Processing of native caspase-14 occurs at an atypical cleavage site in normal epidermal differentiation - PubMed (original) (raw)
Processing of native caspase-14 occurs at an atypical cleavage site in normal epidermal differentiation
Andy J Chien et al. Biochem Biophys Res Commun. 2002.
Abstract
Caspase-14, a cysteinyl aspartate-specific protease expressed during epidermal differentiation, is detected exclusively in the cytosolic fraction of epidermis as a complex of procaspase-14 together with caspase-14 large and small subunits. On non-denaturing protein gels, native caspase-14 has a relative electrophoretic mobility of approximately 80kDa, which resolves into caspase-14 proform, large and small subunit in SDS-polyacrylamide. Purification of caspase-14 from native skin with subsequent N-terminal sequencing of the small subunit and tryptic digest analysis of the large subunit revealed an atypical processing site between Ile152 and Lys153, which distinguishes it from other caspases described to date that are processed at aspartate residues. Expression of caspase-14 in heterologous systems results in unprocessed procaspase-14 without generation of the large and small subunits that characterize this protein family. However, addition of cellular extracts to purified recombinant human caspase-14 generated immunoreactive peptides indistinguishable from large and small subunits in skin. These data provide evidence for novel processing of caspase-14 suggesting that this enzyme has unique mechanisms of regulation during epidermal differentiation.
Similar articles
- Purification and characterization of active caspase-14 from human epidermis and development of the cleavage site-directed antibody.
Hibino T, Fujita E, Tsuji Y, Nakanishi J, Iwaki H, Katagiri C, Momoi T. Hibino T, et al. J Cell Biochem. 2010 Feb 15;109(3):487-97. doi: 10.1002/jcb.22425. J Cell Biochem. 2010. PMID: 19960512 - Nine procaspases are expressed in normal human epidermis, but only caspase-14 is fully processed.
Raymond AA, Méchin MC, Nachat R, Toulza E, Tazi-Ahnini R, Serre G, Simon M. Raymond AA, et al. Br J Dermatol. 2007 Mar;156(3):420-7. doi: 10.1111/j.1365-2133.2006.07656.x. Br J Dermatol. 2007. PMID: 17300228 - Caspase-14 but not caspase-3 is processed during the development of fetal mouse epidermis.
Fischer H, Rossiter H, Ghannadan M, Jaeger K, Barresi C, Declercq W, Tschachler E, Eckhart L. Fischer H, et al. Differentiation. 2005 Oct;73(8):406-13. doi: 10.1111/j.1432-0436.2005.00046.x. Differentiation. 2005. PMID: 16316411 - In vivo calpain/caspase cross-talk during 3-nitropropionic acid-induced striatal degeneration: implication of a calpain-mediated cleavage of active caspase-3.
Bizat N, Hermel JM, Humbert S, Jacquard C, Créminon C, Escartin C, Saudou F, Krajewski S, Hantraye P, Brouillet E. Bizat N, et al. J Biol Chem. 2003 Oct 31;278(44):43245-53. doi: 10.1074/jbc.M305057200. Epub 2003 Aug 12. J Biol Chem. 2003. PMID: 12917435 - Caspase-14 reveals its secrets.
Denecker G, Ovaere P, Vandenabeele P, Declercq W. Denecker G, et al. J Cell Biol. 2008 Feb 11;180(3):451-8. doi: 10.1083/jcb.200709098. Epub 2008 Feb 4. J Cell Biol. 2008. PMID: 18250198 Free PMC article. Review.
Cited by
- Exploring caspase functions in mouse models.
Svandova E, Vesela B, Janeckova E, Chai Y, Matalova E. Svandova E, et al. Apoptosis. 2024 Aug;29(7-8):938-966. doi: 10.1007/s10495-024-01976-z. Epub 2024 Jun 2. Apoptosis. 2024. PMID: 38824481 Free PMC article. Review. - The causal role of circulating immunity-inflammation in preeclampsia: A Mendelian randomization.
Xue X, Guo C, Fan C, Lei D. Xue X, et al. J Clin Hypertens (Greenwich). 2024 May;26(5):474-482. doi: 10.1111/jch.14775. Epub 2024 Mar 12. J Clin Hypertens (Greenwich). 2024. PMID: 38476059 Free PMC article. - Caspase-14: a novel caspase in the retina with a potential role in diabetic retinopathy.
Al-Shabrawey M, Ahmad S, Megyerdi S, Othman A, Baban B, Palenski TL, Shin ES, Gurel Z, Hsu S, Sheibani N. Al-Shabrawey M, et al. Mol Vis. 2012;18:1895-906. Epub 2012 Jul 14. Mol Vis. 2012. PMID: 22876114 Free PMC article. - Gata-3 negatively regulates the tumor-initiating capacity of mammary luminal progenitor cells and targets the putative tumor suppressor caspase-14.
Asselin-Labat ML, Sutherland KD, Vaillant F, Gyorki DE, Wu D, Holroyd S, Breslin K, Ward T, Shi W, Bath ML, Deb S, Fox SB, Smyth GK, Lindeman GJ, Visvader JE. Asselin-Labat ML, et al. Mol Cell Biol. 2011 Nov;31(22):4609-22. doi: 10.1128/MCB.05766-11. Epub 2011 Sep 19. Mol Cell Biol. 2011. PMID: 21930782 Free PMC article. - Hairless is a nuclear receptor corepressor essential for skin function.
Thompson CC. Thompson CC. Nucl Recept Signal. 2009 Dec 31;7:e010. doi: 10.1621/nrs.07010. Nucl Recept Signal. 2009. PMID: 20087431 Free PMC article. Review.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases