THE EFFECT OF SPERMINE AND SPERMIDINE ON THE HYDROLYSIS OF ACETYLTHIOCHOLINE IN THE PRESENCE OF RAT CAUDATE NUCLEUS HOMOGENATE OR ACETYLCHOLINESTERASE FROM <i>ELECTROPHORUS ELECTRICUS</i>

Anand, Rashmi; Gore, Michael G.; Kerkut, G.A.

doi:10.1111/j.1471-4159.1976.tb12257.x

Cited by 21 publications

(3 citation statements)

References 15 publications

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“…It is therefore assumed that polyamines exert their effect by another mechanism. Polyamines were found to play a role in the regulation of AChE activity (Kossorotow et al, 1974;Anand et al, 1976;Peter et al, 1979). In the present work, however, no effect of polyamines on CAT activity could be detected.…”

Section: Discussioncontrasting

confidence: 68%

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Reciprocal Regulation of Ornithine Decarboxylase and Choline Kinase Activities by Their Respective Reaction Products in the Developing Rat Cerebellar Cortex

Gilad

1984

Journal of Neurochemistry

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Changes in the activity of choline kinase were measured in the cerebellum during development. Early transient increase was found in the enzyme activity just prior to and during birth. This period of increase did not coincide with the periods of transient elevation in ornithine decarboxylase and choline acetyltransferase previously observed in the developing cerebellum. The effects of the naturally occurring polyamines (putrescine, spermidine, and spermine) on choline kinase and choline acetyltransferase activities, and of phosphorylcholine (the product of the reaction catalyzed by choline kinase) on ornithine decarboxylase and choline acetyltransferase activities, were also examined. Choline acetyltransferase activity was not influenced by either polyamines or phosphorylcholine. However, choline kinase activity from 7-day-old, but not from adult, cerebellum was increased 25% in the presence of 4 mM spermine. In contrast, low spermidine concentrations (less than 2 mM) inhibited choline kinase activity selectively in 7-day-old cerebellum. Ornithine decarboxylase activity from 7-day-old cerebellum was inhibited in a concentration-dependent manner by phosphorylcholine. The present data together with other previous reports suggest that: (a) polyamines may play a role in choline utilization during development via their regulation of choline kinase activity, on the one hand, and of acetylcholinesterase activity on the other; and (b) during development, a reciprocal regulation of choline kinase and ornithine decarboxylase activities by their respective reaction products may exist, whereby choline kinase activity is regulated in a complex manner by polyamines and, in turn, ornithine decarboxylase is inhibited by phosphorylcholine.

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Section: Discussioncontrasting

confidence: 68%

“…Polyamines were observed to affect AChE activity in a complex manner (Kossorotow e t al., 1974;Anand et at., 1976). Thus polyamines (e.g.,…”

mentioning

confidence: 99%

Reciprocal Regulation of Ornithine Decarboxylase and Choline Kinase Activities by Their Respective Reaction Products in the Developing Rat Cerebellar Cortex

Gilad

1984

Journal of Neurochemistry

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“…The l/[S] against l / v plots for the inhibi-tion of acetylcholinesterase by serotonin showed a considerable scattering of the experimental points repeatedly and it was uncertain whether the inhibition was a competitive type or a mixed (competitive-noncompetitive) type. The reasons for this finding are not obvious but it has been pointed out [17] that the amines spermine and spermidine can interact with and cause a non-enzymic hydrolysis of acetylthiocholine and their inhibition of acetylcholinesterase was more at higher substrate concentrations. Apparently more detailed investigations into the nature of inhibition of the monkey brain acetylcholinesterase by serotonin will be needed.…”

Section: Nature Of Inhibition Of Aryl Acylamidase and Acetylcholinestmentioning

confidence: 92%

The Association of the Serotonin‐Sensitive Aryl Acylamidase with Acetylcholinesterase in the Monkey Brain

