChE-specific inhibitor neostigmine bromide competitively inhibited its activity, implying that maize AChE functions in a similar manner as the animal enzyme. However, kinetic analyses indicated that maize AChE showed a lower affinity to substrates and inhibitors than animal AChE. The full-length cDNA of maize AChE gene is 1,471 nucleotides, which encode a protein having 394 residues, including a signal peptide. The deduced amino acid sequence exhibited no apparent similarity with that of the animal enzyme, although the catalytic triad was the same as in the animal AChE. In silico screening indicated that maize AChE homologs are widely distributed in plants but not in animals. These findings lead us to propose that the AChE family, as found here, comprises a novel family of the enzymes that is specifically distributed in the plant kingdom.

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confidence: 99%

Molecular Characterization of Maize Acetylcholinesterase. A Novel Enzyme Family in the Plant Kingdom

et al. 2005

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“…Hitherto, evidential data of the existence in plants were subsequently reported by many researchers. [6][7][8][9][10][11][12][13][14][15][16][17][18][19] According to Kostir et al 20 and Tung and Raghavan, 21 exogenous ACh influences germination and development at an early growth stage of plants. Bamel et al 22 described that exogenous ACh promotes adventitious root formation in leaf explants from in vitro raised tomato seedlings.…”

Section: Introductionmentioning

confidence: 99%

Acetylcholine promotes the emergence and elongation of lateral roots ofRaphanus sativus

Sugiyama

Tezuka

2011

Plant Signaling & Behavior

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radish (Raphanus sativus L.) was grown on four layers of paper towel moistened with distilled water with and without acetylcholine (ach) for five days in the dark after sowing. ach at 1 nM promoted the growth (emergence and elongation) of lateral roots of radish plants, but had no effect on the stems and main roots. Moreover, ach enhanced the dry weight of roots [main (primary) + lateral roots]. Neostigmine, an inhibitor of acetylcholinesterase (ache) also promoted the emergence and elongation of lateral roots, and atropine, a competitive inhibitor of ach receptor, suppressed the emergence and elongation. ach promoted the activities of glyceraldehyde-3-phosephate dehydrogenase (G-3-PD), nicotinamide adenine dinucleotide-specific isocitrate dehydrogenase (NaD-IcDh), succinate dehydrogenase (SDh) and cytochrome-c oxidase (cyt-c OD) in seedlings. Moreover, ach suppressed the activity of ache and increased the amount of proteins and pyridine nucleotides (NaD and NaDh) in the roots of the seedlings. It also increased the activities of NaDforming enzymes [NaD synthetase and aTP-nicotinamide mononucleotide (aTP-NMN) adenyltransferase], and enhanced the amount of DNa in the roots of the seedlings. The relationship between ach and the emergence and growth of lateral roots was discussed from a biochemical viewpoint.

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“…Além da ACh, suas enzimas de síntese e degradação têm sido amplamente reconhecidas no reino vegetal (EVANS, 1972;FLUCK;JAFFE, 1974a,b;KILBINGER, 1974b;LEES;LAHUE;THOMPSON, 1978;MOMONOKI;MOMONOKI, 1991, SAGANE et al, 2005VERBEEK;VENDRIG, 1977) bem como sítios de ligação da ACh, que corresponderiam aos receptores nicotínicos e muscarínicos, identificados em membranas de células-guarda (MENG et al, 2001). …”

Section: Introductionunclassified

Uma abordagem neurofisiológica da acetilcolina em plantas de milho hidratadas e sob condições de estresse hídrico

Daneluzzi¹

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Changes in the Acetylcholine Titre of Senescing Cotyledons

Cited by 8 publications

References 1 publication

Molecular Characterization of Maize Acetylcholinesterase. A Novel Enzyme Family in the Plant Kingdom

Molecular Characterization of Maize Acetylcholinesterase. A Novel Enzyme Family in the Plant Kingdom

Acetylcholine promotes the emergence and elongation of lateral roots ofRaphanus sativus

Uma abordagem neurofisiológica da acetilcolina em plantas de milho hidratadas e sob condições de estresse hídrico

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