Abstract
Although mutations in the filaggrin gene (FLG) have been shown to be associated with ichthyosis vulgaris and atopic dermatitis, the function and regulation of filaggrin remain incompletely understood. In this issue, Hoste et al. report that filaggrin is directly cleaved by caspase-14. Acting in concert with other proteases, caspase-14 controls the breakdown of filaggrin to free amino acids and amino acid derivatives that contribute to the hydration and UVB absorption capacity of the stratum corneum. These findings identify a new layer of complexity in the regulation of epidermal barrier function. © 2011 The Society for Investigative Dermatology.
Cite
CITATION STYLE
Eckhart, L., & Tschachler, E. (2011). Cuts by caspase-14 control the proteolysis of filaggrin. Journal of Investigative Dermatology. Nature Publishing Group. https://doi.org/10.1038/jid.2011.282
Register to see more suggestions
Mendeley helps you to discover research relevant for your work.