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J Biol Chem, Vol. 273, Issue 5, 2954-2960, January 30, 1998

Galectin-4 and Galectin-6 Are Two Closely Related Lectins Expressed in Mouse Gastrointestinal Tract

Michael A. GittDagger , Céline Colnot, Françoise Poirier, Kathryn J. NaniDagger , Samuel H. BarondesDagger , and Hakon LefflerDagger par

From the Dagger  Center for Neurobiology and Psychiatry, Department of Psychiatry and par  Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94143-0984 and the  Institut Cochin de Genetique Moleculaire, Unite INSERM 257, 24 rue de Faubourg Saint-Jaques, 75014 Paris, France

Galectins are a family of carbohydrate-binding proteins that share a conserved sequence and affinity for beta -galactosides. Some, such as galectin-1, are isolated as dimers and have a single carbohydrate recognition domain (CRD) in each monomer, whereas others, such as galectin-4, are isolated as monomers and have two CRDs in a single polypeptide chain. In the course of studying mouse colon mRNA for galectin-4, we detected a related mRNA that encodes a new galectin that also has two CRDs in a single peptide chain. The new galectin, galectin-6, lacks a 24-amino acid stretch in the link region between the two CRDs that is present in galectin-4. Otherwise, these two galectins have 83% amino acid identity. Expression of both galectin-4 and galectin-6 is confined to the epithelial cells of the embryonic and adult gastrointestinal tract. Galectin-4 is expressed at about equal levels in colon and small intestine but much less in stomach, whereas galectin-6 is expressed at about equal levels throughout the gastrointestinal tract.


Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.



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