Agglutination of murine and guinea pig peritoneal cells by α‐L‐fucose‐binding lectin: Evonymus europaea

Abstract

Among lectins from Lotus tetragonolobus, Ulex europaeus I and Evonymus europaea, agglutinating cells with blood group H determinants containing L-fucose alpha 1 leads to 2-linked to subterminal D-galactose, only the last lectin agglutinates thioglycolate- and paraffin oil-stimulated murine and guinea pig peritoneal exudate cells (PEC). The agglutination is inhibited by specific inhibitors of Evonymus lectin only: lacto-N-fucopentaose I and lactose. These results suggest the presence of a determinant on the surface of PEC, containing L-fucose alpha 1-linked at the nonreducing end which is different from blood group H determinants. Nonstimulated murine peritoneal cells (PC) are not agglutinated by the lectin but become agglutinable after neuraminidase treatment. Unstimulated guinea pig PC from different animals are agglutinated to a different extent by the same lectin concentration and show increased agglutinability after neuraminidase digestion. These results show that receptor for Evonymus lectin also exists on the nonstimulated PC but access to it is hindered by sialic acid. Trypsin- and pronase-digested PEC show increased agglutinability with Evonymus lectin. These results suggest that the lectin receptor is a glycolipid. Since alpha-linked L-fucose has been suggested as a part of the macrophage receptor for migration inhibitory factor in the guinea pig (Remold, J. Exp. Med. 1973. 138: 1065), the effect of Evonymus europaea lectin on the migration of PEC was studied. It was found that lectin inhibits the migration of PEC in the capillary tube assay up to 80%.

Temporal changes in the carbohydrates expressed on BG01 human embryonic stem cells during differentiation as embryoid bodies

“…However, AAA (freshwater eel agglutinin) bound neither 12-nor 28-day EBs, suggesting the absence of Fuc α1,3 GlcNAc (glycan array). UEA 1 specifically binds to α1,2-linked fucose ( [4,[21][22][23], glycan array) and the presence of this epitope appears to increase with differentiation, since UEA1 bound to only 15% of undifferentiated cells, but bound to 70 and 80% of 12-and 28-day EBs, respectively. Lotus lectin, which binds most preferentially to terminal α1,2-linked fucosyl groups when a subterminal α1,3 fucose is also present ( [24], glycan array), did not bind to 12-day EBs, but bound readily to 28-day EBs.…”

“…This lectin binds most preferentially to Gal α1,3 (Fuc α1,2) Gal β1,3 GlcNAc ([23], glycan array); however, this epitope cannot be present because terminal α-Gal was shown to be absent. EEA1 also binds weakly to Gal β1,4 (Fuc α1,3) Glc/GlcNAc (glycan array) or terminal α1,2-linked fucose [22,23], one of which must be the case here. The specificity data given here and in Table 7 was analyzed by a glycan array.…”

Both cell-surface carbohydrates and protein tyrosine phosphatase are involved in the differentiation of astrocytes in vitro

“…It is noteworthy that neither ABA nor DBA, both of which bind to the typical O-linked oligosaccharide (Kaifu and Osawa, 1979;Baker et al, 1983), Gal␤133GalNAc, induced astrocyte stellation at all. The ␣-fucose-binding lectin (Allen et al, 1977;Petryniak et al, 1983), LTA, also did not induce astrocyte stellation. MAL and E-PHA showed a much weaker activity of inducing stellation of astrocytes than DSA, suggesting that Sia␣233Gal(GalNAc) linkage and/or bisecting GlcNAc residues (Irimura et al, 1981;Cummings and Kornfeld, 1982) in the glycans may be partially effective.…”

Inhibition of proliferation and induction of differentiation of glioma cells with Datura stramonium agglutinin

“…It is noteworthy that DBA, which binds to core 1 O-linked oligosaccharide (Galb1?3GalNAc) (Baker et al, 1983), did not inhibit proliferation at all. LTA, a fucose-binding lectin (Allen et al, 1977;Petryniak et al, 1983), also did not inhibit proliferation. Since SSA showed only a small effect on C6 proliferation, glycans containing the Siaa2?6 group may not be effective (Shibuya et al, 1989).…”