Protein kinase D1 modulates aldosterone-induced ENaC activity in a renal cortical collecting duct cell line.

Hdl Handle:
http://hdl.handle.net/10147/126548
Title:
Protein kinase D1 modulates aldosterone-induced ENaC activity in a renal cortical collecting duct cell line.
Authors:
McEneaney, Victoria; Dooley, Ruth; Yusef, Yamil R; Keating, Niamh; Quinn, Ursula; Harvey, Brian J; Thomas, Warren
Affiliation:
Department of Molecular Medicine, Royal College of Surgeons in Ireland, Education and Research Centre, Smurfit Building, Beaumont Hospital, Dublin 9, Ireland.
Citation:
Protein kinase D1 modulates aldosterone-induced ENaC activity in a renal cortical collecting duct cell line. 2010, 325 (1-2):8-17 Mol. Cell. Endocrinol.
Journal:
Molecular and cellular endocrinology
Issue Date:
30-Aug-2010
URI:
http://hdl.handle.net/10147/126548
DOI:
10.1016/j.mce.2010.04.019
PubMed ID:
20434520
Abstract:
Aldosterone treatment of M1-CCD cells stimulated an increase in epithelial Na(+) channel (ENaC) alpha-subunit expression that was mainly localized to the apical membrane. PKD1-suppressed cells constitutively expressed ENaCalpha at low abundance, with no increase after aldosterone treatment. In the PKD1-suppressed cells, ENaCalpha was mainly localized proximal to the basolateral surface of the epithelium both before and after aldosterone treatment. Apical membrane insertion of ENaCbeta in response to aldosterone treatment was also sensitive to PKD1 suppression as was the aldosterone-induced rise in the amiloride-sensitive, trans-epithelial current (I(TE)). The interaction of the mineralocorticoid receptor (MR) with specific elements in the promoters of aldosterone responsive genes is stabilized by ligand interaction and phosphorylation. PKD1 suppression inhibited aldosterone-induced SGK-1 expression. The nuclear localization of MR was also blocked by PKD1 suppression and MEK antagonism implicating both these kinases in MR nuclear stabilization. PKD1 thus modulates aldosterone-induced ENaC activity through the modulation of sub-cellular trafficking and the stabilization of MR nuclear localization.
Item Type:
Article
Language:
en
MeSH:
Aldosterone; Amiloride; Animals; Cell Line; Epithelial Sodium Channel; Gene Expression; Kidney Cortex; Kidney Tubules, Collecting; Mice; Mice, Transgenic; Protein Kinase C; Protein Transport; RNA, Small Interfering; Receptors, Mineralocorticoid
ISSN:
1872-8057

Full metadata record

DC FieldValue Language
dc.contributor.authorMcEneaney, Victoriaen
dc.contributor.authorDooley, Ruthen
dc.contributor.authorYusef, Yamil Ren
dc.contributor.authorKeating, Niamhen
dc.contributor.authorQuinn, Ursulaen
dc.contributor.authorHarvey, Brian Jen
dc.contributor.authorThomas, Warrenen
dc.date.accessioned2011-03-31T12:53:00Z-
dc.date.available2011-03-31T12:53:00Z-
dc.date.issued2010-08-30-
dc.identifier.citationProtein kinase D1 modulates aldosterone-induced ENaC activity in a renal cortical collecting duct cell line. 2010, 325 (1-2):8-17 Mol. Cell. Endocrinol.en
dc.identifier.issn1872-8057-
dc.identifier.pmid20434520-
dc.identifier.doi10.1016/j.mce.2010.04.019-
dc.identifier.urihttp://hdl.handle.net/10147/126548-
dc.description.abstractAldosterone treatment of M1-CCD cells stimulated an increase in epithelial Na(+) channel (ENaC) alpha-subunit expression that was mainly localized to the apical membrane. PKD1-suppressed cells constitutively expressed ENaCalpha at low abundance, with no increase after aldosterone treatment. In the PKD1-suppressed cells, ENaCalpha was mainly localized proximal to the basolateral surface of the epithelium both before and after aldosterone treatment. Apical membrane insertion of ENaCbeta in response to aldosterone treatment was also sensitive to PKD1 suppression as was the aldosterone-induced rise in the amiloride-sensitive, trans-epithelial current (I(TE)). The interaction of the mineralocorticoid receptor (MR) with specific elements in the promoters of aldosterone responsive genes is stabilized by ligand interaction and phosphorylation. PKD1 suppression inhibited aldosterone-induced SGK-1 expression. The nuclear localization of MR was also blocked by PKD1 suppression and MEK antagonism implicating both these kinases in MR nuclear stabilization. PKD1 thus modulates aldosterone-induced ENaC activity through the modulation of sub-cellular trafficking and the stabilization of MR nuclear localization.-
dc.language.isoenen
dc.subject.meshAldosterone-
dc.subject.meshAmiloride-
dc.subject.meshAnimals-
dc.subject.meshCell Line-
dc.subject.meshEpithelial Sodium Channel-
dc.subject.meshGene Expression-
dc.subject.meshKidney Cortex-
dc.subject.meshKidney Tubules, Collecting-
dc.subject.meshMice-
dc.subject.meshMice, Transgenic-
dc.subject.meshProtein Kinase C-
dc.subject.meshProtein Transport-
dc.subject.meshRNA, Small Interfering-
dc.subject.meshReceptors, Mineralocorticoid-
dc.titleProtein kinase D1 modulates aldosterone-induced ENaC activity in a renal cortical collecting duct cell line.en
dc.typeArticleen
dc.contributor.departmentDepartment of Molecular Medicine, Royal College of Surgeons in Ireland, Education and Research Centre, Smurfit Building, Beaumont Hospital, Dublin 9, Ireland.en
dc.identifier.journalMolecular and cellular endocrinologyen
dc.description.provinceLeinster-

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