Editing Apoptosis (section)

==Caspase-independent apoptosis==
The characterization of the caspases allowed the development of caspase inhibitors, which can be used to determine whether a cellular process involves active caspases. Using these inhibitors it was discovered that cells can die while displaying a morphology similar to apoptosis without caspase activation.<ref name="pmid8962091">{{cite journal | vauthors = Xiang J, Chao DT, Korsmeyer SJ | title = BAX-induced cell death may not require interleukin 1 beta-converting enzyme-like proteases | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 93 | issue = 25 | pages = 14559–14563 | date = December 1996 | pmid = 8962091 | pmc = 26172 | doi = 10.1073/pnas.93.25.14559 | doi-access = free | bibcode = 1996PNAS...9314559X }}</ref> Later studies linked this phenomenon to the release of AIF ([[apoptosis-inducing factor]]) from the mitochondria and its translocation into the nucleus mediated by its NLS ([[Nuclear localization sequence|nuclear localization signal]]). Inside the mitochondria, AIF is anchored to the inner membrane. In order to be released, the protein is cleaved by a calcium-dependent [[Calpain|calpain protease]].{{citation needed|date=November 2024}}