Fig. 7.
Fig. 7. Phosphorylation of overexpressed hTRPC1 and mTRPC6 using CAT of cAMP-PK. / 500 μg membrane proteins from QBI-293A cells overexpressing either hTRPC1 or mTRPC6 were incubated with γ[32P] ATP in the absence of CAT (CON), presence of 350 U CAT (+PKA CAT), or presence of 1 μM cAMP-PK inhibitor peptide (+PKA INHIB). (A) Autoradiography of Ank immunoprecipitations of overexpressed hTRPC1 and subsequent probing of the Western blot with the Ank antibody (5 μg/mL). (B) Autoradiography of anti-TRPC6 immunoprecipitations of overexpressed mTRPC6 and probing with anti-TRPC6 antibody (1/400). Note both partial and fully glycosylated forms of mTRPC6 undergo phosphorylation. Molecular size markers are noted in kilodaltons (kDa) and the TRPC protein identifications indicated with arrows.

Phosphorylation of overexpressed hTRPC1 and mTRPC6 using CAT of cAMP-PK.

500 μg membrane proteins from QBI-293A cells overexpressing either hTRPC1 or mTRPC6 were incubated with γ[32P] ATP in the absence of CAT (CON), presence of 350 U CAT (+PKA CAT), or presence of 1 μM cAMP-PK inhibitor peptide (+PKA INHIB). (A) Autoradiography of Ank immunoprecipitations of overexpressed hTRPC1 and subsequent probing of the Western blot with the Ank antibody (5 μg/mL). (B) Autoradiography of anti-TRPC6 immunoprecipitations of overexpressed mTRPC6 and probing with anti-TRPC6 antibody (1/400). Note both partial and fully glycosylated forms of mTRPC6 undergo phosphorylation. Molecular size markers are noted in kilodaltons (kDa) and the TRPC protein identifications indicated with arrows.

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