Skip to main content
. Author manuscript; available in PMC: 2013 Jan 20.
Published in final edited form as: Circ Res. 2011 Dec 15;110(2):265–274. doi: 10.1161/CIRCRESAHA.111.253260

Figure 2. Transgenic mice with cardiac-specific overexpression of wild type (WT) human β2AR or its mutants lacking PKA or GRK phosphorylation sites.

Figure 2

(A) Schematic presentation showing β2AR phosphorylation sites for PKA or GRK. (B) The specific sequences of WT β2AR or its mutants lacking PKA (PKA-) or GRK (GRK-) phosphorylation sites. (C) The β2AR density was 9.6 ± 1.3 fmol/ mg protein and total βAR density was 28.6 ± 3.4 fmol/ mg protein in NTG mice (n=6). In transgenic mice, β2AR density was 856 ± 45, 828 ± 33 and 850 ± 23 fmol/mg protein for WT TG, PKA- TG, and GRK- TG mice, respectively, (n=6 for each group). (D) Phosphorylation of β2AR in PKA or GRK sites were assayed by Western blot using a site-specific antibody reacting with phosphorylated β2AR at a PKA site (aa262) or GRK sites (aa355 and aa366). The antibodies were raised against the peptides CDRTGHGLRRSpSKF-NH2 for the anti-pSer262 PKA site (clone 2G3) and CKAYGNGYpSpSNGN-NH2 for the anti-pS (Ser355, 356) (clone 5C3). Total expression of β2AR in transgenic mouse hearts was detected by Western blot using an antibody reacting with β2ARs.