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Glycobiology, Vol 9, 83-91, Copyright © 1999 by Oxford University Press

ORIGINAL ARTICLES

Mouse C127 cells transfected with fucosyltransferase fuc-TIII express masked Lewisx but not Lewisx antigen

M Valli, A Bardoni and M Trinchera
Department of Biochemistry, University of Pavia, via Taramelli 3B, 27100 Pavia, Italy.

To study human alpha1,3/1,4fucosyltransferase (Fuc-TIII) as an alpha1,3 fucosyltransferase, we constructed two cell clones, C127-FT and C127-T- FT, by transfecting cDNA in parental (C127) or Polyoma T antigen expressing (C127-T) mouse cells, respectively. Both C127-FT and C127-T- FT clones express high levels of a fucosyltransferase activity kinetically similar to Fuc-TIII and an RNA that is amplified by a Fuc- TIII-specific oligonucleotide primer pair after reverse transcription. Clone C127-FT is Lewisxpositive, by flow cytometry, only after alpha- galactosidase or sialidase treatment, and releases [3H]Fuc N-glycans which efficiently bind to immobilized Griffonia simplicifolia I and Sambucus nigra lectins. Immunoblotting confirms that C127-FT glycoproteins acquire Lewisxreactivity only after specific deglycosylation, and shows that a small subset of Griffonia simplicifolia I isolectin B4reactive glycoproteins bears masked Lewisx, suggesting fine substrate recognition by Fuc-TIII. Moreover, transient transfection of H type alpha1, 2fucosyltransferase in clone C127-T-FT directs synthesis of Lewisyantigen, as detected by flow cytometry. Results indicate that Fuc-TIII expressed in C127 cells synthesizes masked Lewisxantigen while Lewisxantigen is not detectable.
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