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(American Journal of Pathology. 2004;164:2027-2038.)
© 2004 American Society for Investigative Pathology

Keratinocytes from Patients Lacking Collagen XVII Display a Migratory Phenotype

Kaisa Tasanen*{ddagger}, Lucy Tunggal{dagger}, Gretel Chometon{dagger}, Leena Bruckner-Tuderman{ddagger} and Monique Aumailley{dagger}

From the Department of Dermatology,* University of Oulu, Oulu, Finland; the Centers for Biochemistry and Molecular Medicine,{dagger} Medical Faculty, University of Cologne, Cologne, Germany; and the Department of Dermatology,{ddagger} University of Freiburg, Freiburg, Germany

Acquired or inherited junctional epidermolysis bullosa are skin diseases characterized by a separation between the epidermis and the dermis. In inherited nonlethal junctional epidermolysis bullosa, genetic analysis has identified mutations in the COL17A1 gene coding for the transmembrane collagen XVII whereas patients with acquired diseases have autoantibodies against this protein. This suggests that collagen XVII participates in the adhesion of basal keratinocytes to the extracellular matrix. To test this hypothesis, we studied the behavior of keratinocytes with null mutations in the COL17A1 gene. Initial adhesion of mutant cells to laminin 5 was comparable to controls and similarly dependent on {alpha}3ß1 integrins. The spreading of mutant cells was, however, enhanced, suggesting a propensity to migrate, which was confirmed by migration assays. In addition, laminin 5 deposited by collagen XVII-deficient keratinocytes was scattered and poorly organized, suggesting that correct integration of laminin 5 within the matrix requires collagen XVII. This assumption was supported by the co-distribution of the two proteins in the matrix of normal human keratinocytes and by protein-protein-binding assays showing that the C-terminus of collagen XVII binds to laminin 5. Together, the results unravel an unexpected role of collagen XVII in the regulation of keratinocyte migration.




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