Oommen

Balasubramanian

1979

European Journal of Biochemistry

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The serotonin-sensitive aryl acylamidase was partially purified from monkey brain. The aryl acylamidase activity was inhibited by serotonin (Ki = 0.425 mM) and tryptamine (Ki = 3.6 mM) but not by a number of other amines. It was also inhibited by acetylcholine (Ki = 2 mM) and its analogues and homologues. The relationship of aryl acylamidase to acetylcholinesterase was examined. The ratios of specific activities of aryl acylamidase and acetylcholinesterase in the different steps of purification were approximately constant and the percentage recoveries of both enzyme activities were comparable. Elution profiles of both enzyme activities from concanavalin-ASepharose, Sephadex G-200 and DEAE-Sephadex A-25 columns were similar. Both enzyme activities migrated in a similar fashion on gel electrophoresis in different percentage gels for different time intervals. Both enzymes showed similar distribution in the various anatomical regions and in the different subcellular fractions of monkey brain.Eserine and neostigmine, potent competitive inhibitors of acetylcholinesterase also potently inhibited aryl acylamidase in a non-competitive manner. Inhibition of both enzymes was 100% at 10 pM of both the inhibitors. Tetraisopropylpyrophosphoramide, a selective inhibitor of pseudocholinesterase, did not inhibit either the brain acetylcholinesterase or aryl acylamidase at 10 pM. Serotonin inhibited acetylcholinesterase only at concentrations above 10 mM. Dixon plots of one inhibitor in the presence of additional inhibitors indicated that serotonin, butyrylcholine, acetylcholine, neostigmine and eserine (all non-competitive inhibitors of aryl acylamidase) acted at the same site as inhibitors of aryl acylamidase.The serotonin-insensitive aryl acylamidase of monkey liver was also insensitive to acetylcholine and eserine and was not found associated with acetylcholinesterase [A. Oommen and A. S. Balasubramanian (1978) Biochem. Pharmacol. 27, 891 -8951. Erythrocyte membrane known to contain true cholinesterase had aryl acylamidase activity sensitive to serotonin, acetylcholine and eserine. All these considerations suggest that the serotonin-sensitive aryl acylamidase activity is a property of true cholinesterase. Although some of the experimental results would suggest that in the monkey brain the two activities may be associated with the same protein with two different active sites further experiments are needed to confirm this.

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Neurobiology of Pyridoxine

Dakshinamurti

1982

Advances in Nutritional Research

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Pyridoxal 5'-phosphate (PLP) is the major coenzymatic form of pyridoxine. There are over one hundred known pyridoxal 5'-phosphate-dependent reactions, most of which are involved in the metabolism of various amino acids . Pyridoxamine 5'-phosphate can function in aminotransf erase reactions by the cyclic regeneration of the two active phosphate forms. Pyridoxal 5'-phosphate-dependent reactions studied in the nervous system are involved in the catabolism of various amino acids.The putative neurotransmitters , dopamine, norepinephrine , serotonin , histamine , aminobutyric acid and taurine , as well as the sphingoiipids and poly amines are synthesized by PLP-dependent enzymes. Of these enzymes, three ( glutamic acid decarboxylase , 5-hydroxytryptophan decarboxylase and crnithine decarboxylase) seem to have crucial roles (Fig. '). The clinical effects of pyridoxine deficiency can be explained on the basis of the known decreases in the activities of these enzymes (1). EXPERIMENTAL PYRIDOXINE DEFICIENCY IN THE NEONATE RATDakshinamurti and Stephens ( 2) first reported the production of congenital pyridoxine deficiency .Our observations extended the "chronic fetal distress" hypothesis of Gruenwald ( 3) to include effects on the development of the central nervous system. We later showed that a deficiency of pyridoxine in rat pups could be produced by depriving the dam of dietary pyridoxine during lactation (4). Such a deficiency has been characterized using biochemical and electrophysiological parameters. The electroencephalogram (EEG)

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THE EFFECT OF SPERMINE AND SPERMIDINE ON THE HYDROLYSIS OF ACETYLTHIOCHOLINE IN THE PRESENCE OF RAT CAUDATE NUCLEUS HOMOGENATE OR ACETYLCHOLINESTERASE FROM ELECTROPHORUS ELECTRICUS

Cited by 21 publications

References 15 publications

Reciprocal Regulation of Ornithine Decarboxylase and Choline Kinase Activities by Their Respective Reaction Products in the Developing Rat Cerebellar Cortex

Reciprocal Regulation of Ornithine Decarboxylase and Choline Kinase Activities by Their Respective Reaction Products in the Developing Rat Cerebellar Cortex

The Association of the Serotonin‐Sensitive Aryl Acylamidase with Acetylcholinesterase in the Monkey Brain

Neurobiology of Pyridoxine

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