期刊
JOURNAL OF BIOMEDICAL MATERIALS RESEARCH PART A
卷 109, 期 10, 页码 1990-2000出版社
WILEY
DOI: 10.1002/jbm.a.37191
关键词
extracellular matrix; mechanotransduction; polyelectrolyte complex; three-dimensional model; tumor microenvironment
资金
- UCF
This study investigated the response of BCa cells to CA scaffold stiffness by preparing CA scaffolds of different concentrations. It was found that 231 cells responded to the stiffness of the CA scaffolds and formed clusters of different sizes. Cell migration speed also varied on different surfaces, suggesting a non-integrin-based mechanism may explain the observed mechanotransduction response.
Breast cancer (BCa) is one of the most common cancers for women and metastatic BCa causes the majority of deaths. The extracellular matrix (ECM) stiffens during cancer progression and provides biophysical signals to modulate proliferation, morphology, and metastasis. Cells utilize mechanotransduction and integrins to sense and respond to ECM stiffness. Chitosan-alginate (CA) scaffolds have been used for 3D culture, but lack integrin binding ligands, resulting in round cell morphology and limited cell-material interaction. In this study, 2, 4, and 6 wt% CA scaffolds were produced to mimic the stages of BCa progression and evaluate the BCa response to CA scaffold stiffness. All three CA scaffold compositions highly porous with interconnected pores and scaffold stiffness increased with increasing polymer concentration. MDA-MB-231 (231) cells were cultured in CA scaffolds and 2D cultures for 7 d. All CA scaffold cultures had similar cell numbers at 7 d and the 231 cells formed clusters that increased in size during the culture. The 2 wt% CA had the largest clusters throughout the 7 d culture compared with the 4 and 6 wt% CA. The 231 cell migration was evaluated on 2D surfaces after 7 d culture. The 6 wt% CA cultured cells had the greatest migration speed, followed by 4 wt% CA, 2D cultures, and 2 wt % CA. These results suggest that 231 cells sensed the stiffness of CA scaffolds without the presence of focal adhesions. This indicates that a non-integrin-based mechanism may explain the observed mechanotransduction response.
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