Ca extrusion by NCX is compromised in olfactory sensory neurons of OMP mice.

<h4>Background</h4>The role of olfactory marker protein (OMP), a hallmark of mature olfactory sensory neurons (OSNs), has been poorly understood since its discovery. The electrophysiological and behavioral phenotypes of OMP knockout mice indicated that OMP influences olfactory signal tra...

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Autores principales: Hyun J Kwon, Jae Hyung Koo, Frank Zufall, Trese Leinders-Zufall, Frank L Margolis
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Publicado: Public Library of Science (PLoS) 2009
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spelling oai:doaj.org-article:bb986dbefd494058bc15bdb250d62e352021-11-25T06:17:40ZCa extrusion by NCX is compromised in olfactory sensory neurons of OMP mice.1932-620310.1371/journal.pone.0004260https://doaj.org/article/bb986dbefd494058bc15bdb250d62e352009-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19165324/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>The role of olfactory marker protein (OMP), a hallmark of mature olfactory sensory neurons (OSNs), has been poorly understood since its discovery. The electrophysiological and behavioral phenotypes of OMP knockout mice indicated that OMP influences olfactory signal transduction. However, the mechanism by which this occurs remained unknown.<h4>Principal findings</h4>We used intact olfactory epithelium obtained from WT and OMP(-/-) mice to monitor the Ca(2+) dynamics induced by the activation of cyclic nucleotide-gated channels, voltage-operated Ca(2+) channels, or Ca(2+) stores in single dendritic knobs of OSNs. Our data suggested that OMP could act to modulate the Ca(2+)-homeostasis in these neurons by influencing the activity of the plasma membrane Na(+)/Ca(2+)-exchanger (NCX). Immunohistochemistry verifies colocalization of NCX1 and OMP in the cilia and knobs of OSNs. To test the role of NCX activity, we compared the kinetics of Ca(2+) elevation by stimulating the reverse mode of NCX in both WT and OMP(-/-) mice. The resulting Ca(2+) responses indicate that OMP facilitates NCX activity and allows rapid Ca(2+) extrusion from OSN knobs. To address the mechanism by which OMP influences NCX activity in OSNs we studied protein-peptide interactions in real-time using surface plasmon resonance technology. We demonstrate the direct interaction of the XIP regulatory-peptide of NCX with calmodulin (CaM).<h4>Conclusions</h4>Since CaM also binds to the Bex protein, an interacting protein partner of OMP, these observations strongly suggest that OMP can influence CaM efficacy and thus alters NCX activity by a series of protein-protein interactions.Hyun J KwonJae Hyung KooFrank ZufallTrese Leinders-ZufallFrank L MargolisPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 4, Iss 1, p e4260 (2009)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Hyun J Kwon
Jae Hyung Koo
Frank Zufall
Trese Leinders-Zufall
Frank L Margolis
Ca extrusion by NCX is compromised in olfactory sensory neurons of OMP mice.
description <h4>Background</h4>The role of olfactory marker protein (OMP), a hallmark of mature olfactory sensory neurons (OSNs), has been poorly understood since its discovery. The electrophysiological and behavioral phenotypes of OMP knockout mice indicated that OMP influences olfactory signal transduction. However, the mechanism by which this occurs remained unknown.<h4>Principal findings</h4>We used intact olfactory epithelium obtained from WT and OMP(-/-) mice to monitor the Ca(2+) dynamics induced by the activation of cyclic nucleotide-gated channels, voltage-operated Ca(2+) channels, or Ca(2+) stores in single dendritic knobs of OSNs. Our data suggested that OMP could act to modulate the Ca(2+)-homeostasis in these neurons by influencing the activity of the plasma membrane Na(+)/Ca(2+)-exchanger (NCX). Immunohistochemistry verifies colocalization of NCX1 and OMP in the cilia and knobs of OSNs. To test the role of NCX activity, we compared the kinetics of Ca(2+) elevation by stimulating the reverse mode of NCX in both WT and OMP(-/-) mice. The resulting Ca(2+) responses indicate that OMP facilitates NCX activity and allows rapid Ca(2+) extrusion from OSN knobs. To address the mechanism by which OMP influences NCX activity in OSNs we studied protein-peptide interactions in real-time using surface plasmon resonance technology. We demonstrate the direct interaction of the XIP regulatory-peptide of NCX with calmodulin (CaM).<h4>Conclusions</h4>Since CaM also binds to the Bex protein, an interacting protein partner of OMP, these observations strongly suggest that OMP can influence CaM efficacy and thus alters NCX activity by a series of protein-protein interactions.
format article
author Hyun J Kwon
Jae Hyung Koo
Frank Zufall
Trese Leinders-Zufall
Frank L Margolis
author_facet Hyun J Kwon
Jae Hyung Koo
Frank Zufall
Trese Leinders-Zufall
Frank L Margolis
author_sort Hyun J Kwon
title Ca extrusion by NCX is compromised in olfactory sensory neurons of OMP mice.
title_short Ca extrusion by NCX is compromised in olfactory sensory neurons of OMP mice.
title_full Ca extrusion by NCX is compromised in olfactory sensory neurons of OMP mice.
title_fullStr Ca extrusion by NCX is compromised in olfactory sensory neurons of OMP mice.
title_full_unstemmed Ca extrusion by NCX is compromised in olfactory sensory neurons of OMP mice.
title_sort ca extrusion by ncx is compromised in olfactory sensory neurons of omp mice.
publisher Public Library of Science (PLoS)
publishDate 2009
url https://doaj.org/article/bb986dbefd494058bc15bdb250d62e35
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AT jaehyungkoo caextrusionbyncxiscompromisedinolfactorysensoryneuronsofompmice
AT frankzufall caextrusionbyncxiscompromisedinolfactorysensoryneuronsofompmice
AT treseleinderszufall caextrusionbyncxiscompromisedinolfactorysensoryneuronsofompmice
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