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J. Cell Biol.,
Volume 143, Number 6, December 14, 1998 1735-1747
3
1 with Laminin 5 Promotes Gap Junctional Communication




* Divisions of Basic Sciences and Public Health Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington 98109; Wounding of skin activates epidermal cell
migration over exposed dermal collagen and fibronectin and over laminin 5 secreted into the provisional
basement membrane. Gap junctional intercellular communication (GJIC) has been proposed to integrate the
individual motile cells into a synchronized colony. We
found that outgrowths of human keratinocytes in
wounds or epibole cultures display parallel changes in
the expression of laminin 5, integrin
Department of Pathobiology and § Division of Dermatology, University of Washington, Seattle, Washington 98105; and
Department of Vascular Biology, The Scripps Research Institute, La Jolla, California 92037
3
1, E-cadherin, and the gap junctional protein connexin 43. Adhesion
of keratinocytes on laminin 5, collagen, and fibronectin
was found to differentially regulate GJIC. When keratinocytes were adhered on laminin 5, both structural (assembly of connexin 43 in gap junctions) and functional (dye transfer) assays showed a two- to threefold increase compared with collagen and five- to eightfold
over fibronectin. Based on studies with immobilized integrin antibody and integrin-transfected Chinese hamster ovary cells, the interaction of integrin
3
1 with
laminin 5 was sufficient to promote GJIC. Mapping of
intermediate steps in the pathway linking
3
1-laminin
5 interactions to GJIC indicated that protein trafficking
and Rho signaling were both required. We suggest that
adhesion of epithelial cells to laminin 5 in the basement
membrane via
3
1 promotes GJIC that integrates individual cells into synchronized epiboles.
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