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Mol. Cells 2010; 30(4): 341-345

Published online September 10, 2010

https://doi.org/10.1007/s10059-010-0124-x

© The Korean Society for Molecular and Cellular Biology

Visfatin Stimulates Proliferation of MCF-7 Human Breast Cancer Cells

Jae Geun Kim1,2, Eun Ok Kim1, Bo Ra Jeong1, Young Joo Min2,4, Jeong Woo Park1,2, Eun Sook Kim3, Il Seong Namgoong3, Young Il Kim3, and Byung Ju Lee1,*

1Department of Biological Sciences, College of Natural Sciences, University of Ulsan, Ulsan 680-749, Korea, 2Biomedical Research Center, College of Medicine, University of Ulsan, Ulsan 682-714, Korea, 3Department of Internal Medicine, Ulsan University Hospital, University of Ulsan College of Medicine, Ulsan 682-714, Korea, 4Division of Hematology and Oncology, Ulsan University Hospital, University of Ulsan College of Medicine, Ulsan 682-714, Korea

Correspondence to : *Correspondence: bjlee@ulsan.ac.kr

Received: March 29, 2010; Revised: July 7, 2010; Accepted: July 9, 2010

Abstract

Obesity, a condition characterized by increased fat con-tent and altered secretion of adipokines, is a risk factor for postmenopausal breast cancer. Visfatin has recently been established as a novel adipokine that is highly enriched in visceral fat. Here we report that visfatin regulated proliferation of MCF-7 human breast cancer cells. Exogenous administration of recombinant visfatin increased cell proliferation and DNA synthesis rate in MCF-7 cells. Furthermore, visfatin activated G1-S phase cell cycle progression by upregulation of cyclin D1 and cdk2 expression. Visfatin also increased the expression of matrix metalloproteinases 2, matrix metalloproteinases 9, and vascular endothelial growth factor genes, suggesting that it may function in metastasis and angiogenesis of breast cancer. Taken together, these findings suggest that visfatin plays an important role in breast cancer progression.

Keywords angiogenesis, breast cancer, metastasis, proliferation, visfatin

Article

Research Article

Mol. Cells 2010; 30(4): 341-345

Published online October 31, 2010 https://doi.org/10.1007/s10059-010-0124-x

Copyright © The Korean Society for Molecular and Cellular Biology.

Visfatin Stimulates Proliferation of MCF-7 Human Breast Cancer Cells

Jae Geun Kim1,2, Eun Ok Kim1, Bo Ra Jeong1, Young Joo Min2,4, Jeong Woo Park1,2, Eun Sook Kim3, Il Seong Namgoong3, Young Il Kim3, and Byung Ju Lee1,*

1Department of Biological Sciences, College of Natural Sciences, University of Ulsan, Ulsan 680-749, Korea, 2Biomedical Research Center, College of Medicine, University of Ulsan, Ulsan 682-714, Korea, 3Department of Internal Medicine, Ulsan University Hospital, University of Ulsan College of Medicine, Ulsan 682-714, Korea, 4Division of Hematology and Oncology, Ulsan University Hospital, University of Ulsan College of Medicine, Ulsan 682-714, Korea

Correspondence to:*Correspondence: bjlee@ulsan.ac.kr

Received: March 29, 2010; Revised: July 7, 2010; Accepted: July 9, 2010

Abstract

Obesity, a condition characterized by increased fat con-tent and altered secretion of adipokines, is a risk factor for postmenopausal breast cancer. Visfatin has recently been established as a novel adipokine that is highly enriched in visceral fat. Here we report that visfatin regulated proliferation of MCF-7 human breast cancer cells. Exogenous administration of recombinant visfatin increased cell proliferation and DNA synthesis rate in MCF-7 cells. Furthermore, visfatin activated G1-S phase cell cycle progression by upregulation of cyclin D1 and cdk2 expression. Visfatin also increased the expression of matrix metalloproteinases 2, matrix metalloproteinases 9, and vascular endothelial growth factor genes, suggesting that it may function in metastasis and angiogenesis of breast cancer. Taken together, these findings suggest that visfatin plays an important role in breast cancer progression.

Keywords: angiogenesis, breast cancer, metastasis, proliferation, visfatin

Mol. Cells
May 31, 2023 Vol.46 No.5, pp. 259~328
COVER PICTURE
The alpha-helices in the lamin filaments are depicted as coils, with different subdomains distinguished by various colors. Coil 1a is represented by magenta, coil 1b by yellow, L2 by green, coil 2a by white, coil 2b by brown, stutter by cyan, coil 2c by dark blue, and the lamin Ig-like domain by grey. In the background, cells are displayed, with the cytosol depicted in green and the nucleus in blue (Ahn et al., pp. 309-318).

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