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JCS ePress online publication date 17 Aug 2004
doi: 10.1242/jcs.01310

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Research Article

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


Randy O. Sigle, Susana G. Gil, Mallar Bhattacharya, Maureen C. Ryan, Tai-Mei Yang, Tod A. Brown, Ariel Boutaud, Yuko Miyashita, John Olerud, and William G. Carter*
* Author for correspondence (e-mail: wcarter{at}fhcrc.org)

In epidermal wounds, precursor laminin 5 ({alpha}3{beta}3{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}3{beta}1 and {alpha}6{beta}4. 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.
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