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The Inhibitory Activity of a Brain Extract on Synaptosomal Na+, K+-ATPase is Sensitive to Carboxypeptidase A and to Chelating Agents

Overview
Journal Neurochem Res
Specialties Chemistry
Neurology
Date 1988 Mar 1
PMID 2838764
Citations 4
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Abstract

In the present study some properties of an inhibitory extract of synaptosomal membrane Na+, K+-ATPase were investigated. This extract (peak II) was prepared by gel filtration in Sephadex G-50 of a soluble fraction of the rat cerebral cortex. Ultrafiltration of peak II through Amicon membranes indicated that the inhibitor has a low MW (less than 1000). The inhibitory activity was not modified by heating in neutral pH at 95 degrees C for 20 min but it was destroyed by charring in acid pH at 200 degrees C for 120 min. The inhibitory activity decreased by incubation of peak II with carboxypeptidase A. These findings suggest that the factor responsible for the inhibition of Na+, K+-ATPase activity is probably a polypeptide. On the other hand, the inhibition was reverted by the chelators EDTA and EGTA, indicating the participation of an ionic compound as well. The increase of Mg2+ concentration during the enzyme assay did not increase the inhibition, indicating that the ion involved might not be vanadate. It is suggested that both a polypeptide and an ionic compound coparticipate in the inhibitory effect of peak II on Na+, K+-ATPase activity.

Citing Articles

An endogenous factor which interacts with synaptosomal membrane Na+, K(+)-ATPase activation by K+.

Rodriguez de Lores Arnaiz G Neurochem Res. 1993; 18(6):655-61.

PMID: 8389989 DOI: 10.1007/BF00966778.


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.


In search of synaptosomal Na+,K(+)-ATPase regulators.

Rodriguez de Lores Arnaiz G Mol Neurobiol. 1992; 6(4):359-75.

PMID: 1363048 DOI: 10.1007/BF02757941.

References
1.
Rodriguez de Lores Arnaiz G, Mistrorigo de Pacheco M . Regulation of (Na+, K+) adenosinetriphosphatase of nerve ending membranes: action of norepinephrine and a soluble factor. Neurochem Res. 1978; 3(6):733-44. DOI: 10.1007/BF00965996. View

2.
Akagawa K, Hara N, Tsukada Y . Partial purification and properties of the inhibitors of Na, K-ATPase and ouabain-binding in bovine central nervous system. J Neurochem. 1984; 42(3):775-80. DOI: 10.1111/j.1471-4159.1984.tb02749.x. View

3.
Antonelli de Gomez de Lima M, Rodriquez de Lores Arnaiz G . Tissue specificity of dopamine effects on brain ATPases. Neurochem Res. 1981; 6(9):969-77. DOI: 10.1007/BF00965028. View

4.
Lores Arnaiz G, Gomez de Lima M . The effect of several neurotransmitter substances on nerve ending membrane ATPase. Acta Physiol Lat Am. 1981; 31(1):39-44. View

5.
Serfozo P, Vizi E . Effect of noradrenaline and vanadate on sodium, potassium-activated ATPase of human brain cortical homogenate. Neurochem Int. 2010; 5(2):237-44. DOI: 10.1016/0197-0186(83)90120-1. View