Gap‐junction disassembly and connexin 43 dephosphorylation induced by 18β‐glycyrrhetinic acid
Identifieur interne : 002A42 ( Main/Exploration ); précédent : 002A41; suivant : 002A43Gap‐junction disassembly and connexin 43 dephosphorylation induced by 18β‐glycyrrhetinic acid
Auteurs : Xiaojun Guan [États-Unis] ; Susan Wilson [États-Unis] ; Keith K. Schlender [États-Unis] ; Randall J. Ruch [États-Unis]Source :
- Molecular Carcinogenesis [ 0899-1987 ] ; 1996-07.
Abstract
Gap‐junction channels connect the interiors of adjacent cells and can be arranged into aggregates or plaques consisting of hundreds to thousands of channel particles. The mechanism of channel aggregation into plaques and whether plaques can disaggregate are not known. Many carcinogenic and tumor‐promoting chemicals have been identified that inhibit cell‐cell gap‐junctional coupling. Here, we provide morphological evidence that 18β‐glycyrrhetinic acid (18β‐GA), a saponin isolated from licorice root that is an inhibitor of gap‐junctional communication, caused the disassembly of gap‐junction plaques in WB‐F344 rat liver epithelial cells. This effect was dose (5–40 μM) and time dependent (1–4 h treatment). Gap‐junction channels in WB‐F344 cells are comprised of connexin 43 (Cx43), and the protein is phosphorylated to a species known as Cx43‐P2 coincident with the assembly of channels into plaques. Consistent with this, the disassembly of plaques induced by 18β‐GA was correlated with decreases in Cx43‐P2 levels and increases in nonphosphorylated Cx43. Biochemical evidence indicated that these changes in the P2 and NP forms of Cx43 represented 18β‐GA‐induced dephosphorylation of Cx43‐P2 and not its degradation or the inhibition of Cx43‐NP phosphorylation. Okadaic acid and calyculin A, which are inhibitors of type 1 and type 2A protein phosphatases, prevented the dephosphorylation of Cx43, suggesting that one or both of these phosphatases were involved in Cx43 dephosphorylation. These data indicate that 18β‐GA causes type 1 or type 2A protein phosphatase‐mediated Cx43 dephosphorylation coincident with the disassembly of gap‐junction plaques. © 1996 Wiley‐Liss, Inc.
Url:
DOI: 10.1002/(SICI)1098-2744(199607)16:3<157::AID-MC6>3.0.CO;2-E
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream Istex, to step Corpus: 002395
- to stream Istex, to step Curation: 002395
- to stream Istex, to step Checkpoint: 001832
- to stream Main, to step Merge: 002A94
- to stream Main, to step Curation: 002A42
Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Gap‐junction disassembly and connexin 43 dephosphorylation induced by 18β‐glycyrrhetinic acid</title><author><name sortKey="Guan, Xiaojun" sort="Guan, Xiaojun" uniqKey="Guan X" first="Xiaojun" last="Guan">Xiaojun Guan</name></author><author><name sortKey="Wilson, Susan" sort="Wilson, Susan" uniqKey="Wilson S" first="Susan" last="Wilson">Susan Wilson</name></author><author><name sortKey="Schlender, Keith K" sort="Schlender, Keith K" uniqKey="Schlender K" first="Keith K." last="Schlender">Keith K. Schlender</name></author><author><name sortKey="Ruch, Randall J" sort="Ruch, Randall J" uniqKey="Ruch R" first="Randall J." last="Ruch">Randall J. Ruch</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:1421EB4DDF8D1DC94D951C3E07E3B786C265CE8D</idno><date when="1996" year="1996">1996</date><idno type="doi">10.1002/(SICI)1098-2744(199607)16:3<157::AID-MC6>3.0.CO;2-E</idno><idno type="url">https://api.istex.fr/ark:/67375/WNG-TCRKWC03-C/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">002395</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">002395</idno><idno type="wicri:Area/Istex/Curation">002395</idno><idno type="wicri:Area/Istex/Checkpoint">001832</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">001832</idno><idno type="wicri:doubleKey">0899-1987:1996:Guan X:gap:junction:disassembly</idno><idno type="wicri:Area/Main/Merge">002A94</idno><idno type="wicri:Area/Main/Curation">002A42</idno><idno type="wicri:Area/Main/Exploration">002A42</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main">Gap‐junction disassembly and connexin 43 dephosphorylation induced by 18β‐glycyrrhetinic acid</title><author><name sortKey="Guan, Xiaojun" sort="Guan, Xiaojun" uniqKey="Guan X" first="Xiaojun" last="Guan">Xiaojun Guan</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Ohio</region></placeName><wicri:cityArea>Departments of Pathology and Pharmacology, Medical College of Ohio, Toledo</wicri:cityArea></affiliation></author><author><name sortKey="Wilson, Susan" sort="Wilson, Susan" uniqKey="Wilson S" first="Susan" last="Wilson">Susan Wilson</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Ohio</region></placeName><wicri:cityArea>Departments