CASP12 (gene)

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Identifiers
Aliases
External IDs	GeneCards: [1]
Orthologs
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a
Wikidata
View/Edit Human

Caspase 12 (gene/pseudogene) is a protein that in humans is encoded by the CASP12 gene.

Function

Caspases are cysteine proteases that cleave C-terminal aspartic acid residues on their substrate molecules. This gene is most highly related to members of the ICE subfamily of caspases that process inflammatory cytokines. In rodents, the homolog of this gene mediates apoptosis in response to endoplasmic reticulum stress. However, in humans this gene contains a polymorphism for the presence or absence of a premature stop codon. The majority of human individuals have the premature stop codon and produce a truncated non-functional protein. The read-through codon occurs primarily in individuals of African descent and carriers have endotoxin hypo-responsiveness and an increased susceptibility to severe sepsis. Several alternatively spliced transcript variants have been noted for this gene. [provided by RefSeq, Feb 2011].

Further reading

• Fischer H, Koenig U, Eckhart L, Tschachler E (May 2002). "Human caspase 12 has acquired deleterious mutations". Biochem. Biophys. Res. Commun. 293 (2): 722–6. doi:10.1016/S0006-291X(02)00289-9. PMID 12054529.
• Hetz C, Russelakis-Carneiro M, Maundrell K, Castilla J, Soto C (October 2003). "Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein". EMBO J. 22 (20): 5435–45. doi:10.1093/emboj/cdg537. PMC 213791. PMID 14532116.
• Díaz-Horta O, Van Eylen F, Herchuelz A (December 2003). "Na/Ca exchanger overexpression induces endoplasmic reticulum stress, caspase-12 release, and apoptosis". Ann. N. Y. Acad. Sci. 1010: 430–2. PMID 15033764.
• Saleh M, Vaillancourt JP, Graham RK, Huyck M, Srinivasula SM, Alnemri ES, Steinberg MH, Nolan V, Baldwin CT, Hotchkiss RS, Buchman TG, Zehnbauer BA, Hayden MR, Farrer LA, Roy S, Nicholson DW (May 2004). "Differential modulation of endotoxin responsiveness by human caspase-12 polymorphisms". Nature. 429 (6987): 75–9. doi:10.1038/nature02451. PMID 15129283.
• Kachapati K, O'Brien TR, Bergeron J, Zhang M, Dean M (September 2006). "Population distribution of the functional caspase-12 allele". Hum. Mutat. 27 (9): 975. doi:10.1002/humu.9448. PMID 16917906.
• Zhao X, Sun Y, Yu H, Ye L, Zhang L, Lu J, Yuan Y, Qian G, Ge S (August 2007). "Apoptosis induced by BIK was decreased with RNA interference of caspase-12". Biochem. Biophys. Res. Commun. 359 (4): 896–901. doi:10.1016/j.bbrc.2007.05.175. PMID 17574210.
• Roy S, Sharom JR, Houde C, Loisel TP, Vaillancourt JP, Shao W, Saleh M, Nicholson DW (March 2008). "Confinement of caspase-12 proteolytic activity to autoprocessing". Proc. Natl. Acad. Sci. U.S.A. 105 (11): 4133–8. doi:10.1073/pnas.0706658105. PMC 2393782. PMID 18332441.
• Bian ZM, Elner SG, Elner VM (December 2008). "Regulated expression of caspase-12 gene in human retinal pigment epithelial cells suggests its immunomodulating role". Invest. Ophthalmol. Vis. Sci. 49 (12): 5593–601. doi:10.1167/iovs.08-2116. PMC 3225203. PMID 18791174.
• Yeretssian G, Doiron K, Shao W, Leavitt BR, Hayden MR, Nicholson DW, Saleh M (June 2009). "Gender differences in expression of the human caspase-12 long variant determines susceptibility to Listeria monocytogenes infection". Proc. Natl. Acad. Sci. U.S.A. 106 (22): 9016–20. doi:10.1073/pnas.0813362106. PMC 2690057. PMID 19447924.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.