Cytochrome c from human heart

Cytochrome c (CYCS) is mapped to human chromosome 7p15.3. CYCS is a heme protein containing three long α-helices. It undergoes domain swapping at the C-terminus and exists in dimeric, trimeric, and tetrameric forms. Insertion mutations in CYCS is implicated in acute myeloid leukemia. Mutations in CYCS modulates the release of proplatelets and decreases platelet production leading to thrombocytopenia 4.

Cytochrome c has been identified as an important mediator in apoptotic pathways. The release of mitochondrial cytochrome c into the cytoplasm stimulates apoptosis and is commonly used as an indicator of the apoptotic process in the cell. Investigation on the effect of Paris Saponin I (PS I) on human gastric carcinoma cell growth (SGC7901 cells) have shown an elevated level cytoplasmic cytochrome c. Results are an inhibition of proliferation in SGC7901 cells by inducing mitochondria-dependent apoptosis through cytochrome c.

Cytochrome c from human heart has been used for the generation of standard curves in the electrochemiluminescence assay for measurement of cytochrome C levels in plasma samples and in electrospray ionization mass spectrum (ESI-MS) analysis.

Cytochrome c is a small heme protein that is a mobile electron carrier in the mitochondrial electron transport chain. It is also an initiator of apoptosis.

The ready fluctuation of cytochrome c within the cell between ferrous and ferric states, makes it an efficient biological electron-transporter. It plays a vital role in cellular oxidations in both plants and animals. Generally regarded as a universal catalyst of respiration, it forms the essential electron-bridge between the respirable substrates and oxygen.

The ready fluctuation of cytochrome c within the cell between ferrous and ferric states, makes it an efficient biological electron-transporter. It plays a vital role in cellular oxidations in both plants and animals. Generally regarded as a universal catalyst of respiration, it forms the essential electron-bridge between the respirable substrates and oxygen.

In addition to its function in electron transport, cytochrome c acts as an apoptosis-triggering agent, forming the apoptosome with apoptosis protease-activating factor-1 (Apaf-1) and activating the caspase cascade. The two functions are finely tuned by phosphorylation of Tyr residues at position 48 and/or 97. One recent report provides suggestive evidence that phosphorylation at Tyr⁴⁸ switches off the apoptotic effect.

Lyophilized from a 0.2 μm filtered solution in phosphate buffered saline.

Chemically oxidized during purification.

View more information on cytochrome c and electron transport at www.sigma-aldrich.com/enzymeexplorer.