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

Pistritto, G., Jost, M., Srinivasula, S. M., Baffa, R., Poyet, J. L., Kari, C., Lazebnik, Y., Rodeck, U., Alnemri, E. S. (2002) Expression and transcriptional regulation of caspase-14 in simple and complex epithelia. Cell Death and Differentiation, 9 (9). pp. 995-991006. ISSN 1350-9047

URL: http://www.ncbi.nlm.nih.gov/pubmed/12181750
DOI: 10.1038/sj.cdd.4401061

Abstract

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.

Item Type: Paper
Uncontrolled Keywords: Antibody Specificity Breast Caspase 14 Caspases Cell Adhesion Cell Compartmentation Cell Cycle Cell Differentiation Cells, Cultured Epidermis Epithelial Cells Epithelium Extracellular Matrix Gene Expression Regulation, Enzymologic Genes, Regulator Humans Infant, Newborn Keratinocytes Male Promoter Regions, Genetic Prostate
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > transcription
organs, tissues, organelles, cell types and functions > cell types and functions > cell functions > apoptosis
organs, tissues, organelles, cell types and functions > tissues types and functions > epithelia
organs, tissues, organelles, cell types and functions > tissues types and functions
CSHL Authors:
Communities: CSHL labs > Labeznik lab
Depositing User: Matt Covey
Date: 2002
Date Deposited: 12 Dec 2012 17:30
Last Modified: 12 Dec 2012 17:30
Related URLs:
URI: https://repository.cshl.edu/id/eprint/26379

Actions (login required)

Administrator's edit/view item Administrator's edit/view item
CSHL HomeAbout CSHLResearchEducationNews & FeaturesCampus & Public EventsCareersGiving