Tissue Specificity of Dopamine Effects on Brain ATPases

Overview

Journal Neurochem Res

Specialties Chemistry
Neurology

Date 1981 Sep 1

PMID 6119633

Citations 6

Authors

M Antonelli de Gomez de Lima

G Rodriquez de Lores Arnaiz

Affiliations

Soon will be listed here.

Abstract

Dopamine inhibits Mg2+,Na+,K+- and Na+,K+-ATPase activities but does not modify Mg2+-ATPase activity of nerve ending membranes isolated from rat cerebral cortex. In the presence of the soluble fraction of brain, dopamine activates total, Na+,K+-, and Mg2+-ATPases. Dopamine stimulation of nerve ending membrane ATPases is achieved when soluble fractions of brain, kidney, or liver are used. On the other hand, dopamine effects are not observed on kidney or heart ATPase preparations. The results indicate tissue specificity of dopamine effect with respect to the enzyme source; there is no tissue specificity for the requirement of the soluble fraction to achieve stimulation of ATPases by dopamine.

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Partial characterization of an endogenous factor which modulates the effect of catecholamines on synaptosomal Na+, K+-ATPase.

Rodriguez de Lores Arnaiz G, Antonelli de Gomez de Lima M Neurochem Res. 1986; 11(7):933-47.

PMID: 3018605 DOI: 10.1007/BF00965584.

The inhibitory activity of a brain extract on synaptosomal Na+, K+-ATPase is sensitive to carboxypeptidase A and to chelating agents.

Antonelli de Gomez de Lima M, Rodriquez de Lores Arnaiz G Neurochem Res. 1988; 13(3):237-41.

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Different properties of two brain extracts separated in Sephadex G-50 that modify synaptosomal ATPase activities.

Rodriguez de Lores Arnaiz G, Antonelli de Gomez de Lima M, Girardi E Neurochem Res. 1988; 13(3):229-35.

PMID: 2455236 DOI: 10.1007/BF00971538.

Effect of tissue specificity of brain soluble fractions on Na+, K(+)-ATPase activity.

Rodriguez de Lores Arnaiz G Neurochem Res. 1990; 15(3):289-94.

PMID: 2164167 DOI: 10.1007/BF00968674.

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