Apoptosis – even the cells must die

from For the sake of reproducibility - a technical replicate by Tumor Necrosis Factor-alpha

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Death-receptor, binding the ligand prompting the clustering and formation of a death-inducing signalling complex
Recruitment, by the Fas-associated death domain, of procaspase-8 molecules, proximal activation

A cascade of caspases amplifying pro-apoptotic signals
A crowd of zymogens allowing for the enzymes’mutual cleavage activation
Protein-protein interactions activating upstream caspase initiators
Proteolytically activated apoptotic cell death effectors

Cytochrome c electron carrier, reveals itself to be crucial in cytosolic caspase-9 activation
Pro-apoptotic Bcl-2 inducing the release of the aforementioned, via rupturing of the mitochondrial outer membrane

Procaspase-9 and Apaf-1 forming the apoptosome (complex)
Apoptotic pathway modulated via heat-shock proteins action
Various downstream interactions and multiple subprogram branching
Resulting in cell removal, in an orderly dismantling

Precisely regulated and tightly organized death-inducing pathway; apoptosis

Ref: Hengartner MO “The biochemistry of apoptosis.” Nature 407(6805):770-776 (2000)

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from For the sake of reproducibility - a technical replicate, released January 24, 2018

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Tumor Necrosis Factor-alpha Neuville, Québec

Scientists, academics, gorefiends and grindheads of the world rejoice: Tumor Necrosis Factor-alpha unleashes its take on full blown Carcass-worship, topped with unique lyrical themes inspired by the most recent knowledge in state-of-the-art scientific research from the fields of cellular and molecular biology. ... more

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