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The stoichiometry of cytochrome c to Apaf-1 within the complex is proved to be 1:1. [1] There are some debates about whether stable incorporation of cytochrome c into the apoptosome is required following oligomerization, but recent structural data favor the idea that cytochrome c stabilizes the oligomeric human apoptosome. [1]
Cytochrome c is a highly conserved protein across the spectrum of eukaryotic species, found in plants, animals, fungi, and many unicellular organisms. This, along with its small size (molecular weight about 12,000 daltons), [7] makes it useful in studies of cladistics. [8] Cytochrome c has been studied for the glimpse it gives into evolutionary ...
Small soluble cytochrome c proteins with a molecular weight of 8-12 kDa and a single heme group belong to class I. [10] [11] It includes the low-spin soluble cytC of mitochondria and bacteria, with the heme-attachment site located towards the N-terminus, and the sixth ligand provided by a methionine residue about 40 residues further on towards the C-terminus.
The X-linked inhibitor of apoptosis protein is overexpressed in cells of the H460 cell line. XIAPs bind to the processed form of caspase-9 and suppress the activity of apoptotic activator cytochrome c, therefore overexpression leads to a decrease in the number of proapoptotic agonists. As a consequence, the balance of anti-apoptotic and ...
The redox potential for cytochrome c can also be "fine-tuned" by small changes in protein structure and solvent interaction. [4] The number of heme C units bound to a holoprotein is highly variable. For vertebrate cells one heme C per protein is the rule but for bacteria this number is often 2, 4, 5, 6 or even 16 heme C groups per holoprotein.
Regarding the activation of caspases, there exists a gene called ced-9 in C. elegans that protects against cell death that is a part of the Bcl-2 family. ced-9 encodes a protein that is structurally similar to Bcl-2 that binds to another protein ced-4, a homolog of APAF-1 in humans, and prevents it from activating caspase ced-3, which is necessary for killing of the cell. [4]
Caspase-9 is an enzyme that in humans is encoded by the CASP9 gene.It is an initiator caspase, [5] critical to the apoptotic pathway found in many tissues. [6] Caspase-9 homologs have been identified in all mammals for which they are known to exist, such as Mus musculus and Pan troglodytes.
Overview of signal transduction pathways involved in apoptosis. Cell death is the event of a biological cell ceasing to carry out its functions. This may be the result of the natural process of old cells dying and being replaced by new ones, as in programmed cell death, or may result from factors such as diseases, localized injury, or the death of the organism of which the cells are part.