Xiaomei Yang1, Yang Si1, Tao Tao2, Tracey A Martin3, Shan Cheng1, Hefen Yu1, Jinyao Li1, Junqi He4, Wen G Jiang5. 1. Department of Biochemistry and Molecular Biology, Basic Medical School, Capital Medical University, Beijing, P.R. China Cancer Institute of Capital Medical University, Capital Medical University, Beijing, P.R. China Capital Medical University-Cardiff University Joint Centre For Biomedical Research, Capital Medical University, Beijing, P.R. China Beijing Key Laboratory for Cancer Invasion and Metastasis Research, Capital Medical University, Beijing, P.R. China Beijing International Cooperation Base for Science and Technology on China-UK Cancer Research, Capital Medical University, Beijing, P.R. China. 2. Department of Biochemistry and Molecular Biology, Basic Medical School, Capital Medical University, Beijing, P.R. China. 3. Metastasis & Angiogenesis Research Group, Cardiff China Medical Research Collaborative, Cardiff University School of Medicine, Cardiff, U.K. 4. Department of Biochemistry and Molecular Biology, Basic Medical School, Capital Medical University, Beijing, P.R. China Cancer Institute of Capital Medical University, Capital Medical University, Beijing, P.R. China Capital Medical University-Cardiff University Joint Centre For Biomedical Research, Capital Medical University, Beijing, P.R. China Beijing Key Laboratory for Cancer Invasion and Metastasis Research, Capital Medical University, Beijing, P.R. China Beijing International Cooperation Base for Science and Technology on China-UK Cancer Research, Capital Medical University, Beijing, P.R. China jq_he@ccmu.edu.cn JiangW@cardiff.ac.uk. 5. Beijing Key Laboratory for Cancer Invasion and Metastasis Research, Capital Medical University, Beijing, P.R. China Metastasis & Angiogenesis Research Group, Cardiff China Medical Research Collaborative, Cardiff University School of Medicine, Cardiff, U.K. jq_he@ccmu.edu.cn JiangW@cardiff.ac.uk.
Abstract
BACKGROUND: The mitochondrial protein translocase of inner mitochondrial membrane 17 homolog A (TIMM17A) has been identified as a biomarker of breast cancer. The present study aimed to investigate the biological role of TIMM17A in human breast cancer cells. MATERIALS AND METHODS: Anti-TIMM17A transgenes were stably transfected into MDA MB-231 and MCF-7 breast cancer cell lines. The impact of TIMM17A knock-down on cell migration and invasion were evaluated using the respective cell models. RESULTS: Reducing the expression of TIMM17A in breast cancer cells resulted in reduction of cell migration using electric cell-substrate impedance sensing. It was also found that reduction of TIMM17A expression resulted in reduction of cell invasion compared to vector control. CONCLUSION: TIMM17A has a profound impact on the cellular function of breast cancer cells. A decrease of TIMM17A expression is associated with the reduction of the aggressiveness of breast cancer cells. TIMM17A, therefore, has potential in prognosis and treatment of breast cancer. Copyright
BACKGROUND: The mitochondrial protein translocase of inner mitochondrial membrane 17 homolog A (TIMM17A) has been identified as a biomarker of breast cancer. The present study aimed to investigate the biological role of TIMM17A in humanbreast cancer cells. MATERIALS AND METHODS: Anti-TIMM17A transgenes were stably transfected into MDA MB-231 and MCF-7 breast cancer cell lines. The impact of TIMM17A knock-down on cell migration and invasion were evaluated using the respective cell models. RESULTS: Reducing the expression of TIMM17A in breast cancer cells resulted in reduction of cell migration using electric cell-substrate impedance sensing. It was also found that reduction of TIMM17A expression resulted in reduction of cell invasion compared to vector control. CONCLUSION:TIMM17A has a profound impact on the cellular function of breast cancer cells. A decrease of TIMM17A expression is associated with the reduction of the aggressiveness of breast cancer cells. TIMM17A, therefore, has potential in prognosis and treatment of breast cancer. Copyright