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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 ...
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 ...
Executioner caspases degrade over 600 cellular components [19] in order to induce the morphological changes for apoptosis. Examples of caspase cascade during apoptosis: Intrinsic apoptopic pathway: During times of cellular stress, mitochondrial cytochrome c is released into the cytosol.
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.
Complex III itself is composed of several subunits, one of which is a b-type cytochrome while another one is a c-type cytochrome. Both domains are involved in electron transfer within the complex. Complex IV contains a cytochrome a/a3-domain that transfers electrons and catalyzes the reaction of oxygen to water.
[7] [10] [12] [14] Through the intrinsic pathway of apoptosis, BCL-2 proteins like BAK and BAX form a pore in the outer mitochondrial membrane, leading to mitochondrial membrane permeabilization and the release of both cytochrome c and SMAC. [9] [10] While cytochrome c directly activates APAF1 and caspase 9, SMAC binds IAPs, such as XIAP and ...
The anti-apoptotic Bcl-2 and Bcl-xL proteins inhibit cytochrome c release through the mitochondrial pore and also inhibit activation of the cytoplasmic caspase cascade by cytochrome c. [8] Dephosphorylated BAD forms a heterodimer with Bcl-2 and Bcl-xL, inactivating them and thus allowing Bax/Bak-triggered apoptosis.