In malignant breast cancer, estrogen metabolism is altered, favoring the accumulation of hydroxyestradiols, which can generate free radicals. These reactive species can activate matrix metalloproteinases (MMPs), which in turn can hydrolyze the proteins of the extracellular matrix (ECM) that act as a
Invasive breast cancer cells exhibit increased mobility of the actin-binding protein CapG
✍ Scribed by Malte Renz; Beate Betz; Dieter Niederacher; Hans Georg Bender; Jörg Langowski
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- French
- Weight
- 282 KB
- Volume
- 122
- Category
- Article
- ISSN
- 0020-7136
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
The CapG protein, a Gelsolin‐related actin‐binding protein, is expressed at higher levels in breast cancer, especially in metastasizing breast cancer, than in normal breast epithelium. Furthermore, it is known that an increased expression of the CapG protein triggers an increase in cell motility. According to in vitro experiments, it was supposed that it is the nuclear fraction of the protein, which causes the increase in cell motility. Here, we examined the dynamical distribution of the CapG protein within the living cell, i.e. the import of the CapG protein into the nucleus. The nuclear import kinetics of invasive, metastasizing breast cancer cells were compared to the import kinetics of non‐neoplastic cells similar to normal breast epithelium. FRAP kinetics showed a highly significant increase in the recovery of photobleached CapG–eGFP in the cancer cells, so that a differentiation of invasive, metastasizing cells and non‐invasive, non‐metastasizing cells on the basis of transport processes of the CapG protein between the nucleus and the cytoplasm seems to be possible. Comprehension of the mobility and compartmentalization of the CapG protein in normal and in cancer cells in vivo could constitute a new basis to characterize the invasiveness and metastasizing potential of breast cancer. © 2007 Wiley‐Liss, Inc.
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