Colon carcinoma cell glycolipids, integrins, and other glycoproteins mediate adhesion to HUVECs under flow

Monica M. Burdick, J. Michael McCaffery, Young S. Kim, Bruce S. Bochner, Konstantinos Konstantopoulos

Research output: Contribution to journalArticlepeer-review

97 Scopus citations


This study was undertaken to investigate the molecular constituents mediating LS174T colon adenocarcinoma cell adhesion to 4-h TNF-α-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, trypsin, and flow cytometry, LS174T cells were shown to express sialyl Lewisx(sLex)- and di-sLex-decorated, 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 nonsialylated E-selectin counterreceptor also exists. Furthermore, LS174T α2, α6, and β1, 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 counterreceptors.

Original languageEnglish (US)
Pages (from-to)C977-C987
JournalAmerican Journal of Physiology - Cell Physiology
Issue number4 53-4
StatePublished - Apr 1 2003


  • E-selectin
  • Glycolipid
  • Shear stress
  • Sialyl Lewis

ASJC Scopus subject areas

  • Physiology
  • Cell Biology


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