From Wikipedia, the free encyclopedia
Caspase 12 is an enzyme known as a cysteine protease. It belongs to a family of enzymes called caspases that cleave their substrates at C-terminal aspartic acid residues. It is closely related to caspase 1 and other members of the caspase family, known as inflammatory caspases, which process and activate inflammatory cytokines such as interleukin 1 and interleukin 18.
The CASP12 gene is subject to polymorphism, which can generate a full length caspase protein (Csp12L) or an inactive truncated form (Csp12S). The functional form appears to be confined to people of African descent and is linked with susceptiblilty to sepsis; people carrying the functional gene have decreased responses to bacterial molecules such as lipopolysaccharide (LPS).[1] [2] The gene for caspase 12 is found on chromosome 11 in humans in a locus with other inflammatory caspases.[3]
[edit] References
- ^ 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 (2004). "Differential modulation of endotoxin responsiveness by human caspase-12 polymorphisms". Nature 429 (6987): 75–9. doi:10.1038/nature02451. PMID 15129283.
- ^ Saleh, Maya Mathison, John C. Wolinski, Melissa K. Bensinger, Steve J. Fitzgerald, Patrick Droin, Nathalie Ulevitch, Richard J. Green, Douglas R. Nicholson, Donald W. (2006). "Enhanced bacterial clearance and sepsis resistance in caspase-12-deficient mice". Nature 440 (7087): 1064–1068. doi:10.1038/nature04656.
- ^ Fischer H, Koenig U, Eckhart L, Tschachler E (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.
