Choline acetyltransferase activity in the larval brain of Manduca sexta. Properties and developmental changes

Lester, David S.; Gilbert, Lawrence I.

doi:10.1016/0020-1790(85)90096-4

Cited by 12 publications

(3 citation statements)

References 14 publications

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“…Addition of choline decreases the production of N-acOA in cerebral ganglia homogenates of P. arnericana. With acetyl-CoA and choline available, ChAT would be very active because all of its requirements are fulfilled in this preparation [19]. Increasing the concentration of acetyl-CoA in the incubation decreases the amount of inhibition, which suggests that choline inhibition does not reflect competition with OA at the active site of NAT but, rather, results from competition for the available acetyl-CoA by ChAT and NAT.…”

Section: Discussionmentioning

confidence: 99%

“…However, it is a non-competitive inhibitor when incubated with ChAT prior to the addition of acetyl-CoA [27]. Lester and Gilbert [19] found no inhibition of ChAT from Manduca larvae at 5.0 mM juglone. Pronounced inhibition of NAT from cockroach Malpighian tubules and cerebral gangha is obtained with addition of juglone to the enzyme pre-incubation and subsequent incubation.…”

Section: Discussionmentioning

confidence: 99%

“…Rat pineal NAT is protected from inactivation by DTT, acetyl-CoA, and related compounds [16,17] and inhibited by N-ethylmaleimide and iodoacetic acid [16]. ChAT in insects is also subject to sulfhydryl inhibition [18,19]. Previous studies of NAT in insects included DTT in the enzyme preparation but did not investigate the effect of sulfhydryl inhibitors [2,4].…”

Section: Discussionmentioning

confidence: 99%

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Effects of potential inhibitors on N‐acetylation of octopamine by tissue extracts from malpighian tubules and cerebral ganglia of Periplaneta americana L

Martin

Downer

1989

Arch Insect Biochem Physiol

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N-acetyltransferase activity in extracts of Malpighian tubules and cerebral ganglia from Periplaneta americana L. was monitored using high performance liquid chromatography with coulometric electrochemical detection. Several potential inhibitors were tested against the tissue preparations, and the results indicate distinct differences in the nature of the enzyme derived from the two sources. The Malpighian tubule and cerebral ganglia extracts were sensitive to sulfhydryl inhibition and divalent cations, and both preparations also showed end-product inhibition with coenzyme A. Juglone, an inhibitor of choline acetyltransferase, inhibits N-acetyltransferase activity from both tissues; however, separate studies with choline indicate that the N-acetylation observed in this study is not due to choline acetyltransferase. A number of phenyl, phenol, catechol and indole derivatives were tested and the results indicate that the presence of a 4-hydroxyl group on the phenol ring enhances the capacity of phenol and catechol derivatives to inhibit N-acetyltransferase. Demethylchlordimeform inhibits the production of N-acetyl-p-Octopamine by Malpighian tubule preparations and intact tissues whereas other formamidines, BTS-27271 and amitraz, inhibit N-acetyl-p-Octopamine production only in intact tissues.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Effects of potential inhibitors on N‐acetylation of octopamine by tissue extracts from malpighian tubules and cerebral ganglia of Periplaneta americana L

Martin

Downer

1989

Arch Insect Biochem Physiol

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Developmental changes and acetylcholinesterase activity in the metamorphosing brain of Tenebrio molitor: Correlation to ecdysteroid titers

Lenoir-Rousseaux

Delbecque

Gautron³

1994

Arch Insect Biochem Physiol

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The brain of Tenebrio molitor exhibited marked fluctuations in acetylcholinesterase (AChE) activity throughout metamorphosis. This was true AChE activity, since it was inhibited by high substrate concentrations and by 10 pM of the specific AChE inhibitor BW284C51 [(I ,5-bis'4-allyldimethylammoniumphenyl)-pentan-3-one dibromide] but not by iso-OMPA (tetraisopropylpyrophosphoramide), a cholinesterase (but not AChE) inhibitor. The histochemical AChE activity was localized in the neuropile and the nuclear envelope of neurons and glial cells. The enzyme extracted from brains with 1 O h Triton X-I 00 and 1 M NaCl sedimented as a single peak in a sucrose density gradient, with a sedimentation coefficient of 5.4s. This single AChE sedimentation peak was mainly due to an amphiphilic dimeric form. AChE activity per brain increased in newly ecdysed pupa. AChE activity per milligram of protein exhibited a peak in the mid-pupa which could be correlated to the increase in ecdysteroid titers. o 1994 WiIey-Liss, Inc.

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Acetylcholine

Eldefrawi¹,

Eldefrawi²

1988

Comparative Invertebrate Neurochemistry

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Choline acetyltransferase activity in the larval brain of Manduca sexta. Properties and developmental changes

Cited by 12 publications

References 14 publications

Effects of potential inhibitors on N‐acetylation of octopamine by tissue extracts from malpighian tubules and cerebral ganglia of Periplaneta americana L

Effects of potential inhibitors on N‐acetylation of octopamine by tissue extracts from malpighian tubules and cerebral ganglia of Periplaneta americana L

Developmental changes and acetylcholinesterase activity in the metamorphosing brain of Tenebrio molitor: Correlation to ecdysteroid titers

Acetylcholine

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