Am. Wu et al., Forssman pentasaccharide and polyvalent Ga1 beta 1 -> 4GlcNAc as major ligands with affinity for Caragana arborescens agglutinin, FEBS LETTER, 463(3), 1999, pp. 225-230
The binding properties of Caragana arborescens agglutinin (CAA, pea tree ag
glutinin) were studied by enzyme linked lectinosorbent assay (ELLSA) and by
inhibition of CAA-glycan interaction. Among glycoproteins (gps) tested, CA
A reacted strongly with asialo bird nest gp, asialo rat sublingual gp, huma
n Tamm-Horsfall Sd(a(+)) urinary gp (THGP) and asialo THGP that are rich in
GalNAc alpha 1-->, GalNAc beta 1--> and/or Gal beta 1 --> 4GlcNAc residues
. CAA also bound tightly with multivalent Gal beta 1 --> 4GlcNAc (mII) cont
aining glycoproteins (human blood group precursor gps, asialo fetuin) and a
sialo ovine salivary glycoprotein (Tn, GalNAc alpha 1 --> Ser/Thr) but CAA
reacted poorly of not at all with sialylated glycoproteins tested, Of the s
ugars tested for inhibition of binding, Forssman pentasaccharide (F-p, GalN
Ac alpha 1 --> 3GalNAc beta 1 --> 3Gal alpha 1 --> 4Gal beta 1 --> 4Glc) wa
s the best, It nas about 2.3, 9.5 and 52.6 times more active than Gal beta
1 --> 4GlcNAc, GalNAc and Gal, respectively, and about 1.9 times more activ
e than tri-antennary Gal beta 1 --> 4GlcNAc (Tri-II), These results suggest
that this agglutinin is mainly specific for F-p, mil and Tn clusters. This
property can be used to detect human abnormal glycotopes related to F-p an
d unmasked mII/Tn clusters and to study cell growth and differentiation giv
en the lack of toxicity of this lectin toward mouse fibroblast cells, (C) 1
999 Federation of European Biochemical Societies.