ADAM-13 - A NOVEL ADAM EXPRESSED IN SOMITIC MESODERM AND NEURAL CRESTCELLS DURING XENOPUS-LAEVIS DEVELOPMENT

Embryonic development involves a series of cell adhesive interactions that provide mechanical and instructive information required for morph ogenesis. The ADAMs family of membrane-anchored proteins, containing a disintegrin and metalloprotease domain, is well suited for participat ing in such developmental events. They encode not only a potential adh esive function, through an integrin-binding disintegrin domain, but al so a potential antiadhesive function, through a zinc-dependent metallo protease domain. In order to investigate the role of ADAMs in early de velopment we cloned a cDNA encoding a novel member of the ADAM family from a Xenopus laevis neurula stage library. We call this cDNA, and th e 915-amino-acid protein it encodes, ADAM 13. X-ADAM 13 RNA is express ed during embryogenesis from the midblastula stage through tadpole sta ge 45. X-ADAM 13 is localized to semitic mesoderm and cranial neural c rest cells during gastrulation, neurulation, and in tail bud stages. S equence analyses of the X-ADAM 13 metalloprotease and disintegrin doma ins indicate that the protein is likely to be involved in both proteol ytic and cell-adhesive functions. The X-ADAM 13 sequence is most close ly related to that of mouse meltrin alpha, which is implicated in myob last fusion. Our data suggest that X-ADAM. 13 may be involved in neura l crest cell adhesion and migration as well as myoblast differentiatio n. (C) 1997 Academic Press.