Abstract
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.
Highlights
Galectins are a family of carbohydrate-binding proteins that share a conserved sequence and affinity for -galactosides
In the course of studying mouse colon mRNA for galectin-4, we detected a related mRNA that encodes a new galectin that has two carbohydrate recognition domain (CRD) in a single peptide chain
Identification of Galectin-4 and Galectin-6 —To isolate mouse galectin-4 cDNA, we amplified a portion of cDNA prepared from mouse colon RNA by Polymerase Chain Reaction (PCR) using different pairs of primers designed on the basis of the sequence of rat galectin-4
Summary
Galectins are a family of carbohydrate-binding proteins that share a conserved sequence and affinity for -galactosides. When the galectin-6 probe was mixed with small intestinal RNA and digested with RNases, the size of the largest protected fragment was 335 nt (Fig. 4A, lane b), which is equal to the length of the galectin-6-specific sequence in this probe (Fig. 4B).
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