TABLE 2.
Competition binding using the two radioligands
| Ligand | [125I]‐hGLP‐2(1–33.M10Y) | [125I]‐hGLP‐2(3–33,M10Y) | |||||||
|---|---|---|---|---|---|---|---|---|---|
| pIC50 (M) ± SEM | K i (K D ) (nM) | % max ± SEM | n | pIC50 (M) ± SEM | Ki (K D ) (nM) | % max ± SEM | n | ||
| hGLP‐2R | hGLP‐2(1–33) | 7.9 ± 0.12 | 14 | 98.8 ± 4.1 | 3 | 7.8 ± 0.09 | 15 | 99.4 ± 2.8 | 5 |
| hGLP‐2(1–33, M10Y) | 7.2 ± 0.07 | 59 (K D ) | 99.7 ± 1.8 | 5 | 7.1 ± 0.13 | 78 | 98.9 ± 3.1 | 6 | |
| hGLP‐2(3–33) | 7.2 ± 0.08 | 57 | 100.0 ± 2.1 | 5 | 7.1 ± 0.13 | 81 | 98.8 ± 3.1 | 6 | |
| hGLP‐2(3–33, M10Y) | 7.3 ± 0.10 | 49 | 99.5 ± 3.0 | 5 | 7.4 ± 0.13 | 41 (K D ) | 98.7 ± 3.6 | 5 | |
| mGLP‐2R | hGLP‐2(1–33) | 8.2 ± 0.13 | 6.6 | 97.7 ± 3.3 | 3 | 7.7 ± 0.16 | 18 | 92.3 ± 4.1 | 3 |
| rGLP‐2R | hGLP‐2(1–33) | 8.3 ± 0.24 | 5.4 | 89.5 ± 6.2 | 3 | 8.2 ± 0.18 | 6.5 | 95.9 ± 5.2 | 3 |
| hGLP‐1R | hGLP‐2(1–33) | 6.9 ± 0.50 | 130 | 37.8 ± 3.6 | 3 | 6.5 ± 0.5 | 330 | 26.7 ± 2.3 | 3 |
| mGLP‐1R | hGLP‐2(1–33) | 6.7 ± 0.22 | 208 | 84.5 ± 3.8 | 3 | 6.7 ± 0.14 | 183 | 93.3 ± 2.4 | 3 |
| rGLP‐1R | hGLP‐2(1–33) | N.B. | N.B. | N.B. | 3 | N.B. | N.B. | N.B. | 3 |
Note: Competitive binding. Affinities, displayed as pIC50, K i and K D values of GLP‐2 and GLP‐2 variants measured in competition with either [125I]‐hGLP‐2(1–33,M10Y), left‐hand side, or [125I]‐hGLP‐2(3–33,M10Y), right‐hand side. All data were fitted with a three‐parameter logistic curve to obtain pIC50. Data represent the mean ± SEM of at least three independent experiments performed in duplicates. The numbers of experiments, n, are indicated in the table. N.B. refers to no binding detected. R refers to receptor.