CASP3
Каспаза-3 — это белок, который кодируется геном CASP3. Участвует в активации каскада каспаз, ответственных за апоптоз. В начале апоптоза он протеолитически расщепляет поли(АДФ-рибозу) полимеразу (PARP) в связи '216-Asp-|-Gly-217'. Расщепляет и активирует белки, связывающие регуляторные элементы стерола (SREBP) между основным доменом лейциновой молнии helix-loop-helix и доменом прикрепления мембраны. Расщепляет и активирует каспазу-6, -7 и -9. Участвует в расщеплении гентингтина. Вызывает клеточную адгезию в симпатических нейронах через расщепление RET.
The CASP3 encodes the caspase-3, one of the major executioner caspases in the apoptotic signaling because of its role in coordinating the demolishment of cellular structures such as DNA fragmentation or membrane blebbing. Caspase-3 is produced as a zymogen in an inactive pro-form. Cleavage and activation of pro-caspase-3 are catalyzed by initiator caspases, caspase-8, and caspase-9 through an internal cleavage to separate the large and small subunits to generate the active caspase-3 heterodimer. In the APAF-1/caspase-9 apoptosome-initiated caspase activation cascade, caspase-3 has been shown to mediate feedback processing on caspase-9. Once activated, caspase-3 cleaves Bcl-2 and Bcl-XL, which abolishes the anti-apoptotic function of these proteins and releases C-terminal fragments that are pro-apoptotic. The cleavage of ICAD (inhibitor of caspase-activated DNase) by caspase-3 prompts the release of active CAD, which cleaves DNA and promotes chromatin condensation. Caspase-3 also cleaves and activates gelsolin, a protein that regulates actin dynamics. Activated gelsolin promotes both cytoplasmic and nuclear apoptosis. Katelyn G. Ponder et al. proved an initial cleavage event at D9 is required to allow cleavage at D28 that causes the complete removal of the prodomain allowing for full caspase-3 activation. |
