Skip to main content
. Author manuscript; available in PMC: 2015 Jun 15.
Published in final edited form as: Bioorg Med Chem. 2014 Apr 20;22(12):3123–3140. doi: 10.1016/j.bmc.2014.04.024

Table 1.

Binding Selectivity of DAG-indololactones for PKCα and PKCε versus RasGRP.

Compound PKCαa Ki(nM) PKCε Ki(nM) RasGRP3 Ki(nM) PKCα: RasGRP3 PKCε: RasGRP3 RasGRP1-C1 Ki(nM) PKCα: RasGRP1 PKCε: RasGRP1
1 16.2 ± 1.0 21.1 ± 1.9 0.33 ± 0.06 49 64 0.25 ± 0.10 65 84
2 17.8 ± 2.0 14.6 ± 2.7 1.63 ± 0.18 11 9.0 1.55 ± 0.10 10 9.4
3 8.25 ± 0.88 2.17 ± 0.36 0.34 ± 0.01 24 6.4 0.41 ± 0.10 24 5.3
4 7.5 ± 1.0 8.08 ± 0.31 1.22 ± 0.21 6 6.6 0.87 ± 0.04 9 9.3
5 12.9 ± 1.4 11.7 ± 0.30 1.12 ± 0.05 10 11 0.69 ± 0.14 19 17
[3H]PDBub 0.17 ± 0.02 0.22 ± 0.05 0.42 ± 0.03 --- — 0.12 ± 0.01 — —
a

Values represent mean ± SEM of triplicate independent experiments

b

[Kd(nM]