Observations of skin grafts derived from keratinocytes expressing selectively engineered mutant laminin-332 molecules.
Observations of skin grafts derived from keratinocytes expressing selectively engineered mutant laminin-332 molecules.
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对表达选择性工程突变层粘连蛋白 332 分子的角质形成细胞衍生的皮肤移植物的观察。
DOI：
10.1038/jid.2010.85
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发表时间：
2010
期刊：
影响因子：
--
通讯作者：
Marinkovich,MPeter
中科院分区：
文献类型：
--
作者：
Sakai,Noriyasu;Waterman,ElizabethA;Nguyen,NgonT;Keene,DouglasR;Marinkovich,MPeter
Laminin-332 is a large extracellular basement membrane zone protein that is critical for dermal–epidermal cohesion. The laminin-332 heterotrimer (α3/β3/γ2) is believed to link keratinocytes with the basement membrane zone by simultaneously binding epidermal integrin receptors via the C-terminal globular domain of its α3 chain, and type VII collagen through domains on the short arm of its β3 chain (Chen et al., 1997; Rousselle et al., 1997). Antibodyinduced inhibition of laminin-332’s integrin-binding domains produces extensive skin blistering (Rousselle et al., 1991; Kirtschig et al., 1995); however, the in vivo significance of the laminin β3 short arm in dermal–epidermal cohesion has not been tested directly.To further study the laminin β3 short arm in dermal–epidermal cohesion, we produced two deletion mutants of the laminin β3 cDNA. One (ΔVI) contained a deletion of domain VI (LN) but left the type VII collagen-binding domain intact. The other contained a deletion of the entire β3 short arm I comprising domains VI and V-III (LN, LE, LF), which includes the collagenbinding region (ΔVI-III). Mutant and wild-type (WT) β3 chain cDNAs were retrovirally expressed in laminin β3 null junctional epidermolysis bullosa (JEB Null) primary keratinocytes
