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First published online 17 August 2004
doi: 10.1242/jcs.01310

Journal of Cell Science 117, 4481-4494 (2004)
Published by The Company of Biologists 2004
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Research Article

Globular domains 4/5 of the laminin {alpha}3 chain mediate deposition of precursor laminin 5

Randy O. Sigle1, Susana G. Gil1, Mallar Bhattacharya2, Maureen C. Ryan1,*, Tai-Mei Yang1, Tod A. Brown1, Ariel Boutaud4, Yuko Miyashita2, John Olerud2 and William G. Carter1,3,{ddagger}

1 Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue, Seattle, WA 98109, USA
2 Department of Medicince (Dermatology), University of Washington, 1959 N.E. Pacific St, Seattle, WA 98195, USA
3 Department of Pathobiology, University of Washington, 1959 N.E. Pacific St, Seattle, WA 98195, USA
4 BioStratum Incorporated, 4620 Creekstone Drive, Suite 200, Durham, NC 27703, USA

{ddagger} Author for correspondence (e-mail: wcarter{at}fhcrc.org)

Accepted 12 May 2004

In epidermal wounds, precursor laminin 5 ({alpha}3ß3{gamma}2) is deposited in the provisional basement membrane (PBM) before other BM components. Precursor laminin 5 contains G4/5 globular domains at the carboxyl terminus of the {alpha}3 chain. Here, the function of G4/5 was evaluated in deposition of laminin 5. Soluble laminin 5, secreted by keratinocytes in culture, is cleaved by an endogenous protease releasing G4/5. Thrombin, a serum protease, cleaves G4/5 indistinguishably from endogenous protease. Soluble human precursor laminin 5, but not cleaved laminin 5, was bound and deposited by mouse keratinocytes null for mouse {alpha}3 chain ({alpha}3–/– MKs). The deposition rescued adhesion and spreading and survival. In a model for PBM assembly, precursor laminin 5 was deposited along fibronectin fibrils at the junction between co-cultures of keratinocytes and fibroblasts. In both models, the deposition of precursor laminin 5 was inhibited by removal of G4/5 with thrombin. To confirm that G4/5 participates in deposition, the human LAMA3A gene was modified to produce {alpha}3 chains either without or with G4/5 that cannot be cleaved. Both precleaved and noncleavable {alpha}3 isoforms were expressed in {alpha}3–/– MKs, where they deposited sufficiently to rescue adhesion via integrins {alpha}3ß1 and {alpha}6ß4. Despite this similarity, noncleavable laminin 5 was at least threefold more efficiently deposited than precleaved isoform. We conclude that the G4/5 domain in the {alpha}3 chain facilitates deposition of precursor laminin 5 into the PBM in epidermal wounds.

Key words: Laminin 5, Adhesion, Basement membrane assembly, Extracellular matrix




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