Abstract

Chondrosarcoma, the second most common type of bone malignancy, is characterized by distant metastasis and local invasion. Previous studies have shown that treatment by pulsed electromagnetic field (PEMF) has beneficial effects on various cancer cells. In this study, we investigated the effects of PEMF applied for 3 and 7 days on the matrix metalloproteinase (MMP) levels in chondrosarcoma SW1353 cells stimulated with two different doses of IL-1β. SW1353 cells were treated with (0.5 and 5 ng/ml) IL-1β and PEMF exposure was applied either 3 or 7 days. MMP-9 and TIMP-1 levels were measured in conditioned media by enzyme-linked immunosorbent assay. The results were relative to protein levels. Statistical analyses were performed using one-way analysis of variance (ANOVA). P<0.05 was considered significant. PEMF treatment significantly decreased MMP-9 protein levels in human chondrosarcoma cells stimulated with 0.5 ng/ml IL-1β at day 7, whereas it did not show any effect on cells stimulated with 5 ng/ml IL-1β. There was no significant change in TIMP-1 protein levels either by IL-1β stimulation or by PEMF treatment. The results of this study showed that PEMF treatment suppressed IL-1β-mediated upregulation of MMP-9 protein levels in a dual effect manner. This finding may offer new perspectives in the therapy of bone cancer.

Highlights

  • Chondrosarcoma is one of the tumours of bone and soft tissue known as sarcomas and it is composed of cells derived from transformed cells that produce cartilage

  • We investigated the effects of pulsed electromagnetic field (PEMF) applied for 3 and 7 days on the matrix metalloproteinase (MMP) levels in chondrosarcoma SW1353 cells stimulated with two different doses of IL-1β

  • In order to investigate the effect of PEMF on MMP-9 and tissue inhibitors of matrix metalloproteinases (TIMPs)-1 protein levels produced by human chondrocytes, medium was harvested and subjected to enzyme-linked immunosorbent assays (ELISA)

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Summary

Introduction

Chondrosarcoma is one of the tumours of bone and soft tissue known as sarcomas and it is composed of cells derived from transformed cells that produce cartilage. One family of proteases which take a role in tumour invasion and metastasis is matrix metalloproteinases (MMPs) (Wang et al, 2014). Proteolytic activities of MMPs are inhibited by tissue inhibitors of matrix metalloproteinases (TIMPs). It is known that the balance between MMP and TIMP levels is a critical determinant of proteolytic degradation. Numerous clinical and experimental studies have demonstrated that elevated levels of MMPs are associated with tumour growth, cancer progression and metastasis (Nelson et al, 2000; Benassi et al, 2001; Wang et al, 2014; Yadav et al, 2014; Zhu et al, 2014). In cancer the production of MMP is stimulated by inflammatory mediators and the activity of MMP under different stimulators has been reported (Pei et al, 2006; Lim et al, 2011; Lee et al, 2012)

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