A2 Vertaisarvioitu katsausartikkeli tieteellisessä lehdessä
Metacaspases
Tekijät: Tsiatsiani L, Van Breusegem F, Gallois P, Zavialov A, Lam E, Bozhkov PV
Kustantaja: NATURE PUBLISHING GROUP
Julkaisuvuosi: 2011
Journal: Cell Death and Differentiation
Tietokannassa oleva lehden nimi: CELL DEATH AND DIFFERENTIATION
Lehden akronyymi: CELL DEATH DIFFER
Vuosikerta: 18
Numero: 8
Aloitussivu: 1279
Lopetussivu: 1288
Sivujen määrä: 10
ISSN: 1350-9047
DOI: https://doi.org/10.1038/cdd.2011.66
Tiivistelmä
Metacaspases are cysteine-dependent proteases found in protozoa, fungi and plants and are distantly related to metazoan caspases. Although metacaspases share structural properties with those of caspases, they lack Asp specificity and cleave their targets after Arg or Lys residues. Studies performed over the past 10 years have demonstrated that metacaspases are multifunctional proteases essential for normal physiology of non-metazoan organisms. This article provides a comprehensive overview of the metacaspase function and molecular regulation during programmed cell death, stress and cell proliferation, as well as an analysis of the first metacaspase-mediated proteolytic pathway. To prevent further misapplication of caspase-specific molecular probes for measuring and inhibiting metacaspase activity, we provide a list of probes suitable for metacaspases. Cell Death and Differentiation (2011) 18, 1279-1288; doi:10.1038/cdd.2011.66; published online 20 May 2011
Metacaspases are cysteine-dependent proteases found in protozoa, fungi and plants and are distantly related to metazoan caspases. Although metacaspases share structural properties with those of caspases, they lack Asp specificity and cleave their targets after Arg or Lys residues. Studies performed over the past 10 years have demonstrated that metacaspases are multifunctional proteases essential for normal physiology of non-metazoan organisms. This article provides a comprehensive overview of the metacaspase function and molecular regulation during programmed cell death, stress and cell proliferation, as well as an analysis of the first metacaspase-mediated proteolytic pathway. To prevent further misapplication of caspase-specific molecular probes for measuring and inhibiting metacaspase activity, we provide a list of probes suitable for metacaspases. Cell Death and Differentiation (2011) 18, 1279-1288; doi:10.1038/cdd.2011.66; published online 20 May 2011
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