Targeted deletion of the sciellin gene resulted in normal development and maturation

Abstract

Summary: Sciellin, together with other precursor proteins, was cross-linked by transglutaminase 1 to form the cornified envelope, an essential component of the physical barrier of the epidermis and stratified squamous epithelia. To more fully understand the function of sciellin in cornified envelope formation, we generated sciellin null mice. The mice appeared normal in their development and maturation and there were no structural features that distinguished them from littermate controls. Isolated cornified envelopes appeared normal in structure and were not more fragile to mechanical stress. There was no evidence of decreased barrier function or altered expression of other cornified envelope components. Transgenic mice expressing the repeat domain appeared to have a normal phenotype, like the null, and did not alter endogenous sciellin expression. We conclude that sciellin null mice had no structural anomalies and the transgenic mice did not act as a dominant-negative mutation.

Transcriptional changes in organoculture of full‐thickness human skin following topical application of all‐trans retinoic acid

“…The specific function of this gene in human skin is not known to date, but deletion of this gene in mice did not affect normal barrier function 54.…”

Genome-Wide Expression Analysis of Human In Vivo Irritated Epidermis: Differential Profiles Induced by Sodium Lauryl Sulfate and Nonanoic Acid

“…Although the expressions of other claudins have been shown to be influenced by phorbol ester exposure to murine skin (Arabzadeh et al, 2008), expression of claudin 23 in skin was never previously reported. The expression of sciellin has not been described in any pathological skin conditions; in contrast, sciellin null mice have normal skin development and structure (Baden et al, 2005). Downregulation of SQLE indicates altered epidermal cholesterol biosynthesis.…”

Biomechanical stress induces novel arterial intima-enriched genes: implications for vascular adaptation to stress

“…Sciellin was initially characterized in a screen of antigens generated from human keratinocyte CE fragments as a highly insoluble CE precursor and transglutaminase substrate [40]. Subsequently, sciellin was shown to contain a proline-rich N-terminal domain, a central 16 repeat glutamine- and lysine-rich motif—the transglutaminase substrate—and a C-terminal LIM domain [13,15]. LIM domains, which are protein-interaction motifs, have been demonstrated in other proteins associated with the cytoskeleton and biomechanical stress in VSMCs [33,41].…”

“…Sciellin contains a core of conserved repeats and a unique proline-rich N-terminal domain that are proposed to serve a structural role. Furthermore, it possesses a C-terminal LIM domain that is believed to be a protein-interaction domain, possibly bestowing a scaffolding function on sciellin [13–15]. Periplakin, a member of the plakin family of proteins, is enriched in desmosomes where it acts as a mediator of intermediate filament assembly [16,17].…”