Inhibition of LRP-Mediated Degradation of125I-RAP by LRP Fragments
Cell Line . | Unlabeled Competitor . | % Degradation of125I-RAP . | |
---|---|---|---|
MEF 1 | None | 100.0 ± 2.3 | |
400 nmol/L | E4 | 100.7 ± 2.9 | |
E4-C3 | 99.8 ± 1.5 | ||
E4-C10 | 39.9 ± 0.3 | ||
C9-E6 | 103.6 ± 3.0 | ||
E5-AA1399 | 101.8 ± 2.9 | ||
200 nmol/L | RAP | 24.9 ± 0.4 | |
PEA 13 | None | 14.4 ± 0.3 |
Cell Line . | Unlabeled Competitor . | % Degradation of125I-RAP . | |
---|---|---|---|
MEF 1 | None | 100.0 ± 2.3 | |
400 nmol/L | E4 | 100.7 ± 2.9 | |
E4-C3 | 99.8 ± 1.5 | ||
E4-C10 | 39.9 ± 0.3 | ||
C9-E6 | 103.6 ± 3.0 | ||
E5-AA1399 | 101.8 ± 2.9 | ||
200 nmol/L | RAP | 24.9 ± 0.4 | |
PEA 13 | None | 14.4 ± 0.3 |
Replicate monolayers of wild-type (MEF 1) or LRP-deficient (PEA 13) mouse fibroblasts were incubated with serum-free media containing125I-RAP and recombinant LRP fragments. After incubation at 37°C for 4 hours, the total amount of 125I-RAP degradation products secreted into the media was measured. % Degradation is the mean of triplicates ± 1 SD and is normalized to the amount of degradation products released by MEF 1 cells with no competitor added.