tailieunhanh - Báo cáo khoa học: Caveolin-1 influences P2X7 receptor expression and localization in mouse lung alveolar epithelial cells

The P2X7receptor has recently been described as a marker for lung alveo-lar epithelial type I cells. Here, we demonstrate both the expression of P2X7 protein and its partition into lipid rafts in the mouse lung alveolar epithelial cell line E10. | ỊFEBS Journal Caveolin-1 influences P2X7 receptor expression and localization in mouse lung alveolar epithelial cells K. Barth1 z K. Weinhold1 z A. Guenther1 M. T. Young2 H. Schnittler3 and M. Kasper1 1 Institute of Anatomy MedicalFaculty CarlGustav Carus Dresden University of Technology Germany 2 Faculty of Life Sciences University of Manchester UK 3 Institute of Physiology MedicalFaculty CarlGustav Carus Dresden University of Technology Germany Keywords alveolar epithelium Caveolin-1 mouse lung P2X7 receptor Correspondence M. Kasper Institute of Anatomy Medical Faculty Carl Gustav Carus Dresden University of Technology Fiedlerstr. 42 D-01307 Dresden Germany Fax 49 351 458 6303 Tel 49 351 458 6080 E-mail These authors contributed equally to this work Received 3 January 2007 revised 11 April 2007 accepted 16 April 2007 doi The P2X7 receptor has recently been described as a marker for lung alveolar epithelial type I cells. Here we demonstrate both the expression of P2X7 protein and its partition into lipid rafts in the mouse lung alveolar epithelial cell line E10. A significant degree of colocalization was observed between P2X7 and the raft marker protein Caveolin-1 also P2X7 protein was associated with caveolae. A marked reduction in P2X7 immunoreactivity was observed in lung sections prepared from Caveolin-1-knockout mice indicating that Caveolin-1 expression was required for full expression of P2X7 protein. Indeed suppression of Caveolin-1 protein expression in E10 cells using short hairpin RNAs resulted in a large reduction in P2X7 protein expression. Our data demonstrate a potential interaction between P2X7 protein and Caveolin-1 in lipid rafts and provide a basis for further functional and biochemical studies to probe the physiologic significance of this interaction. Extracellular nucleotide signaling in vertebrate cells is mediated by plasma membrane P2 receptors which may be divided into two .