Cytochrome C

Traumatic brain injury (TBI) currently contributes to nearly 30% of all injury deaths in the United States.  Characterized by an abrasive head injury that interrupts normal brain function, TBI can range from mild to severe.  Mild symptoms can present themselves as excessive tiredness, difficulty concentrating and lack of clear thinking.  Severe cases of TBI are hallmarked by unusual behavior, seizures and loss of consciousness.  Research has shown that on a molecular level TBI triggers various mechanisms of cell death alongside attempted tissue recovery, therefore Choi et al sought

Have you ever wondered why cells in the same population respond differently to an apoptotic stimulus? Apoptosis, a form of programmed cell death, is vital for the removal of unwanted or damaged cells. As with most cellular processes, too much or too little activation can be detrimental and lead to various diseases including autoimmune disorders and cancer.

Apoptosis is a method of programmed cell death that is notably characterized by a morphological change in cellular nuclei and membrane appearance.  Not to be confused with necrosis, apoptosis is a pathway that is induced by a variety of factors that activate cysteine proteases known as caspases to lead the cell to its ultimate death versus natural death of a cell.

B-cell lymphoma 2 (Bcl-2) protein is an oncogene that normally acts as an apoptotic inhibitor and localizes to the mitochondrial membrane where it prevents the release of cytochrome c. The Bcl-2 protein family consists of over 20 proteins each containing at least one Bcl-2 homology (BH) domains and have either proapoptic or antiapoptotic activities.

Cytochrome C is a small heme protein within the inner mitochondrial membrane responsible for carrying electrons within the respiratory transport chain.  Additionally, cytochrome c has also been identified as a player in programmed cell death (apoptosis). During the early phases of apoptotic death reactions, cytochrome c translocates from the mitochondria membrane into the cytoplasm and serves to trigger the apoptotic proteolytic cascade by activating caspase 3, through association with protease activating factor-1 (Apaf-1).

Cytochrome C is an electron carrier protein that localizes in mitochondrion intermembrane space and has been identified as one of the key signaling molecules of apoptosis or programmed cell death. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol.

Mitofilin was originally described as a heart muscle protein due to its high expression in the heart. Recently, analysis of the human heart mitochondrial proteome demonstrated that Mitofilin is one of the most abundant mitochondrial proteins (1). Researchers have reported finding two alternately spliced Mitofilin variants producing proteins of 88 and 90 kDa, that were detected in immunoblots with Mitofilin antibodies (2).

Bax is a member of the Bcl-2 family; an extensive range of proteins which play key roles in apoptosis, or programmed cell death, by regulating outer mitochondrial membrane permeability. We at Novus Biologicals are one of the leading antibody suppliers for apoptosis research, with an extensive range of Bax antibody products.

The caspases are a group of cysteine protease enzymes essential to apoptosis, inflammation and necrosis. Caspase 3 has been identified as one of the key mediators of apoptosis.