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Mekahli, D; Sammels, E; Luyten, T; Welkenhuyzen, K; van den Heuvel, L.P; Levtchenko, E.N; Gijsbers, R; Bultynck, G; Parys, J.B; De Smedt, H; Missiaen, L
Cell calcium (Edinburgh), 06/2012, Letnik: 51, Številka: 6Journal Article
Abstract Autosomal dominant polycystic kidney disease is caused by loss-of-function mutations in the PKD1 or PKD2 genes encoding respectively polycystin-1 and polycystin-2. Polycystin-2 stimulates the inositol trisphosphate (IP3 ) receptor (IP3 R), a Ca2+ -release channel in the endoplasmic reticulum (ER). The effect of ER-located polycystin-1 is less clear. Polycystin-1 has been reported both to stimulate and to inhibit the IP3 R. We now studied the effect of polycystin-1 and of polycystin-2 on the IP3 R activity under conditions where the cytosolic Ca2+ concentration was kept constant and the reuptake of released Ca2+ was prevented. We also studied the interdependence of the interaction of polycystin-1 and polycystin-2 with the IP3 R. The experiments were done in conditionally immortalized human proximal-tubule epithelial cells in which one or both polycystins were knocked down using lentiviral vectors containing miRNA-based short hairpins. The Ca2+ release was induced in plasma membrane-permeabilized cells by various IP3 concentrations at a fixed Ca2+ concentration under unidirectional45 Ca2+ -efflux conditions. We now report that knock down of polycystin-1 or of polycystin-2 inhibited the IP3 -induced Ca2+ release. The simultaneous presence of the two polycystins was required to fully amplify the IP3 -induced Ca2+ release, since the presence of polycystin-1 alone or of polycystin-2 alone did not result in an increased Ca2+ release. These novel findings indicate that ER-located polycystin-1 and polycystin-2 operate as a functional complex. They are compatible with the view that loss-of-function mutations in PKD1 and in PKD2 both cause autosomal dominant polycystic kidney disease.
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