Ascorbic acid-like effect of the soluble fraction of rat brain on adenosine triphosphatases and its relation to catecholamines and chelating agents

The inhibitory effect of the soluble fraction of rat brain on the Na +, K +-ATPase, Mg 2+-ATPase and K +- p-nitrophenylphosphatase activities of rat brain subcellular particles and its antagonization by catecholamines have been studied. The soluble fraction could be replaced by l-ascorbic acid in th...

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Veröffentlicht in:Biochemical pharmacology 1974-08, Vol.23 (16), p.2257-2271
Hauptverfasser: Schaefer, András, Seregi, András, Komlós, Márta
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creator Schaefer, András
Seregi, András
Komlós, Márta
description The inhibitory effect of the soluble fraction of rat brain on the Na +, K +-ATPase, Mg 2+-ATPase and K +- p-nitrophenylphosphatase activities of rat brain subcellular particles and its antagonization by catecholamines have been studied. The soluble fraction could be replaced by l-ascorbic acid in the process, but dehydroascorbic acid or cytoplasmic reducing agents such as l-cysteine and l-glutathione did not show the same effect. Catecholamines could be replaced by chelating agents; EDTA, EGTA, o-phenanthroline and α,α'-dipyridyl prevented the inhibition by the soluble fraction and by l-ascorbic acid. The inhibition of the enzyme activities was not prevented by catecholamines or chelators when they were added after preincubation of the enzyme preparation in the presence of soluble fraction or of l-ascorbic acid. The effect of EGTA was eliminated by an excess of Ca 2+ and the effect of EDTA by an excess of Ni 2+. Excesses of Ca 2+, Mn 2+ and Co 2+ did not influence the effect of EDTA. It is supposed that a reoxidizable heavy metal bound to the membrane structures is responsible for the inhibitory effect of the soluble fraction and of l-ascorbic acid. Catecholamines may act by chelating this metal. The possible role of iron in the phenomenon has been investigated and discussed.
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The soluble fraction could be replaced by l-ascorbic acid in the process, but dehydroascorbic acid or cytoplasmic reducing agents such as l-cysteine and l-glutathione did not show the same effect. Catecholamines could be replaced by chelating agents; EDTA, EGTA, o-phenanthroline and α,α'-dipyridyl prevented the inhibition by the soluble fraction and by l-ascorbic acid. The inhibition of the enzyme activities was not prevented by catecholamines or chelators when they were added after preincubation of the enzyme preparation in the presence of soluble fraction or of l-ascorbic acid. The effect of EGTA was eliminated by an excess of Ca 2+ and the effect of EDTA by an excess of Ni 2+. Excesses of Ca 2+, Mn 2+ and Co 2+ did not influence the effect of EDTA. It is supposed that a reoxidizable heavy metal bound to the membrane structures is responsible for the inhibitory effect of the soluble fraction and of l-ascorbic acid. Catecholamines may act by chelating this metal. 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Seregi, András ; Komlós, Márta</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-1ae44cfc5a61b64a6d064f7c4340783510c946b7657624fb86577c7cd58d6f3d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1974</creationdate><topic>Adenosine Triphosphatases - antagonists &amp; inhibitors</topic><topic>Animals</topic><topic>Ascorbic Acid - pharmacology</topic><topic>Brain - cytology</topic><topic>Catecholamines - pharmacology</topic><topic>Cell Fractionation</topic><topic>Chelating Agents - pharmacology</topic><topic>Deoxycholic Acid - pharmacology</topic><topic>Edetic Acid - pharmacology</topic><topic>Female</topic><topic>Histidine - pharmacology</topic><topic>In Vitro Techniques</topic><topic>Iron - analysis</topic><topic>Magnesium</topic><topic>Male</topic><topic>Microsomes - enzymology</topic><topic>Phenylhydrazines</topic><topic>Phosphoric Monoester Hydrolases - analysis</topic><topic>Potassium</topic><topic>Rats</topic><topic>Rats, Inbred Strains</topic><topic>Sodium</topic><topic>Solubility</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>Tissue Extracts - antagonists &amp; inhibitors</topic><topic>Tissue Extracts - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schaefer, András</creatorcontrib><creatorcontrib>Seregi, András</creatorcontrib><creatorcontrib>Komlós, Márta</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical pharmacology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schaefer, András</au><au>Seregi, András</au><au>Komlós, Márta</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ascorbic acid-like effect of the soluble fraction of rat brain on adenosine triphosphatases and its relation to catecholamines and chelating agents</atitle><jtitle>Biochemical pharmacology</jtitle><addtitle>Biochem Pharmacol</addtitle><date>1974-08-15</date><risdate>1974</risdate><volume>23</volume><issue>16</issue><spage>2257</spage><epage>2271</epage><pages>2257-2271</pages><issn>0006-2952</issn><eissn>1873-2968</eissn><abstract>The inhibitory effect of the soluble fraction of rat brain on the Na +, K +-ATPase, Mg 2+-ATPase and K +- p-nitrophenylphosphatase activities of rat brain subcellular particles and its antagonization by catecholamines have been studied. The soluble fraction could be replaced by l-ascorbic acid in the process, but dehydroascorbic acid or cytoplasmic reducing agents such as l-cysteine and l-glutathione did not show the same effect. Catecholamines could be replaced by chelating agents; EDTA, EGTA, o-phenanthroline and α,α'-dipyridyl prevented the inhibition by the soluble fraction and by l-ascorbic acid. The inhibition of the enzyme activities was not prevented by catecholamines or chelators when they were added after preincubation of the enzyme preparation in the presence of soluble fraction or of l-ascorbic acid. The effect of EGTA was eliminated by an excess of Ca 2+ and the effect of EDTA by an excess of Ni 2+. Excesses of Ca 2+, Mn 2+ and Co 2+ did not influence the effect of EDTA. It is supposed that a reoxidizable heavy metal bound to the membrane structures is responsible for the inhibitory effect of the soluble fraction and of l-ascorbic acid. Catecholamines may act by chelating this metal. The possible role of iron in the phenomenon has been investigated and discussed.</abstract><cop>England</cop><pub>Elsevier Inc</pub><pmid>4368431</pmid><doi>10.1016/0006-2952(74)90555-3</doi><tpages>15</tpages></addata></record>
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subjects Adenosine Triphosphatases - antagonists & inhibitors
Animals
Ascorbic Acid - pharmacology
Brain - cytology
Catecholamines - pharmacology
Cell Fractionation
Chelating Agents - pharmacology
Deoxycholic Acid - pharmacology
Edetic Acid - pharmacology
Female
Histidine - pharmacology
In Vitro Techniques
Iron - analysis
Magnesium
Male
Microsomes - enzymology
Phenylhydrazines
Phosphoric Monoester Hydrolases - analysis
Potassium
Rats
Rats, Inbred Strains
Sodium
Solubility
Spectrophotometry, Ultraviolet
Tissue Extracts - antagonists & inhibitors
Tissue Extracts - pharmacology
title Ascorbic acid-like effect of the soluble fraction of rat brain on adenosine triphosphatases and its relation to catecholamines and chelating agents
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