J Cancer 2011; 2:165-176. doi:10.7150/jca.2.165 This volume Cite

Research Paper

Protein Signatures in Human MDA-MB-231 Breast Cancer Cells Indicating a More Invasive Phenotype Following Knockdown of Human Endometase/Matrilysin-2 by siRNA

Seakwoo Lee1*, Doris Terry2, Douglas R. Hurst3, Danny R. Welch3, Qing-Xiang Amy Sang1✉

1. Department of Chemistry and Biochemistry and Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32306-4390, USA;
2. Department of Biomedical Sciences, College of Medicine, Florida State University, Tallahassee, Florida 32306-4390, USA;
3. Department of Pathology, Comprehensive Cancer Center, and National Foundation for Cancer Research Center for Metastasis Research, University of Alabama at Birmingham, Birmingham, Alabama, USA.
* Present address: Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland, 21205, USA.

Citation:
Lee S, Terry D, Hurst DR, Welch DR, Sang QXA. Protein Signatures in Human MDA-MB-231 Breast Cancer Cells Indicating a More Invasive Phenotype Following Knockdown of Human Endometase/Matrilysin-2 by siRNA. J Cancer 2011; 2:165-176. doi:10.7150/jca.2.165. https://www.jcancer.org/v02p0165.htm
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Abstract

Human matrix metalloproteinase-26 (MMP-26/endometase/matrilysin-2) is a putative biomarker for carcinomas of breast, prostate, and other cancers of epithelial origin. MMP-26 expression was silenced using small interfering RNA (siRNA) in the human breast cancer cell line MDA-MB-231. Immunological and proteomics approaches, including two-dimensional gel electrophoresis and matrix assisted laser desorption/ionization time-of-flight mass spectrometry, were employed to identify differential protein expression in MMP-26 knockdown cells. A comparison of the protein expression profiles of control and MMP-26 knockdown cells revealed nine differentially regulated proteins. Five of the proteins (heat shock protein 90, glucose-regulated protein 78 (GRP78), annexin V, tropomyosin, and peroxiredoxin II) were up-regulated, while alpha-tubulin, cystatin SA-III, breast cancer metastasis suppressor 1 (BRMS1) and beta-actin were down-regulated. This decrease of BRMS1 expression is concomitant with an increase of invasion through matrix-coated membranes. These results suggest an important role for MMP-26 in the regulation of proteins involved in invasive and metastatic breast cancers.

Keywords: Matrix metalloproteinase (MMP), MMP-26, breast cancer metastasis suppressor 1, putative protein biomarkers, invasion and metastasis, mass spectrometry, proteomics


Citation styles

APA
Lee, S., Terry, D., Hurst, D.R., Welch, D.R., Sang, Q.X.A. (2011). Protein Signatures in Human MDA-MB-231 Breast Cancer Cells Indicating a More Invasive Phenotype Following Knockdown of Human Endometase/Matrilysin-2 by siRNA. Journal of Cancer, 2, 165-176. https://doi.org/10.7150/jca.2.165.

ACS
Lee, S.; Terry, D.; Hurst, D.R.; Welch, D.R.; Sang, Q.X.A. Protein Signatures in Human MDA-MB-231 Breast Cancer Cells Indicating a More Invasive Phenotype Following Knockdown of Human Endometase/Matrilysin-2 by siRNA. J. Cancer 2011, 2, 165-176. DOI: 10.7150/jca.2.165.

NLM
Lee S, Terry D, Hurst DR, Welch DR, Sang QXA. Protein Signatures in Human MDA-MB-231 Breast Cancer Cells Indicating a More Invasive Phenotype Following Knockdown of Human Endometase/Matrilysin-2 by siRNA. J Cancer 2011; 2:165-176. doi:10.7150/jca.2.165. https://www.jcancer.org/v02p0165.htm

CSE
Lee S, Terry D, Hurst DR, Welch DR, Sang QXA. 2011. Protein Signatures in Human MDA-MB-231 Breast Cancer Cells Indicating a More Invasive Phenotype Following Knockdown of Human Endometase/Matrilysin-2 by siRNA. J Cancer. 2:165-176.

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