Volume 52 (12): 1561-1574, 2004 Copyright ©The Histochemical Society, Inc. Ultrastructural Localization of Caspase-14 in Human Epidermis
Dipartimento di Biologia Evoluzionistica Sperimentale, University of Bologna, Bologna, Italy (LA); Department of Dermatology, Medical University of Vienna, Vienna, Austria (MD,CR,ET,LE); and Centre de Recherches et d'Investigations Epidermiques et Sensorielles (CE.R.I.E.S.), Neuilly, France (ET) Correspondence to: Lorenzo Alibardi, Dept. of Biology, University of Bologna, via Selmi 3, 40126 Bologna, Italy. E-mail: Alibardi{at}biblio.cib.unibo.it Caspase-14 has been implicated in the formation of stratum corneum because of its specific expression and activation in terminally differentiating keratinocytes. However, its precise physiological role and its protein substrate are elusive. We studied the ultrastructural localization of caspase-14 in human epidermis to compare its distribution pattern with that of well-characterized differentiation markers. Immunogold cytochemistry confirmed that caspase-14 is nearly absent in basal and spinous layers. In the granular, layer nuclei and keratohyalin granules were labeled with increasing intensity towards the transitional layer. Particularly strong caspase-14 labeling was associated with areas known to be occupied by involucrin and loricrin, whereas F-granules, occupied by profilaggrin/filaggrin, were much less labeled. A high density of gold particles was also present at the forming cornified cell envelope, including desmosomes. In corneocytes, intense labeling was both cytoplasmic and associated with nuclear remnants and corneodesmosomes. These observations will allow focusing efforts of biochemical substrate screening on a subset of proteins localizing to distinct compartments of terminally differentiated keratinocytes. (J Histochem Cytochem 52:15611574, 2004)
Key Words: human epidermis cornification caspase-14 ultrastructural immunocytochemistry
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