Caspase 14

Caspase 14 is an enzyme that in humans is encoded by the CASP14 gene. Orthologs of this gene also exist in other mammals, such as sirenians and cetaceans, though they are inactivated in these two clades. Curiously, manatees, which are sirenians, retain some functional CASP14 genes.

CASP14
Identifiers
Aliases	CASP14, caspase 14, ARCI12
External IDs	OMIM: 605848; MGI: 1335092; HomoloGene: 36304; GeneCards: CASP14; OMA:CASP14 - orthologs
Gene location (Human) Chr. Chromosome 19 (human) Band 19p13.12 Start 15,049,480 bp End 15,058,293 bp
Gene location (Mouse) Chr. Chromosome 10 (mouse) Band 10|10 C1 Start 78,547,825 bp End 78,554,128 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in skin of abdomen skin of leg skin of arm vulva testicle vagina human penis skin of thigh tibialis anterior muscle mucosa of ileum Top expressed in lip esophagus skin of back umbilical cord skin of abdomen skin of external ear left colon sexually immature organism epidermis cornea More reference expression data BioGPS n/a
Gene ontology Molecular function peptidase activity cysteine-type endopeptidase activity cysteine-type peptidase activity protein binding hydrolase activity endopeptidase activity cysteine-type endopeptidase activity involved in execution phase of apoptosis cysteine-type endopeptidase activity involved in apoptotic process Cellular component cytoplasm keratin filament nucleus cytosol mitochondrion Biological process cornification cell differentiation keratinization proteolysis epidermis development execution phase of apoptosis apoptotic process intrinsic apoptotic signaling pathway in response to DNA damage Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 23581 12365 Ensembl ENSG00000105141 ENSMUSG00000005355 UniProt P31944 O89094 RefSeq (mRNA) NM_012114 NM_009809 RefSeq (protein) NP_036246 NP_033939 Location (UCSC) Chr 19: 15.05 – 15.06 Mb Chr 10: 78.55 – 78.55 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

The CASP14 gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This caspase has been shown to be processed and activated by caspase 8 and caspase 10 in vitro, and by anti-Fas agonist antibody or TNF-related apoptosis inducing ligand in vivo. The expression and processing of this caspase may be involved in keratinocyte terminal differentiation, which is important for the formation of the skin barrier.

According to the Human Protein Atlas, the CASP14 protein is enriched in human skin and mainly expressed in the upper layers of the epidermis. The protein is mainly localised to the cytosol according to the Cell Atlas.

See also

• The Proteolysis Map
• Caspase

Further reading

• Rasmussen HH, van Damme J, Puype M, et al. (1993). "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes". Electrophoresis. 13 (12): 960–9. doi:10.1002/elps.11501301199. PMID 1286667. S2CID 41855774.
• Ahmad M, Srinivasula SM, Hegde R, et al. (1998). "Identification and characterization of murine caspase-14, a new member of the caspase family". Cancer Res. 58 (22): 5201–5. PMID 9823333.
• Eckhart L, Ban J, Fischer H, Tschachler E (2000). "Caspase-14: analysis of gene structure and mRNA expression during keratinocyte differentiation". Biochem. Biophys. Res. Commun. 277 (3): 655–9. doi:10.1006/bbrc.2000.3698. PMID 11062009.
• Eckhart L, Declercq W, Ban J, et al. (2001). "Terminal differentiation of human keratinocytes and stratum corneum formation is associated with caspase-14 activation". J. Invest. Dermatol. 115 (6): 1148–51. doi:10.1046/j.1523-1747.2000.00205.x. PMID 11121154.
• Lippens S, Kockx M, Knaapen M, et al. (2001). "Epidermal differentiation does not involve the pro-apoptotic executioner caspases, but is associated with caspase-14 induction and processing". Cell Death Differ. 7 (12): 1218–24. doi:10.1038/sj.cdd.4400785. PMID 11175259.
• Pistritto G, Jost M, Srinivasula SM, et al. (2003). "Expression and transcriptional regulation of caspase-14 in simple and complex epithelia". Cell Death Differ. 9 (9): 995–1006. doi:10.1038/sj.cdd.4401061. PMID 12181750. S2CID 23933663.
• Chien AJ, Presland RB, Kuechle MK (2002). "Processing of native caspase-14 occurs at an atypical cleavage site in normal epidermal differentiation". Biochem. Biophys. Res. Commun. 296 (4): 911–7. doi:10.1016/S0006-291X(02)02015-6. PMID 12200134.
• Rendl M, Ban J, Mrass P, et al. (2003). "Caspase-14 expression by epidermal keratinocytes is regulated by retinoids in a differentiation-associated manner". J. Invest. Dermatol. 119 (5): 1150–5. doi:10.1046/j.1523-1747.2002.19532.x. PMID 12445205.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Lippens S, Kockx M, Denecker G, et al. (2004). "Vitamin D3 induces caspase-14 expression in psoriatic lesions and enhances caspase-14 processing in organotypic skin cultures". Am. J. Pathol. 165 (3): 833–41. doi:10.1016/s0002-9440(10)63346-9. PMC 1618612. PMID 15331408.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Walsh DS, Borke JL, Singh BB, et al. (2005). "Psoriasis is characterized by altered epidermal expression of caspase 14, a novel regulator of keratinocyte terminal differentiation and barrier formation". J. Dermatol. Sci. 37 (1): 61–3. doi:10.1016/j.jdermsci.2004.10.003. PMID 15619438.
• Koenig U, Sommergruber W, Lippens S (2005). "Aberrant expression of caspase-14 in epithelial tumors". Biochem. Biophys. Res. Commun. 335 (2): 309–13. doi:10.1016/j.bbrc.2005.07.072. PMID 16061209.
• Krajewska M, Kim H, Shin E, et al. (2006). "Tumor-associated alterations in caspase-14 expression in epithelial malignancies". Clin. Cancer Res. 11 (15): 5462–71. doi:10.1158/1078-0432.CCR-04-2527. PMID 16061862.
• Kam DW, Charles AK, Dharmarajan AM (2005). "Caspase-14 expression in the human placenta". Reprod. Biomed. Online. 11 (2): 236–43. doi:10.1016/S1472-6483(10)60964-9. PMID 16168224.
• Park K, Kuechle MK, Choe Y, et al. (2006). "Expression and characterization of constitutively active human caspase-14". Biochem. Biophys. Res. Commun. 347 (4): 941–8. doi:10.1016/j.bbrc.2006.06.156. PMID 16854378.
• White L, Dharmarajan A, Charles A (2007). "Caspase-14: a new player in cytotrophoblast differentiation". Reprod. Biomed. Online. 14 (3): 300–7. doi:10.1016/S1472-6483(10)60871-1. PMID 17359582.
• Hsu S, Qin H, Dickinson D, et al. (2007). "Expression of caspase-14 reduces tumorigenicity of skin cancer cells". In Vivo. 21 (2): 279–83. PMID 17436577.

External links

• The MEROPS online database for peptidases and their inhibitors: C14.018 Archived 2007-10-24 at the Wayback Machine