Abstract
The identification and description of an intrinsic program of regulated cellular suicide or apoptosis was originally obtained from morphological analyses in developmental biology (76, 77). This program exists in all multicellular organisms, and genetic analyses in the nematode Caenorhabditis elegans identified three ced-genes (for C. elegans death) as basal, highly conserved components of this program, see (39, 57). In mammals, several structural and functional homologs of these ced-encoded proteins are involved in the apoptosis regulating complex formation at the outer mitochondrial membrane (Fig. 1), the apoptosome (56, 124), such as Apaf-1 (for “apoptosis protease activating factor”) or proteins of the Bcl-2 family (see chapter I.2.2). Another important discovery from C. elegans genetics was the identification of interleukin-lß-converting enzyme (ICE or caspase-1) as a functional homolog of the ced-3 gene product. This discovery triggered the identification of a whole cascade of caspases (for “cysteine-containing aspartic acid proteases”, see chapter I.3.1). This cascade is involved in the execution phase of apoptosis (164), and one source for activating the cascade is the mitochondrial apoptosome (Fig. 1).
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Holtz, J., Darmer, D. (2000). Death receptors and their ligands. In: Schunkert, H., Riegger, G.A.J. (eds) Apoptosis in Cardiac Biology. Basic Science for the Cardiologist, vol 5. Springer, Boston, MA. https://doi.org/10.1007/978-0-585-38143-5_1
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