Ouabain Modulates the Adherens Junction in Renal Epithelial Cells.


Journal

Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology
ISSN: 1421-9778
Titre abrégé: Cell Physiol Biochem
Pays: Germany
ID NLM: 9113221

Informations de publication

Date de publication:
2019
Historique:
received: 16 10 2017
accepted: 06 05 2019
entrez: 11 5 2019
pubmed: 11 5 2019
medline: 22 5 2019
Statut: ppublish

Résumé

Ouabain, a well-known plant-derived toxin, is also a hormone found in mammals at nanomolar levels that binds to a site located in the a-subunit of Na⁺,K⁺-ATPase. Our main goal was to understand the physiological roles of ouabain. Previously, we found that ouabain increases the degree of tight junction sealing, GAP junction-mediated communication and ciliogenesis. Considering our previous results, we investigated the effect of ouabain on adherens junctions. We used immunofluorescence and immunoblot methods to measure the effect of 10 nM ouabain on the cellular and nuclear content of E-cadherin, β-catenin and γ-catenin in cultured monolayers of Marin Darby canine renal cells (MDCK). We also studied the effect of ouabain on adherens junction biogenesis through sequential Ca²⁺ removal and replenishment. Then, we investigated whether c-Src and ERK1/2 kinases are involved in these responses. Ouabain enhanced the cellular content of the adherens junction proteins E-cadherin, β-catenin and γ-catenin and displaced β-catenin and γ-catenin from the plasma membrane into the nucleus. Ouabain also increased the expression levels of E-cadherin and β-catenin in the plasma membrane after Ca²⁺ replenishment. These effects on adherens junctions were sensitive to PP2 and PD98059, suggesting that they depend on c-Src and ERK1/2 signaling. The translocation of β-catenin and γ-catenin into the nucleus was specific because ouabain did not change the localization of the tight junction proteins ZO-1 and ZO-2. Moreover, in ouabain-resistant MDCK cells, which express a Na⁺,K⁺-ATPase α1-subunit with low affinity for ouabain, this hormone was unable to regulate adherens junctions, indicating that the ouabain receptor that regulates adherens junctions is Na⁺,K⁺-ATPase. Ouabain (10 nM) upregulated adherens junctions. This novel result supports the proposition that one of the physiological roles of this hormone is the modulation of cell contacts.

Sections du résumé

BACKGROUND/AIMS OBJECTIVE
Ouabain, a well-known plant-derived toxin, is also a hormone found in mammals at nanomolar levels that binds to a site located in the a-subunit of Na⁺,K⁺-ATPase. Our main goal was to understand the physiological roles of ouabain. Previously, we found that ouabain increases the degree of tight junction sealing, GAP junction-mediated communication and ciliogenesis. Considering our previous results, we investigated the effect of ouabain on adherens junctions.
METHODS METHODS
We used immunofluorescence and immunoblot methods to measure the effect of 10 nM ouabain on the cellular and nuclear content of E-cadherin, β-catenin and γ-catenin in cultured monolayers of Marin Darby canine renal cells (MDCK). We also studied the effect of ouabain on adherens junction biogenesis through sequential Ca²⁺ removal and replenishment. Then, we investigated whether c-Src and ERK1/2 kinases are involved in these responses.
RESULTS RESULTS
Ouabain enhanced the cellular content of the adherens junction proteins E-cadherin, β-catenin and γ-catenin and displaced β-catenin and γ-catenin from the plasma membrane into the nucleus. Ouabain also increased the expression levels of E-cadherin and β-catenin in the plasma membrane after Ca²⁺ replenishment. These effects on adherens junctions were sensitive to PP2 and PD98059, suggesting that they depend on c-Src and ERK1/2 signaling. The translocation of β-catenin and γ-catenin into the nucleus was specific because ouabain did not change the localization of the tight junction proteins ZO-1 and ZO-2. Moreover, in ouabain-resistant MDCK cells, which express a Na⁺,K⁺-ATPase α1-subunit with low affinity for ouabain, this hormone was unable to regulate adherens junctions, indicating that the ouabain receptor that regulates adherens junctions is Na⁺,K⁺-ATPase.
CONCLUSION CONCLUSIONS
Ouabain (10 nM) upregulated adherens junctions. This novel result supports the proposition that one of the physiological roles of this hormone is the modulation of cell contacts.

Identifiants

pubmed: 31075189
doi: 10.33594/000000097
doi:

Substances chimiques

Cadherins 0
beta Catenin 0
gamma Catenin 0
Ouabain 5ACL011P69
CSK Tyrosine-Protein Kinase EC 2.7.10.2
src-Family Kinases EC 2.7.10.2
Mitogen-Activated Protein Kinase 1 EC 2.7.11.24
Mitogen-Activated Protein Kinase 3 EC 2.7.11.24
Sodium-Potassium-Exchanging ATPase EC 7.2.2.13
Calcium SY7Q814VUP

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

1381-1397

Subventions

Organisme : Conacyt
ID : P285263
Pays : Mexico
Organisme : Conacyt
ID : P221513
Pays : Mexico
Organisme : SEP-Cinvestav
ID : Fondo de Investigación Científica y Desarrollo Tecnológico del Cinvestav, 143
Pays : Mexico

Informations de copyright

© Copyright by the Author(s). Published by Cell Physiol Biochem Press.

Déclaration de conflit d'intérêts

The authors declare they have no conflicts of interest.

Auteurs

Aida Castillo (A)

Department of Physiology, Biophysics and Neurosciences, Cinvestav, Mexico City, Mexico.

Carlos Ortuño-Pineda (C)

Laboratory of Nucleic Acids and Proteins, Faculty of Chemical and Biological Sciences, Autonomous University of Guerrero, Chilpancingo, Mexico.

Catalina Flores-Maldonado (C)

Department of Physiology, Biophysics and Neurosciences, Cinvestav, Mexico City, Mexico.

Isabel Larre (I)

Marshall Institute for Interdisciplinary Research and Department of Clinical and Translational Sciences, Joan C. Edwards School of Medicine, Marshall University, Huntington, WV, USA.

Jacqueline Martínez Rendón (J)

Department of Physiology, Biophysics and Neurosciences, Cinvestav, Mexico City, Mexico.

Lorena Hinojosa (L)

Department of Physiology, Biophysics and Neurosciences, Cinvestav, Mexico City, Mexico.

Arturo Ponce (A)

Department of Physiology, Biophysics and Neurosciences, Cinvestav, Mexico City, Mexico.

Alejandro Ogazón (A)

Department of Physiology, Biophysics and Neurosciences, Cinvestav, Mexico City, Mexico.

Mauricio Serrano (M)

Department of Physiology, Biophysics and Neurosciences, Cinvestav, Mexico City, Mexico.

Jesús Valdes (J)

Department of Biochemistry, Cinvestav, Mexico City, Mexico.

Rubén G Contreras (RG)

Department of Physiology, Biophysics and Neurosciences, Cinvestav, Mexico City, Mexico.

Marcelino Cereijido (M)

Department of Physiology, Biophysics and Neurosciences, Cinvestav, Mexico City, Mexico, cereijido@fisio.cinvestav.mx.

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Classifications MeSH