1528 Structural disruption of collagen XVII/BP180 decelerates the cutaneous wound closure in mice

Collagen XVII (ColXVII, also known as BP180, BPAg2) is a constituent of hemidesmosomes that bind epidermis to underlying layers the skin. It type II transmembrane protein with 15 extracellular collagenous domains. Juxtamembraneous non-collagenous 16th A domain (NC16A) in human ColXVII target for cleavage proteases shed from cell surface during keratinocyte migration and differentiation. The important collagen triple helix formation. ΔNC14A mice have an exon 18 deletion inCol17a1 gene leading absence 14th (NC14A) ColXVII, corresponding NC16A. We studied role NC14A on structure function ColXVII. disrupts trimerization found trimers ectodomain but only minority full-length skin mice. level was decreased whereas levels other hemidesmosomal proteins were comparable wild-type In vitro, primary keratinocytes showed slower scratch wound vivo, closure full-thickness dorsal wounds decelerated compared wounds. Immunostainings localized membranes basal uninjured epidermal tongue mainly intracellular while it membranes. majority calcium-induced differentiation increased targeting ER Our results support previous findings migration. essential domains lack trimeric associated open wound.