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Am J Physiol Cell Physiol (December 11, 2002). doi:10.1152/ajpcell.00423.2002
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Articles in PresS, published online ahead of print December 11, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00423.2002
Submitted on September 16, 2002
Accepted on December 4, 2002

Colon Carcinoma Cell Glycolipids, Integrins, and Other Glycoproteins Mediate Adhesion to HUVECs Under Flow

Monica M Burdick1, J. Michael McCaffery2, Young S Kim3, Bruce S Bochner4, and Konstantinos Konstantopoulos1*

1 Department of Chemical Engineering, Johns Hopkins University, Baltimore, Maryland, USA
2 Integrated Imaging Center, Department of Biology, Johns Hopkins University, Baltimore, Maryland, USA
3 Gastrointestinal Research Laboratory, Veterans Affairs Medical Center and Department of Medicine, University of California, San Francisco, California, USA
4 Department of Medicine, Division of Clinical Immunology, Johns Hopkins University, Baltimore, Maryland, USA

* To whom correspondence should be addressed. E-mail: kkonsta1{at}jhu.edu.

This study was undertaken to investigate the molecular constituents mediating LS174T colon adenocarcinoma cell adhesion to 4 h TNF-{alpha} stimulated human umbilical vein endothelial cells (HUVECs) under flow. At 1 dyn/cm2, ~57% of cells rolled and then became firmly adherent, whereas others continuously rolled on endothelium. Initial cell binding was primarily mediated by endothelial E-selectin. By using neuraminidase, glycolipid biosynthesis inhibitor d,l-threo-1-phenyl-2-hexadecanoylamino-3-pyrrolidino-1-propanol.HCl (PPPP), trypsin, and flow cytometry, LS174T cells were shown to express sialyl Lewisx (sLex)- and di-sLex-, but not sLea-decorated glycolipid and glycoprotein ligands for E-selectin. The cells preferentially employed sialylated glycoproteins over glycolipids in adhesion as measured by conversion of rolling to firm adhesion, resistance to detachment by increased shear stress, and rolling velocity. However, a non-sialylated E-selectin counter-receptor also exists. Furthermore, LS174T {alpha}2, {alpha}6, and {beta}1 integrins support a minor pathway in adhesion to HUVECs. Finally, tumor cell attachment specifically increases HUVEC endocytosis of E-selectin. Altogether, the data indicate the complexity of carcinoma cell-endothelium adhesion via sialylated glycoconjugates, integrins, and their respective counter-receptors.




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