Ma. Gitt et al., GALECTIN-4 AND GALECTIN-6 ARE 2 CLOSELY-RELATED LECTINS EXPRESSED IN MOUSE GASTROINTESTINAL-TRACT, The Journal of biological chemistry, 273(5), 1998, pp. 2954-2960
Galectins are a family of carbohydrate-binding proteins that share a c
onserved sequence and affinity for beta-galactosides. Some, such as ga
lectin-1, are isolated as dimers and have a single carbohydrate recogn
ition domain (CRD) in each monomer, whereas others, such as galectin-4
, are isolated as monomers and have two CRDs in a single polypeptide c
hain. In the course of studying mouse colon mRNA for galectin-4, we de
tected a related mRNA that encodes a new galectin that also has two CR
Ds 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 pr
esent in galectin-4. Otherwise, these two galectins have 83% amino aci
d identity. Expression of both galectin-4 and galectin-6 is confined t
o the epithelial cells of the embryonic and adult gastrointestinal tra
ct. Galectin-4 is expressed at about equal levels in colon and small i
ntestine but much less in stomach, whereas galectin-6 is expressed at
about equal levels throughout the gastrointestinal tract.