Mehul B, Doyennette-Moyne M A, Aubery M, Mannherz H G, Codogno P
Unité 180 INSERM, Laboratoire de Biologie et Pathologie Moléculaires des Glycoprotéines, Paris, France.
Cell Biol Int Rep. 1990 Feb;14(2):155-64. doi: 10.1016/0309-1651(90)90032-t.
Previous studies have shown that 5'-nucleotidase, an ectoenzyme from chicken gizzard, interacts specifically with laminin and fibronectin, two glycoproteins of the extracellular matrix. Recently, we demonstrated that 5'-nucleotidase was involved in the spreading of chick embryo fibroblast on laminin. In the present communication, we report that a monoclonal antibody (CG37) raised-directed against 5'-nucleotidase inhibited the spreading of chick embryo myoblasts on laminin after their initial attachment to the substrate. Furthermore, monoclonal antibody CG37 specifically eluted 5'-nucleotidase from immobilized laminin and thus enabled its isolation from other myoblast laminin-binding proteins.