%0 Journal Article
%T Glycosylated VCAM-1 isoforms revealed in 2D western blots of HUVECs treated with tumoral soluble factors of breast cancer cells
%A Delina Montes-S¨¢nchez
%A Jose Ventura
%A Irma Mitre
%A Susana Fr¨ªas
%A Layla Mich¨¢n
%A Aurora Espejel-Nu£¿ez
%A Felipe Vadillo-Ortega
%A Alejandro Zentella
%J BMC Chemical Biology
%D 2009
%I BioMed Central
%R 10.1186/1472-6769-9-7
%X 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.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.Endothelial cells line the inside of all blood vessels forming an interface between circulating blood and the underlying tissues. As such, endothelial cells comprise, a critical metabolic organ involved in the generation and regulation of multiple physiological and pathological processes such as coagulation, hemostasis of local vascular pressure, inflammation, atherosclerosis, angiogenesis, and metastasis [1]. In the context of the current model of tumoral dissemination, glycoproteins including cell adhesion molecules are expressed on the apical endothelial membrane, interacting with counter-receptors on circulating cancer cells, facilitating the spread of the disease [2,3].Glycoproteins are prominent constituents of biological membranes, and are involved in various biological functions, including immunological protection, enzymatic catalysis, hormonal control, ion transport, structural support, molecular recognition, and cell adhesion. Structurally, glycoproteins are comprised of a peptide backbone, with carbohydrate chains covalently attached to asparagine (N-glycan) or serine/threonine (O-glycan) residues [4,5]. The immunoglobulin super family of cell adhesion molecules (IgCAMs) constitutes a larg
%U http://www.biomedcentral.com/1472-6769/9/7