Postnatal Changes in the Activity Ratio of Specific and Nonspecific Cholinesterases from Neuronal Perikarya

Ochoa, Enrique L. M.; Brusco, Alicia; Idoyaga-Vargas, Víctor; Carminatti, Héctor

doi:10.1111/j.1471-4159.1982.tb07896.x

Cited by 11 publications

(3 citation statements)

References 25 publications

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“…In the absence of any biochemically verifiable interaction with membrane lipids, it is difficult to reconcile our results with those hypotheses linking BuChE with any significant membrane-associated function, be it in glia or neuron (Davis and Koelle, 1978;Graybiel and Ragsdale, 1982;Ochoa et al, 1982). Nor are these data consistent with any simple interconvertibility of the two enzymes (Koelle et al, 1979), at least in CNS tissue.…”

Section: Resultscontrasting

confidence: 75%

“…Also, according to Graybiel and Ragsdale (1982), BuChE in the monkey brain shows a distinct neuronal localization that is different from that of AChE, suggesting that the enzyme or its substrate may act as a neuroactive substance in the primate visual system. Similarly, Ochoa et al (1982) have shown that BuChE activity is present, albeit in low activity, not only in isolated neuronal peri-karya, but in synaptosomal and microsomal fractions as well.…”

Section: Introductionmentioning

confidence: 77%

“…Recently, however, this matter has become controversial. Thus, while electron microscopic studies in rat cerebellum (Clos et al, 1980) have confirmed the glial and endothelial localization, several other studies (Davis and Koelle, 1978;Graybiel and Ragsdale, 1982;Ochoa et al, 1982) have indicated neuronal localization for the enzyme as well. Indeed, according to Davis and Koelle (1982), in the cat superior cervical ganglia, BuChE is localized in the postsynaptic membranes of the postganglionic neurons, a localization identical to that found for AChE (EC 3.1.1.7).…”

Section: Introductionmentioning

confidence: 89%

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Is Butyrylcholinesterase of the Rat CNS a Membrane‐Bound Enzyme?

Meisami

1984

Journal of Neurochemistry

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The study of Arrhenius plots for acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) activity from the rat brain and spinal cord revealed that in contrast to AChE, which exhibited biphasic Arrhenius plots with a distinct break (transition temperature) at about 16-18 degrees C, BuChE showed no evidence of discontinuity and a higher activation energy in the physiological range of temperature. The results indicate lack of lipid-protein interaction in the case of BuChE of the CNS tissue. It is inferred that BuChE, in contrast to AChE, is not bound in any significant way to cellular membranes of the CNS tissue.

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Section: Resultscontrasting

confidence: 75%

Section: Introductionmentioning

confidence: 77%

Section: Introductionmentioning

confidence: 89%

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Is Butyrylcholinesterase of the Rat CNS a Membrane‐Bound Enzyme?

Meisami

1984

Journal of Neurochemistry

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Temperature effects on cholinesterases from rat brain capillaries

Catalán

Hernández

1986

Bioscience Reports

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The activities of acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) in rat brain capillaries were measured as a function of temperature. Arrhenius plots of the data revealed that AChE exhibits a biphasic Arrhenius plot with a distinct break (transition temperature) at about 15.2 kcal/mol. In contrast, BuChE did not show evidence of discontinuity. BuChE showed an activation energy higher than that of AChE in the physiological range of temperature. These data suggest a lack of lipid-protein interaction in the case of BuChE. Although the possibility exists that BuChE is weakly anchored to the membranes, our results indicate that BuChE is not bound, at least significantly, to cellular membranes in brain capillaries as is AChE.

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Desensitization of central cholinergic mechanisms and neuroadaptation to nicotine

Ochoa

McNamee

1990

Mol Neurobiol

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This review focuses on neuroadaptation to nicotine. The first part of the paper delineates some possible general mechanisms subserving neuroadaptation to commonly abused drugs. The postulated role of the mesocorticolimbic neuroanatomical pathway and drug-receptor desensitization mechanisms in the establishment of tolerance to, dependence on, and withdrawal from psychoactive drugs are discussed. The second part of the review deals with the pharmacological effects of nicotine at both pre- and postsynaptic locations within the central nervous system, and the still-perplexing upregulation of brain nicotine-binding sites seen after chronic nicotine administration. A special emphasis has been put on desensitization of presynaptic cholinergic mechanisms, and postsynaptic neuronal nicotinic-receptor function and its modulation by endogenous substances. A comparison with the inactivation process occurring at peripheral nicotinic receptors is also included. Finally, a hypothesis on the possible connections between desensitization of central cholinergic mechanisms and neuroadaptation to nicotine is advanced. A brief comment on the necessity of fully understanding the effects of nicotine on the developing nervous system closes this work.

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Postnatal Changes in the Activity Ratio of Specific and Nonspecific Cholinesterases from Neuronal Perikarya

Cited by 11 publications

References 25 publications

Is Butyrylcholinesterase of the Rat CNS a Membrane‐Bound Enzyme?

Is Butyrylcholinesterase of the Rat CNS a Membrane‐Bound Enzyme?

Temperature effects on cholinesterases from rat brain capillaries

Desensitization of central cholinergic mechanisms and neuroadaptation to nicotine

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