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J. Cell Biol.
© The Rockefeller University Press
0021-9525/97/08/719/10 $2.00
Volume 138, Number 3, August 11, 1997 719-728

Laminin 5 Binds the NC-1 Domain of Type VII Collagen

Patricia Rousselle,* Douglas R. Keene,par Florence Ruggiero,* Marie-France Champliaud,Dagger Michel van der Rest,§ and Robert E. BurgesonDagger

* Institut de Biologie et Chimie des Protéines, Unité Propre de Recherche 412 du Centre National de la Recherche Scientifique, associée à l'Université Lyon I, 69367 Lyon Cedex 07, France; Dagger  The Cutaneous Biology Research Center, Massachusetts General Hospital and Harvard Medical School, Charlestown, Massachusetts 02129; § Institut de Biologie Structurale, J.P. Ebel, Grenoble CEDEX 38027, France; and par  Shriners Hospital for Children, Portland, Oregon 97201

Mutational analyses of genes that encode components of the anchoring complex underlying the basolateral surface of external epithelia indicate that this structure is the major element providing for resistance to external friction. Ultrastructurally, laminin 5 (alpha 3beta 3gamma 2; a component of the anchoring filament) appears as a thin filament bridging the hemidesmosome with the anchoring fibrils. Laminin 5 binds the cell surface through hemidesmosomal integrin alpha 6beta 4. However, the interaction of laminin 5 with the anchoring fibril (type VII collagen) has not been elucidated. In this study we demonstrate that monomeric laminin 5 binds the NH2-terminal NC-1 domain of type VII collagen. The binding is dependent upon the native conformation of both laminin 5 and type VII collagen NC-1. Laminin 6 (alpha 3beta 1gamma 1) has no detectable affinity for type VII collagen NC-1, indicating that the binding is mediated by the beta 3 and/or gamma 2 chains of laminin 5. Approximately half of the laminin 5 solubilized from human amnion or skin is covalently complexed with laminins 6 or 7 (alpha 3beta 2gamma 1). The adduction occurs between the NH2 terminus of laminin 5 and the branch point of the short arms of laminins 6 or 7. The results are consistent with the presumed orientation of laminin 5, having the COOH-terminal G domain apposed to the hemidesmosomal integrin, and the NH2-terminal domains within the lamina densa. The results also support a model predicting that monomeric laminin 5 constitutes the anchoring filaments and bridges integrin alpha 6beta 4 with type VII collagen, and the laminin 5-6/7 complexes are present within the interhemidesmosomal spaces bound at least by integrin alpha 3beta 1 where they may mediate basement membrane assembly or stability, but contribute less significantly to epithelial friction resistance.


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