Binding characteristics of N-acetylglucosamine-specific lectin of the isolated chicken hepatocytes: similarities to mammalian hepatic galactose/N-acetylgalactosamine-specific lectin

Abstract

Binding characteristics of N-acetylglucosamine- (GlcNAc) specific lectin on the chicken hepatocyte surface were probed by an inhibition assay using various sugars and glycosides as inhibitors. Results indicated that the binding area of the lectin is small, interacting only with GlcNAc residues whose 3- and 4-OH's are open. The combining site is probably of trough-type, since substitution with as large a group as monosaccharide is permitted on the C-6 side of GlcNAc, and on the C-1 side, the aglycon of GlcNAc can be very large (e.g., a glycoprotein). These binding characteristics are shared with the homologous mammalian lectin specific for galactose/N-acetylgalactosamine, suggesting that tertiary structure of the combining area of these two lectins is similar. This is understandable, since there is approximately 40% amino acid sequence identity in the carbohydrate recognition domain of these two lectins [Drickamer, K., Mannon, J. F., Binns, G., & Leung, J. O. (1984) J. Biol. Chem. 259, 770-778]. A series of glycosides, each containing two GlcNAc residues separated by different distances (from 0.8 to 4.7 nm), were synthesized. Inhibition assay with these and other cluster glycosides indicated that clustering of two or more GlcNAc residues increased the affinity toward the chicken lectin tremendously. Among the ligands containing two GlcNAc residues, the structure which allows a maximal inter-GlcNAc distance of 3.3 nm had the strongest affinity, its affinity increase over GlcNAc (monosaccharide) amounting to 100-fold. Longer distances slightly diminished the affinity, while shortening the distance caused substantial decrease in the affinity.(ABSTRACT TRUNCATED AT 250 WORDS)

Analysis of the molecular interaction of glycosylated proteins with rabbit liver asialoglycoprotein receptors using surface plasmon resonance spectroscopy

“…Since the chance of multivalent binding with liver ASGPRs is expected to be higher for highly galactosylated BSA, more energy would be required for dissociation. In addition, clustering effect of liver ASGPRs has been observed in the Triton-solubilized form as well as on the hepatocyte surface [16][17][18][19]. These findings would support the present results.…”

“…The association rate constants (k a ) of Gal-BSAs increased according to the number of galactose residues. As the number of 19 -, Gal 28 -, Gal 39 -, and Gal 48 -BSA, respectively). Thus, the association of galactosylated protein with liver ASGPRs appears to be a simple probabilistic process.…”

Enzyme‐assisted synthesis of a bivalent high‐affinity dodecasaccharide inhibitor of mouse gamete adhesion The length of the chains carrying distal α1,3‐bonded galactose residues is critical

“…[4] on sperm surface. The scribed enzymatic de novo synthesis of a 18-meric poly-Nnotion of multiple binding of oligosaccharide ligands to isoacetyllactosaminoglycan that contains four distal ~l,3-bonded lated lectin molecules and also to lectins on cell or virus surfaces galactose residues [8], and possesses considerable 'sperm recephas been put forward experimentally by several groups [23][24][25][26][27][28][29][30]. tor activity' (IC50 = 2.7/IM) [6].…”

Kinetics and the Mechanism of Interaction of the Endoplasmic Reticulum Chaperone, Calreticulin, with Monoglucosylated (Glc1Man9GlcNAc2) Substrate

“…In the latter, multivalency increases not only their binding affinities but also their specificities and physiological responses such as cell agglutination, mitogenicity, etc. (51)(52)(53)(54). A wealth of information on the affinities of plant lectin-saccharide/glycopeptide interaction is available, which in turn has been exploited for the isolation and the structural characterization of the latter by affinity chromatography (55)(56)(57).…”