MOLECULAR-CLONING AND FUNCTIONAL EXPRESSION OF GICERIN, A NOVEL CELL-ADHESION MOLECULE THAT BINDS TO NEURITE OUTGROWTH FACTOR

Gicerin is an integral membrane glycoprotein of about 82 kd that is tr ansiently expressed in the developing CNS. Gicerin was first identifie d as a binding protein for neurite outgrowth factor (NOF), a member of the laminin family of extracellular matrix proteins. By isolating and sequencing a gicerin cDNA, we have found that this protein is a novel member of the immunoglobulin superfamily. The deduced protein (584 am ino acids) consists of five immunoglobulin-like loop structures in an extracellular domain, a single transmembrane region, and a short cytop lasmic tail. Cells transfected stably with gicerin cDNA adhered to NOF and aggregated with each other, indicating that gicerin exhibits both heterophilic and hemophilic adhesion activities.