A soluble beta-galactoside-binding lectin with subunit molecular weight of about 14,000 has been isolated from many vertebrate tissues. The lectin shows striking developmental regulation in certain tissues and has been detected on the surface of cells and in the extracellular matrix surounding them, suggesting possible roles in regulation of cellular development and in morphogenesis. Recent studies with the human form of this lectin indicate that there are several variants which are the products of distinct genes. These findings raise the possibility that these, like other lectins, may have a second functional domain distinct from their carbohydrate binding sites. They also raise the possibility that these structural variations mediate specificity in glycoconjugate binding. The purpose of this project is to further characterize this gene family in humans, with the ultimate aim of understanding its regulation and functions. To this end, a series of full length human cDNAs will be isolated and sequenced. The human genomic DNAs encoding members of this gene family will also be isolated and sequenced.
