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© The Rockefeller University Press, 0021-9525/1997//719 $5.00
The Journal of Cell Biology, Volume 138, Number 3, , 1997 719-728

Article

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



Patricia Rousselle*, Douglas R. Keene||, Florence Ruggiero*, Marie-France Champliaud{ddagger}, Michel van der Rest§, and Robert E. Burgeson{ddagger}

* 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; {ddagger} 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 || 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}3β3{gamma}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}6β4. 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}3β1{gamma}1) has no detectable affinity for type VII collagen NC-1, indicating that the binding is mediated by the β3 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}3β2{gamma}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}6β4 with type VII collagen, and the laminin 5–6/7 complexes are present within the interhemidesmosomal spaces bound at least by integrin {alpha}3β1 where they may mediate basement membrane assembly or stability, but contribute less significantly to epithelial friction resistance.

Abbreviations used in this paper: NHK, normal human keratinocytes; pAb, polyclonal antibody; SCC, squamous carcinoma cells.

Part of this work was supported by a grant (3056) from the Association pour la Recherche sur le Cancer (to P. Rousselle); from a Fondation René Touraine pour la Recherche en Dermatologie award (to P. Rouselle); a Journal of Cell Science Traveling Fellowship to P. Rouselle, U.S. Public Health Service grants AR35689 and AR38923 (R.E. Burgeson); and from the Cutaneous Biology Research Center, Massachusetts General Hospital.

Please address all correspondence to Robert E. Burgeson, Ph.D., MGH-East-CBRC, Building 149, 13th Street, Charlestown, MA 02129. Tel.: (617) 726-4186. Fax: (617) 726-4187. e-mail: BBurgeson{at}CBRC.MGH.Harvard.edu


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