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Glycobiology Advance Access published online on October 23, 2003
Glycobiology, doi:10.1093/glycob/cwh018
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Submitted on July 30, 2003
Revised on October 2, 2003
Accepted on October 3, 2003

© 2003 Oxford University Press

ORIGINAL ARTICLES

Human galectin-1 recognition of poly-N-acetyllactosamine and chimeric polysaccharides

Sean R. Stowell 1, Marcelo Dias-Baruffi 2, Leena Penttilä 3, Ossi Renkonen 3, A. Kwame Nyame 1, and Richard D. Cummings 1*

1 Department of Biochemistry and Molecular Biology University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104; Oklahoma Center for Medical Glycobiology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104
2 School of Pharmaceutical Science of Ribeirão Preto-SP, University of São Paulo-Brazil, Av. do Café s/n - 14015-900
3 Haartman Institute, University of Helsinki, Helsinki, Finland

* To whom correspondence should be addressed. E-mail: richard-cummings{at}ouhsc.edu.

Abstract

Human galectin-1 is a dimeric carbohydrate binding protein (Gal-1) (subunit 14.6 kDa) widely expressed by many cells, but whose carbohydrate binding specificity is not well understood. Because of conflicting evidence regarding the ability of human Gal-1 to recognize N-acetyllactosamine (LN - Gal{beta}4GlcNAc) and poly-N-acetyllactosamine sequences (PL - [-3Gal{beta}4GlcNAc{beta}1-]n), we synthesized a number of neoglycoproteins containing galactose-, N-acetylgalactosamine, fucose, LN-, PL, and chimeric polysaccharides conjugated to bovine serum albumin (BSA). All neoglycoproteins were characterized by matrix-assisted laser desorption/ionization time-of-flight. Binding was determined in ELISA-type assays with immobilized neoglycoproteins and apparent binding affinities were estimated. For comparison, we also tested the binding of these neoglycoconjugates to Ricinus communis Agglutinin I, (RCA-I, a galactose binding lectin) and Lycopersicon esculentum agglutinin (LEA or tomato lectin), a PL-binding lectin. Gal-1 bound to immobilized Gal{beta}4GlcNAc{beta}3Gal{beta}4Glc-BSA with an apparent Kd of ~23 µM, but bound better to BSA conjugates with long PL and chimeric polysaccharide sequences (Kd's ranging from 11.9 ± 2.9 µM to 20.9 ±5.1 µM). By contrast, Gal-1 did not bind glycans lacking a terminal, non-reducing unmodified LN disaccharide and also bound very poorly to lactosyl-BSA (Gal{beta}4Glc-BSA). By contrast, RCA bound well to all glycans containing terminal, non-reducing Gal{beta}1-R, including lactosyl-BSA, and bound independently of the modification of the terminal, non-reducing LN or the presence of PL. LEA bound with increasing affinity to unmodified PL in proportion to chain length. Thus, Gal-1 binds terminal {beta}4Gal residues and its binding affinity is enhanced significantly by the presence of this determinant on long-chain PL or chimeric polysaccharides.


galectin, poly-N-acetyllactosamine, neoglycoprotein, human
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