KEY WORDS: entactin /nidogen, laminin, gene expression, morphogenesis, chick embryoLaminin and entactin/nidogen are major glycoproteins of the extracellular matrix, including the basement membranes and of embryonic tissues. The prototype of laminin consists of three distinct polypeptide chains designated as α1 (400 kDa), β1 (210 kDa) and γ1 (210 kDa) (Chung et al., 1979; review Zagris, 2001). Several genetically different isoforms as well as spliced products of the chains have been identified giving rise to various classes of laminin with distinct tissue distributions and co-distributions, unique properties and developmentally regulated expression. Entactin (150 kDa) (Carlin et al., 1981), also referred to as nidogen, is a small rodshaped molecule with three globular domains (G1, G2, G3) connected by a flexible link and a rod. The entactin carboxyl globular domain G3 binds to laminin on the γ1 chain, the G2 domain binds to the protein core of perlecan, the N-terminal domain of fibronectin and fibrinogen and to collagen IV and the molecule serves as a link between laminin and collagen IV networks (review Miosge et al., 2000). This raised the question whether competition for binding to the entactin G2 domain may provide a mechanism for modifying Int.