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Proteolytic fragments of the laminin \u03b32 chain stimulate migration and scattering of keratinocytes and cancer cells. Sulfur mustard (SM) is a bifunctional alkylating agent that induces separation of basal keratinocytes from the dermal\u2010epidermal junction and invokes a strong inflammatory response leading to delayed wound repair. In the present studies, the role of laminin \u03b32 in SM\u2010induced skin injury and wound repair was investigated using the mouse ear vesicant model. We found that laminin \u03b32 chain mRNA was preferentially upregulated in mouse ear skin exposed to SM. <jats:italic>In situ<\/jats:italic> hybridization confirmed overexpression of laminin \u03b32 transcript. Western blot analysis showed increased protein expression of the full\u2010length proform of laminin \u03b32 and smaller processed fragments of laminin \u03b32 in skin exposed to SM. Dual immunofluorescence labeling indicated that laminin \u03b32 fragments are prevalent in suprabasal keratinocytes behind the leading edge in areas of hyperplasia in injured skin. In addition, co\u2010expression of laminin \u03b32 and the senescent marker, p16<jats:sup>\u2212INK4a<\/jats:sup> was found to overlap with the hyperplastic migratory epithelial sheet. This observation is similar to hypermotile keratinocytes reported in invasive carcinoma cells. Overall, our studies indicate that laminin \u03b32 is preferentially expressed in skin post SM exposure and that protein expression appears to become progressively more fragmented. The laminin \u03b32 fragments may play a role in regulating SM\u2010induced skin wound repair. 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