of Pathology and Pharmacology, Medical College of Ohio, Toledo</wicri:cityArea></affiliation></author><author><name sortKey="Schlender, Keith K" sort="Schlender, Keith K" uniqKey="Schlender K" first="Keith K." last="Schlender">Keith K. Schlender</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Ohio</region></placeName><wicri:cityArea>Departments of Pathology and Pharmacology, Medical College of Ohio, Toledo</wicri:cityArea></affiliation></author><author><name sortKey="Ruch, Randall J" sort="Ruch, Randall J" uniqKey="Ruch R" first="Randall J." last="Ruch">Randall J. Ruch</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Ohio</region></placeName><wicri:cityArea>Departments of Pathology and Pharmacology, Medical College of Ohio, Toledo</wicri:cityArea></affiliation><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Ohio</region></placeName><wicri:cityArea>Correspondence address: Department of Pathology, Medical College of Ohio, 3000 Arlington Avenue, Toledo</wicri:cityArea></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Molecular Carcinogenesis</title><title level="j" type="alt">MOLECULAR CARCINOGENESIS</title><idno type="ISSN">0899-1987</idno><idno type="eISSN">1098-2744</idno><imprint><biblScope unit="vol">16</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="157">157</biblScope><biblScope unit="page" to="164">164</biblScope><biblScope unit="page-count">8</biblScope><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>New York</pubPlace><date type="published" when="1996-07">1996-07</date></imprint><idno type="ISSN">0899-1987</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0899-1987</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Gap‐junction channels connect the interiors of adjacent cells and can be arranged into aggregates or plaques consisting of hundreds to thousands of channel particles. The mechanism of channel aggregation into plaques and whether plaques can disaggregate are not known. Many carcinogenic and tumor‐promoting chemicals have been identified that inhibit cell‐cell gap‐junctional coupling. Here, we provide morphological evidence that 18β‐glycyrrhetinic acid (18β‐GA), a saponin isolated from licorice root that is an inhibitor of gap‐junctional communication, caused the disassembly of gap‐junction plaques in WB‐F344 rat liver epithelial cells. This effect was dose (5–40 μM) and time dependent (1–4 h treatment). Gap‐junction channels in WB‐F344 cells are comprised of connexin 43 (Cx43), and the protein is phosphorylated to a species known as Cx43‐P2 coincident with the assembly of channels into plaques. Consistent with this, the disassembly of plaques induced by 18β‐GA was correlated with decreases in Cx43‐P2 levels and increases in nonphosphorylated Cx43. Biochemical evidence indicated that these changes in the P2 and NP forms of Cx43 represented 18β‐GA‐induced dephosphorylation of Cx43‐P2 and not its degradation or the inhibition of Cx43‐NP phosphorylation. Okadaic acid and calyculin A, which are inhibitors of type 1 and type 2A protein phosphatases, prevented the dephosphorylation of Cx43, suggesting that one or both of these phosphatases were involved in Cx43 dephosphorylation. These data indicate that 18β‐GA causes type 1 or type 2A protein phosphatase‐mediated Cx43 dephosphorylation coincident with the disassembly of gap‐junction plaques. © 1996 Wiley‐Liss, Inc.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Ohio</li></region></list><tree><country name="États-Unis"><region name="Ohio"><name sortKey="Guan, Xiaojun" sort="Guan, Xiaojun" uniqKey="Guan X" first="Xiaojun" last="Guan">Xiaojun Guan</name></region><name sortKey="Ruch, Randall J" sort="Ruch, Randall J" uniqKey="Ruch R" first="Randall J." last="Ruch">Randall J. Ruch</name><name sortKey="Ruch, Randall J" sort="Ruch, Randall J" uniqKey="Ruch R" first="Randall J." last="Ruch">Randall J. Ruch</name><name sortKey="Schlender, Keith K" sort="Schlender, Keith K" uniqKey="Schlender K" first="Keith K." last="Schlender">Keith K. Schlender</name><name sortKey="Wilson, Susan" sort="Wilson, Susan" uniqKey="Wilson S" first="Susan" last="Wilson">Susan Wilson</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/ChloroquineV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002A42 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 002A42 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= ChloroquineV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= ISTEX:1421EB4DDF8D1DC94D951C3E07E3B786C265CE8D
|texte= Gap‐junction disassembly and connexin 43 dephosphorylation induced by 18β‐glycyrrhetinic acid
}}
| This area was generated with Dilib version V0.6.33. |  |