In Hs578T breast cancer cells, [LR3]IGF-I did not reduce the proportion of phosphorylated IGFBP-3, whereas IGF-I did.
In plain wordsIn lab tests on breast cancer cells, an IGF-I analogue did not change IGFBP-3 phosphorylation, while natural IGF-I did.
- Peptide
- IGF-1 LR3
- Outcome
- No significant changeProportion of phosphorylated IGFBP-3 in conditioned medium
- Study
humann: not reported in source
Hs578T breast cancer cells- Comparator
- Native IGF-I
- Outcome group
- Receptor activity and mechanism · Cancer
- Studied dose
- Dose not stated
Source sentences
IGF-I, but not [LR3]IGF-I, reduced the proportion of phosphorylated IGFBP-3 in Hs578T conditioned medium, consistent with increased release of non-phosphorylated, cell-associated IGFBP-3.
1 context sentence(design, population, supporting numbers)
In this study, we have examined phosphorylation of IGFBP-3 in two breast cancer cell lines: the estrogen receptor negative (ER-ve) Hs578T cell line in which IGFBP-3 is normally expressed, and ER+ve T47D breast cancer cells transfected with IGFBP-3 cDNA (T47D(BP-3)) and therefore expressing IGFBP-3 constitutively.