α2,6-sialyltransferase gene transfection into a human glioma cell line (U373 MG) results in decreased invasivity

Hirotaka Yamamoto, Yoichi Kaneko, Abdelhadi Rebbaa, Eric G. Bremer, Joseph R. Moskal*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

34 Scopus citations

Abstract

Glycosyltransferase gene transfection into cell lines has been an approach used successfully to elucidate the functional role of cell surface glycoconjugates. We have transfected the rat CMP-NeuAc:Galβ1,4GlcNAc α2,6- sialyltransferase (EC 2.4.99.1) gene into a human, tumorigenic, glioma cell line, U373 MG. This transfection led to a marked inhibition of invasivity, alterations in adhesivity to fibronectin and collagen matrices, and inappropriately sialylated α3β1 integrin. Adhesion-mediated protein tyrosine phosphorylation was reduced in the transfectants despite increased expression of focal adhesion kinase, p125(fak). Furthermore, the transfectants showed a distinct cell morphology, an increased number of focal adhesion sites, and different sensitivity to cytochalasin D treatment than control U373 MG cells. These results suggest that inappropriate sialylation of cell surface glycoconjugates, such as integrins, can change focal adhesion as well as adhesion-mediated signal transduction and block glioma cell invasivity in vitro.

Original languageEnglish (US)
Pages (from-to)2566-2576
Number of pages11
JournalJournal of neurochemistry
Volume68
Issue number6
DOIs
StatePublished - Jun 1997

Keywords

  • Focal adhesion kinase
  • Glioma
  • Integrin
  • Invasivity
  • Sialyltransferase

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

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