Modulation of plasma membrane Ca2-ATPase by neutral Phospholipids: effect of the micelle-vesicle transition and the bilayer thickness
Background: Membrane proteins require phospholipids to be biologically active. Results: An increase of phosphatidylcholine/detergent molar ratio leads to a biphasic behavior of the PMCA Ca2-ATPase activity, whose maximum depends on phosphatidylcholine characteristics. Conclusion: The optimum hydroph...
| Autores: | , , , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2015 |
| País: | Argentina |
| Institución: | Consejo Nacional de Investigaciones Científicas y Técnicas |
| Repositorio: | CONICET Digital (CONICET) |
| Idioma: | inglés |
| OAI Identifier: | oai:ri.conicet.gov.ar:11336/21341 |
| Acceso en línea: | http://hdl.handle.net/11336/21341 |
| Access Level: | acceso abierto |
| Palabra clave: | CALCIUM ATPASE ENZYME TURNOVER LIPID BILAYER MOLECULAR DYNAMICS https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
| Sumario: | Background: Membrane proteins require phospholipids to be biologically active. Results: An increase of phosphatidylcholine/detergent molar ratio leads to a biphasic behavior of the PMCA Ca2-ATPase activity, whose maximum depends on phosphatidylcholine characteristics. Conclusion: The optimum hydrophobic thickness for PMCA structure and Ca2-ATPase activity is about 24 Å. Significance: Differential modulation by neutral phospholipids could be a general mechanism for regulating membrane protein function. |
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