Mycophenolic acid does not inhibit protein glycosylation in T lymphocytes

Background: Mycophenolic acid inhibits guanosine nucleotide synthesis and h as been shown to be a potent inhibitor of lymphocyte proliferation as well as being effective at decreasing the incidence of graft rejection. Guanosin e nucleosides are essential for protein glycosylation and many cell surface proteins including adhesion molecules, which are important for graft infil tration and rejection, are glycoproteins. There have been conflicting repor ts concerning the ability of MPA to interfere with glycosylation in lymphoi d cells. Therefore, the purpose of this study was to investigate the effect s of MPA on cell surface protein glycosylation in lymphoid cells. Methods: Cells were cultured in the presence of increasing concentrations of MPA for different lengths of time and stained with fluorescent-labelled lectins sp ecific for either mannose or fucose residues on glycoproteins. Analysis was then performed by flow cytometry. Results: MPA treatment had no effect on the binding of either fucose or mannose-specific lectins to Con A stimulate d human PBLs and rat lymph node lymphocytes or to a CEMC7a T cell line. Con clusion: The results show that, contrary to previous reports, MPA does not affect cell surface glycosylation in T cells using T cells from different s ources of both human and non-human origin. (C) 2000 Elsevier Science B.V. A ll rights reserved.