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Expression and transcriptional regulation of caspase-14 in simple and complex epithelia
Journal article   Open access   Peer reviewed

Expression and transcriptional regulation of caspase-14 in simple and complex epithelia

G Pistritto, M Jost, S M Srinivasula, R Baffa, J-L Poyet, C Kari, Y Lazebnik, U Rodeck and E S Alnemri
Cell death and differentiation, v 9(9), pp 995-1006
Sep 2002
DOI: https://doi.org/10.1038/sj.cdd.4401061
PMID: 12181750
Featured in Collection :   UN Sustainable Development Goals @ Drexel
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https://doi.org/10.1038/sj.cdd.4401061View
Published, Version of Record (VoR) Open

Abstract

Epithelium - enzymology Humans Prostate - growth & development Male Epidermis - growth & development Promoter Regions, Genetic - genetics Cell Differentiation - genetics Genes, Regulator - genetics Antibody Specificity - immunology Epidermis - enzymology Caspase 14 Epithelial Cells - cytology Keratinocytes - enzymology Infant, Newborn Epithelium - growth & development Breast - cytology Breast - enzymology Caspases - genetics Cells, Cultured Breast - growth & development Keratinocytes - cytology Cell Compartmentation - physiology Extracellular Matrix - enzymology Cell Adhesion - physiology Gene Expression Regulation, Enzymologic - genetics Epithelial Cells - enzymology Prostate - cytology Cell Cycle - physiology Prostate - enzymology Epidermis - cytology
Caspase-14 is a recent addition to the caspase family of aspartate proteases involved in apoptotic processes. Human caspase-14 appears to be only weakly processed during apoptosis, and it does not cleave classical caspase substrates. Post partum, caspase-14 is prominently expressed by human keratinocytes and reportedly participates in terminal differentiation of complex epithelia. Here we provide evidence challenging the view that caspase-14 expression or processing is linked exclusively to terminal keratinocyte differentiation. We demonstrate that caspase-14 expression extended to multiple cell lines derived from simple epithelia of the breast, prostate, and stomach. In keratinocytes and breast epithelial cells, caspase-14 expression was upregulated in high-density cultures and during forced suspension culture. These effects were primarily due to transcriptional activation as indicated by reporter gene assays using a 2 kb caspase-14 promoter fragment. Importantly, caspase-14 was not cleaved during forced suspension culture of either cell type although this treatment induced caspase-dependent apoptosis (anoikis). Forced expression of caspase-14 in immortalized human keratinocytes had no effect on cell death in forced suspension nor was the transfected caspase-14 processed in this setting. In contrast to postconfluent and forced suspension culture, terminal differentiation of keratinocytes induced in vitro by Ca2+ treatment was not associated with increased caspase-14 expression or promoter activity. Our results indicate that (1) caspase-14 is expressed not only in complex but also simple epithelia; (2) cells derived from complex and simple epithelia upregulate caspase-14 expression in conditions of high cell density or lack of matrix interaction and; (3) in both cell types this phenomenon is due to transcriptional regulation.

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Collaboration types
Domestic collaboration
Web of Science research areas
Biochemistry & Molecular Biology
Cell Biology
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