Table 2.
Selectivity profiling of reference KATP inhibitors.
| Compound | Structure | Kir6.1/SUR2B | Kir6.2/SUR1 | Kir6.2/SUR2A |
|---|---|---|---|---|
| IC50 (µM) | IC50 (µM) | IC50 (µM) | ||
| Glibenclamide |
|
0.021 ± 0.014 (5) | 0.00087 ± 0.0005 (5) | 0.0099 ± 0.0041 (5) |
| Glimepiride |
|
0.033 ± 0.023 (6) | 0.0023 ± 0.0012 (6) | 0.017 ± 0.009 (5) |
| Gliquidone |
|
4.5 ± 3.6 (6) | 0.0069 ± 0.0050 (6) | 0.78 ± 0.58 (6) |
| Gliclazide |
|
24 ± 11 (5) | 0.61 ± 0.45 (7) | 55 ± 22 (6) |
| Tolbutamide |
|
41 ± 11 (5) | 7.5 ± 4.1 (6) | 71 ± 12 (5) |
| Repaglinide |
|
0.0011 ± 0.0006 (5) | 0.0039 ± 0.0014 (5) | 0.00094 ± 0.00046 (5) |
| Nateglinide |
|
14 ± 6.7 (6) | 0.044 ± 0.013 (5) | 16 ± 7.3 (5) |
| Troglitazone |
|
10 ± 6.5 (8) | 14 ± 3.1 (5) | 30 ± 16 (5) |
| Rosiglitazone |
|
8.5 ± 4.6 (6) | >100 (5) | >100 (5) |
| PNU-37883A |
|
0.29 ± 0.21 (6) | >100 (6) | >100 (6) |
Functional properties of KATP channel inhibitors were characterized at human Kir6.1/SUR2B, Kir6.2/SUR1, and Kir6.2/SUR2A channels stably expressed in HEK293 cells. The values are given as mean ± S.D. and the number of individual experiments (each performed in quadruplicate) are in parentheses (n).