PIP2 and PIP as determinants for ATP inhibition of KATP channels.
Adenosine triphosphate (ATP)-sensitive potassium (KATP) channels couple electrical activity to cellular metabolism through their inhibition by intracellular ATP. ATP inhibition of KATP channels varies among tissues and is affected by the metabolic and regulatory state of individual cells, suggesting...
| Váldodahkkit: | , , , , , , , |
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| Materiálatiipa: | Journal article |
| Giella: | English |
| Almmustuhtton: |
1998
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| _version_ | 1826302924943261696 |
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| author | Baukrowitz, T Schulte, U Oliver, D Herlitze, S Krauter, T Tucker, S Ruppersberg, J Fakler, B |
| author_facet | Baukrowitz, T Schulte, U Oliver, D Herlitze, S Krauter, T Tucker, S Ruppersberg, J Fakler, B |
| author_sort | Baukrowitz, T |
| collection | OXFORD |
| description | Adenosine triphosphate (ATP)-sensitive potassium (KATP) channels couple electrical activity to cellular metabolism through their inhibition by intracellular ATP. ATP inhibition of KATP channels varies among tissues and is affected by the metabolic and regulatory state of individual cells, suggesting involvement of endogenous factors. It is reported here that phosphatidylinositol-4, 5-bisphosphate (PIP2) and phosphatidylinositol-4-phosphate (PIP) controlled ATP inhibition of cloned KATP channels (Kir6.2 and SUR1). These phospholipids acted on the Kir6.2 subunit and shifted ATP sensitivity by several orders of magnitude. Receptor-mediated activation of phospholipase C resulted in inhibition of KATP-mediated currents. These results represent a mechanism for control of excitability through phospholipids. |
| first_indexed | 2024-03-07T05:54:50Z |
| format | Journal article |
| id | oxford-uuid:ea2dd6b6-78c8-4ace-a666-b6bd3e1e568d |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T05:54:50Z |
| publishDate | 1998 |
| record_format | dspace |
| spelling | oxford-uuid:ea2dd6b6-78c8-4ace-a666-b6bd3e1e568d2022-03-27T10:59:46ZPIP2 and PIP as determinants for ATP inhibition of KATP channels.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:ea2dd6b6-78c8-4ace-a666-b6bd3e1e568dEnglishSymplectic Elements at Oxford1998Baukrowitz, TSchulte, UOliver, DHerlitze, SKrauter, TTucker, SRuppersberg, JFakler, BAdenosine triphosphate (ATP)-sensitive potassium (KATP) channels couple electrical activity to cellular metabolism through their inhibition by intracellular ATP. ATP inhibition of KATP channels varies among tissues and is affected by the metabolic and regulatory state of individual cells, suggesting involvement of endogenous factors. It is reported here that phosphatidylinositol-4, 5-bisphosphate (PIP2) and phosphatidylinositol-4-phosphate (PIP) controlled ATP inhibition of cloned KATP channels (Kir6.2 and SUR1). These phospholipids acted on the Kir6.2 subunit and shifted ATP sensitivity by several orders of magnitude. Receptor-mediated activation of phospholipase C resulted in inhibition of KATP-mediated currents. These results represent a mechanism for control of excitability through phospholipids. |
| spellingShingle | Baukrowitz, T Schulte, U Oliver, D Herlitze, S Krauter, T Tucker, S Ruppersberg, J Fakler, B PIP2 and PIP as determinants for ATP inhibition of KATP channels. |
| title | PIP2 and PIP as determinants for ATP inhibition of KATP channels. |
| title_full | PIP2 and PIP as determinants for ATP inhibition of KATP channels. |
| title_fullStr | PIP2 and PIP as determinants for ATP inhibition of KATP channels. |
| title_full_unstemmed | PIP2 and PIP as determinants for ATP inhibition of KATP channels. |
| title_short | PIP2 and PIP as determinants for ATP inhibition of KATP channels. |
| title_sort | pip2 and pip as determinants for atp inhibition of katp channels |
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