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Glycobiology Advance Access originally published online on December 23, 2003
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Glycobiology vol 14 no 3 pp. 293-300, 2004
Glycobiology vol. 14 no. 3 © Oxford University Press 2004; all rights reserved.

Quaternary solution structures of galectins-1, -3, and -7

Stephanie Morris2,3, Nisar Ahmad4, Sabine André5, Herbert Kaltner5, Hans-J. Gabius5, Michael Brenowitz1,2 and Fred Brewer1,4

2 Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461; 3 Laboratory for Macromolecular Analysis & Proteomics, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461; 4 Department of Molecular Pharmacology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461; and 5 Institut fur Physiologische Chemie, Ludwig-Maximilians Universitat Munchen, 80539 Munchen, Germany

Received on October 2, 2003; accepted on November 3, 2003

Galectins are a growing family of animal lectins with functions in growth regulation and cell adhesion that bind ß-Gal residues in oligosaccharides. Evidence indicates that some of the biological properties of galectins are due to their cross-linking activities with multivalent glycoconjugate receptors. Therefore determination of the quaternary solution structures of these proteins is important in understanding their structure–function properties. The present study reports analytical sedimentation velocity and equilibrium data for galectins-1, -3, and -7 in the absence and presence of bound LacNAc, the natural ligand epitope. Galectin-1 from bovine heart and recombinant human galectin-7 were found to be stable dimers by both methods. In contrast, recombinant murine galectin-3, as well as its proteolytical derived C-terminal domain, are predominantly monomeric. The presence of LacNAc at concentrations sufficient to fully saturate the proteins had no significant effect on either the weight average molecular weight determined by sedimentation equilibrium or the hydrodynamic properties determined from sedimentation velocity experiments. These results show that binding of a monovalent ligand does not affect oligomerization of these galectins.

1 To whom correspondence should be addressed; e-mail: brewer{at}aecom.yu.edu


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