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Repositorio Atenea de la Facultad de Ciencias, UNAM >
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Please use this identifier to cite or link to this item:
http://hdl.handle.net/11154/3946
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Title: | Glycosylated VCAM-1 isoforms revealed in 2D westerns of HUVECs treated with tumoral soluble factors of breast cancer cells |
Authors: | Sánchez, DM Ventura, JL Mitre, I Frías, S Nuñez, AE Ortega, FV Zentella, A Michán Aguirre, Layla |
Keywords: | cáncer mama huvec´s |
Issue Date: | 2009 |
Citation: | Sanchez, D. M., Ventura, J. L., Mitre, I., Frias, S., Michan-Aguirre, Layla., Nunez, A. E., Ortega, F. V., & Zentella, A. (2009). Glycosylated VCAM-1 isoforms revealed in 2D westerns of HUVECs treated with tumoral soluble factors of breast cancer cells. BMC Chemical Biology , 9 (1), 7+. URL http://dx.doi.org/10.1186/1472-6769-9-7 |
Abstract: | Background
Several common aspects of endothelial phenotype, such as the expression of cell adhesion molecules, are shared between metastasis and inflammation. Here, we analyzed VCAM-1 variants as biological markers of these two types of endothelial cell activation. With the combination of 2-DE and western blot techniques and the aid of tunicamycin, we analyzed N-glycosylation variants of VCAM-1 in primary human endothelial cells stimulated with either TNF or tumoral soluble factors (TSF's) derived from the human breast cancer cell line ZR75.30.
Results
Treatments induced a pro-adhesive endothelial phenotype. 2D western blots analysis of cells subjected to both treatments revealed the expression of the two known VCAM-1 isoforms and of previously unknown isoforms. In particular TSFZR75.30 induced an isoform with a relative molecular mass (Mr) and isoelectric point (pI) of 75-77 kDa and 5.0, respectively.
Conclusion
The unknown isoforms of VCAM-1 that were found to be overexpressed after treatment with TSF's compared with TNF, could serve as biomarkers to discriminate between inflammation and metastasis. 2D western blots revealed three new VCAM-1 isoforms expressed in primary human endothelial cells in response to TSF stimulation. Each of these isoforms varies in Mr and pI and could be the result of differential glycosylation states. |
URI: | http://hdl.handle.net/11154/3946 |
ISSN: | 1472-6769 |
Appears in Collections: | Departamento de Biología Comparada
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