Human colon cancer cells express multiple glycoprotein ligands for E-selectin.

Abstract:

:The interaction between the colon tumor cell surface and the endothelial cell layer is an important component of tumor intravasation, extravasation, and metastasis. Multiple studies suggest that tumor cells may bind to E-selectin expressed on endothelial cells during these processes. To identify possible E-selectin ligands on tumor cells that may participate in this mechanism, we used E-selectin-Ig chimera affinity chromatography to isolate glycoproteins from the human colon cancer cell line Colo-205. Binding of these cells to E-selectin was specific, required the presence of calcium, and could be blocked by antibodies against E-selectin. We identified LAMP-1 (lysosomal membrane glycoprotein-1), LAMP-2, and two high molecular weight glycoproteins (>400 kDa and 300 kDa) as the main E-selectin ligands on Colo-205 cells. Treatment of the cells with N-glycanase and O-sialoglycoprotease abolished their binding to E-selectin. The high MW glycoproteins contained sialyl Lewis X and/or sialyl Lewis A glycoconjugates, and appeared to be either alternatively spliced or alternatively glycosylated forms of MUC-1 (mucin-1).

journal_name

Int J Oncol

authors

Tomlinson J,Wang JL,Barsky SH,Lee MC,Bischoff J,Nguyen M

doi

10.3892/ijo.16.2.347

keywords:

subject

Has Abstract

pub_date

2000-02-01 00:00:00

pages

347-53

issue

2

eissn

1019-6439

issn

1791-2423

journal_volume

16

pub_type

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