Acetylcholine-induced Phosphorylation in Isolated Outer Hair Cells.
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| Title: | Acetylcholine-induced Phosphorylation in Isolated Outer Hair Cells. |
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| Authors: | Szõnyi, Magdolna, Csermely, Péter, Sziklai, István |
| Source: | Acta Oto-Laryngologica. 4/22/99, Vol. 119 Issue 2, p185-188. 4p. |
| Subjects: | Hair cells, Acetylcholine |
| Abstract: | Two groups of isolated, surviving outer hair cells (OHCs) of guinea pig cochleas (n=20, for each group) were treated with 10 μM acetylcholine or acetylcholine plus strichnine (an α9 nAChR antagonist), respectively, under short-term tissue culture conditions. The protein content of the cell homogenates was separated by SDS-polyacrylamide gel electrophoresis, Western blotted and labelled with an antibody against phosphoserine residues. Signals were detected using the ECL system. Acetylcholine challenge of the OHCs resulted in a difference in the pattern of phosphorylated proteins from those of strichnine pretreated cells. A 220 kDa and a 120 kDa protein expressed a more intense phosphorylated state in the ACh group compared with the ACh plus strichnine group. The 220 kDa phosphoprotein is in the range of the cytoskeletal protein β-fodrin, whereas the 120 kDa fraction is similar to α-fodrin or an ankyrin isoform. Phosphorylation of proteins due to activation of the AChR by agonist can play a role in the signalling mechanism between receptor activation and increase in the electromotile capability of isolated OHCs. [ABSTRACT FROM AUTHOR] |
| Copyright of Acta Oto-Laryngologica is the property of Taylor & Francis Ltd and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Psychology and Behavioral Sciences Collection |
| FullText | Links: – Type: pdflink Text: Availability: 0 |
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| Header | DbId: pbh DbLabel: Psychology and Behavioral Sciences Collection An: 4876049 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Acetylcholine-induced Phosphorylation in Isolated Outer Hair Cells. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Szõnyi%2C+Magdolna%22">Szõnyi, Magdolna</searchLink><br /><searchLink fieldCode="AR" term="%22Csermely%2C+Péter%22">Csermely, Péter</searchLink><br /><searchLink fieldCode="AR" term="%22Sziklai%2C+István%22">Sziklai, István</searchLink> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Acta+Oto-Laryngologica%22">Acta Oto-Laryngologica</searchLink>. 4/22/99, Vol. 119 Issue 2, p185-188. 4p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Hair+cells%22">Hair cells</searchLink><br /><searchLink fieldCode="DE" term="%22Acetylcholine%22">Acetylcholine</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Two groups of isolated, surviving outer hair cells (OHCs) of guinea pig cochleas (n=20, for each group) were treated with 10 μM acetylcholine or acetylcholine plus strichnine (an α9 nAChR antagonist), respectively, under short-term tissue culture conditions. The protein content of the cell homogenates was separated by SDS-polyacrylamide gel electrophoresis, Western blotted and labelled with an antibody against phosphoserine residues. Signals were detected using the ECL system. Acetylcholine challenge of the OHCs resulted in a difference in the pattern of phosphorylated proteins from those of strichnine pretreated cells. A 220 kDa and a 120 kDa protein expressed a more intense phosphorylated state in the ACh group compared with the ACh plus strichnine group. The 220 kDa phosphoprotein is in the range of the cytoskeletal protein β-fodrin, whereas the 120 kDa fraction is similar to α-fodrin or an ankyrin isoform. Phosphorylation of proteins due to activation of the AChR by agonist can play a role in the signalling mechanism between receptor activation and increase in the electromotile capability of isolated OHCs. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Acta Oto-Laryngologica is the property of Taylor & Francis Ltd and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1080/00016489950181639 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 4 StartPage: 185 Subjects: – SubjectFull: Hair cells Type: general – SubjectFull: Acetylcholine Type: general Titles: – TitleFull: Acetylcholine-induced Phosphorylation in Isolated Outer Hair Cells. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Szõnyi, Magdolna – PersonEntity: Name: NameFull: Csermely, Péter – PersonEntity: Name: NameFull: Sziklai, István IsPartOfRelationships: – BibEntity: Dates: – D: 22 M: 04 Text: 4/22/99 Type: published Y: 1999 Identifiers: – Type: issn-print Value: 00016489 Numbering: – Type: volume Value: 119 – Type: issue Value: 2 Titles: – TitleFull: Acta Oto-Laryngologica Type: main |
| ResultId | 1 |
