Structure and chromosomal localization of the murine gene encoding GLYCAM 1. A mucin-like endothelial ligand for L selectin.

We recently described the molecular cloning of a murine cDNA encoding an endothelial cell surface ligand for the leukocyte adhesion molecule, L Selectin (Lasky, L. A., Singer, M., Dowbenko, D., Ima, Y., Henzel, W., Grimley, C., Gennie, C., Gillett, N., Watson, S., and Rosen, S. D (1992) Cell 69, 927-938). This glycoprotein ligand was found to resemble mucins in that it contained a large percentage of serine and threonine residues that were apparently O-glycosylated. At least one of the O-linked carbohydrates found on this endothelial ligand interacts with the lectin domain of L Selectin. These data suggest that this endothelial ligand is an adhesion molecule that accomplishes cell binding by presenting carbohydrate(s) to the lectin domain of L Selectin, and the name GLYCAM 1 (GLY-cosylation-dependent Cell Adhesion Molecule 1) has been proposed. In this paper we describe the genomic structure and chromosomal localization of this unique Selectin ligand. The gene has been found to be encoded on four separate exons, and it thus differs from the cell surface mucin leukosialin, whose coding region is contained on one exon, but is similar to glycophorin and CD34, other cell surface mucins whose genes are divided into multiple coding exons. While there is some correlation between exon division and protein domain structure, these relationships are not as clear as they are in other genes. The gene encoding GLYCAM 1 was found to map to murine chromosome 15.