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Published online
doi:10.1083/jcb.200709098
The Journal of Cell Biology, Vol. 180, No. 3, 451-458
The Rockefeller University Press, 0021-9525 $30.00
© Denecker et al.
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Mini-Review

Caspase-14 reveals its secrets



Geertrui Denecker1,2, Petra Ovaere1,2, Peter Vandenabeele1,2, and Wim Declercq1,2

1 Department for Molecular Biomedical Research, Flanders Institute for Biotechnology (VIB), 9052 Ghent, Belgium
2 Department of Molecular Biology, Ghent University, 9000 Ghent, Belgium

Correspondence to Peter Vandenabeele: Peter.vandenabeele{at}dmbr.ugent.be; or Wim Declercq: Wim.declercq{at}dmbr.ugent.be

Caspase-14 is a unique member of the evolutionarily conserved family of cysteinyl aspartate–specific proteinases, which are mainly involved in inflammation and apoptosis. However, recent evidence also implicates these proteases in proliferation and differentiation. Although most caspases are ubiquitously expressed, caspase-14 expression is confined mainly to cornifying epithelia, such as the skin. Moreover, caspase-14 activation correlates with cornification, indicating that it plays a role in terminal keratinocyte differentiation. The determination of in vitro conditions for caspase-14 activity paved the way to identifying its substrates. The recent development of caspase-14–deficient mice underscored its importance in the correct degradation of (pro)filaggrin and in the formation of the epidermal barrier that protects against dehydration and UVB radiation. Here, we review the current knowledge on caspase-14 in skin homeostasis and disease.

G. Denecker and P. Ovaere contributed equally to this paper.

Abbreviations used in this paper: AP-1, activator protein 1; EGCG, (–)-epigallocatechin-3-gallate.


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