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...
Gespeichert in:
Veröffentlicht in: | Biochemical pharmacology 1974-08, Vol.23 (16), p.2257-2271 |
---|---|
Hauptverfasser: | , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 2271 |
---|---|
container_issue | 16 |
container_start_page | 2257 |
container_title | Biochemical pharmacology |
container_volume | 23 |
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. |
doi_str_mv | 10.1016/0006-2952(74)90555-3 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_82485277</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0006295274905553</els_id><sourcerecordid>82485277</sourcerecordid><originalsourceid>FETCH-LOGICAL-c357t-1ae44cfc5a61b64a6d064f7c4340783510c946b7657624fb86577c7cd58d6f3d3</originalsourceid><addsrcrecordid>eNp9UctuFDEQtBAobAJ_AJJPiBwG7PFr9oIURbykSFzgbHna7YxhdrzY3kh8Bz-MZ3eVI6d-VFVbriLkFWfvOOP6PWNMd_1W9W-NvN4ypVQnnpANH4xoaz08JZtHynNyWcrPdRw0vyAXUuhBCr4hf28KpDxGoA6i7-b4CymGgFBpCrROSEuaD-OMNGQHNaZl3WdX6ZhdbMNCnccllbggrTnup1T2k6uuYKFu8TTWQjPO7iitiYKrCFOa3a4pThSYjvhyT909LrW8IM-Cmwu-PNcr8uPTx--3X7q7b5-_3t7cdSCUqR13KCUEUE7zUUunPdMyGJBCMjMIxRlspR6NVkb3MoxDawwY8GrwOggvrsib0919Tr8PWKrdxQI4z27BdCh26OWgemMaUZ6IkFMpGYPd57hz-Y_lzK5Z2NVZuxptjbTHLKxostfn-4dxh_5RdDa_4R9OOLZPPkTMtkDEBdDH3AKwPsX_P_APq0Kavw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>82485277</pqid></control><display><type>article</type><title>Ascorbic acid-like effect of the soluble fraction of rat brain on adenosine triphosphatases and its relation to catecholamines and chelating agents</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Schaefer, András ; Seregi, András ; Komlós, Márta</creator><creatorcontrib>Schaefer, András ; Seregi, András ; Komlós, Márta</creatorcontrib><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.</description><identifier>ISSN: 0006-2952</identifier><identifier>EISSN: 1873-2968</identifier><identifier>DOI: 10.1016/0006-2952(74)90555-3</identifier><identifier>PMID: 4368431</identifier><language>eng</language><publisher>England: Elsevier Inc</publisher><subject>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</subject><ispartof>Biochemical pharmacology, 1974-08, Vol.23 (16), p.2257-2271</ispartof><rights>1974</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-1ae44cfc5a61b64a6d064f7c4340783510c946b7657624fb86577c7cd58d6f3d3</citedby><cites>FETCH-LOGICAL-c357t-1ae44cfc5a61b64a6d064f7c4340783510c946b7657624fb86577c7cd58d6f3d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0006295274905553$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4368431$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schaefer, András</creatorcontrib><creatorcontrib>Seregi, András</creatorcontrib><creatorcontrib>Komlós, Márta</creatorcontrib><title>Ascorbic acid-like effect of the soluble fraction of rat brain on adenosine triphosphatases and its relation to catecholamines and chelating agents</title><title>Biochemical pharmacology</title><addtitle>Biochem Pharmacol</addtitle><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.</description><subject>Adenosine Triphosphatases - antagonists & inhibitors</subject><subject>Animals</subject><subject>Ascorbic Acid - pharmacology</subject><subject>Brain - cytology</subject><subject>Catecholamines - pharmacology</subject><subject>Cell Fractionation</subject><subject>Chelating Agents - pharmacology</subject><subject>Deoxycholic Acid - pharmacology</subject><subject>Edetic Acid - pharmacology</subject><subject>Female</subject><subject>Histidine - pharmacology</subject><subject>In Vitro Techniques</subject><subject>Iron - analysis</subject><subject>Magnesium</subject><subject>Male</subject><subject>Microsomes - enzymology</subject><subject>Phenylhydrazines</subject><subject>Phosphoric Monoester Hydrolases - analysis</subject><subject>Potassium</subject><subject>Rats</subject><subject>Rats, Inbred Strains</subject><subject>Sodium</subject><subject>Solubility</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>Tissue Extracts - antagonists & inhibitors</subject><subject>Tissue Extracts - pharmacology</subject><issn>0006-2952</issn><issn>1873-2968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1974</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9UctuFDEQtBAobAJ_AJJPiBwG7PFr9oIURbykSFzgbHna7YxhdrzY3kh8Bz-MZ3eVI6d-VFVbriLkFWfvOOP6PWNMd_1W9W-NvN4ypVQnnpANH4xoaz08JZtHynNyWcrPdRw0vyAXUuhBCr4hf28KpDxGoA6i7-b4CymGgFBpCrROSEuaD-OMNGQHNaZl3WdX6ZhdbMNCnccllbggrTnup1T2k6uuYKFu8TTWQjPO7iitiYKrCFOa3a4pThSYjvhyT909LrW8IM-Cmwu-PNcr8uPTx--3X7q7b5-_3t7cdSCUqR13KCUEUE7zUUunPdMyGJBCMjMIxRlspR6NVkb3MoxDawwY8GrwOggvrsib0919Tr8PWKrdxQI4z27BdCh26OWgemMaUZ6IkFMpGYPd57hz-Y_lzK5Z2NVZuxptjbTHLKxostfn-4dxh_5RdDa_4R9OOLZPPkTMtkDEBdDH3AKwPsX_P_APq0Kavw</recordid><startdate>19740815</startdate><enddate>19740815</enddate><creator>Schaefer, András</creator><creator>Seregi, András</creator><creator>Komlós, Márta</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19740815</creationdate><title>Ascorbic acid-like effect of the soluble fraction of rat brain on adenosine triphosphatases and its relation to catecholamines and chelating agents</title><author>Schaefer, András ; 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 & 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 & 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> |
fulltext | fulltext |
identifier | ISSN: 0006-2952 |
ispartof | Biochemical pharmacology, 1974-08, Vol.23 (16), p.2257-2271 |
issn | 0006-2952 1873-2968 |
language | eng |
recordid | cdi_proquest_miscellaneous_82485277 |
source | MEDLINE; Elsevier ScienceDirect Journals |
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 |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-11T08%3A49%3A27IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Ascorbic%20acid-like%20effect%20of%20the%20soluble%20fraction%20of%20rat%20brain%20on%20adenosine%20triphosphatases%20and%20its%20relation%20to%20catecholamines%20and%20chelating%20agents&rft.jtitle=Biochemical%20pharmacology&rft.au=Schaefer,%20Andr%C3%A1s&rft.date=1974-08-15&rft.volume=23&rft.issue=16&rft.spage=2257&rft.epage=2271&rft.pages=2257-2271&rft.issn=0006-2952&rft.eissn=1873-2968&rft_id=info:doi/10.1016/0006-2952(74)90555-3&rft_dat=%3Cproquest_cross%3E82485277%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=82485277&rft_id=info:pmid/4368431&rft_els_id=0006295274905553&rfr_iscdi=true |