Caspase 9

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.

Caspase-3 is one of the most important players in apoptosis signaling. It is synthesized as an inactive 32 kDa pro-enzyme and upon direct activation by Caspase-8, -9 or -10, it gets processed into its active forms, the p17-20 and p10-12 subunits. The latter are responsible for the cleavage of PARP (poly ADP-ribose polymerase), actin and SREBP, which are associated with apoptosis [1].

The D4-GDI protein is a negative regulator of the Ras-related Rho family of small molecule "molecular switch" GTPases. The Rho GTPases modify cell structure and architecture via rapid changes to the actin cytoskeleton and cell membrane. Many of these physiological processes are associated with apoptotic cell death, thus the in vivo removal of D4-GDI inhibitory block is critical for proper induction and progression of apoptosis in cells.

DNA methylation plays a critical role the long-term silencing of transcription and is essential for processes such as embryonic development, germline differentiation, and tissue maturation.

Cell death via apoptosis is a basic cellular function occurring through the cell death receptor family and their ligands which signal through downstream adaptor molecules and the caspase protease family. Caspases have a precursor form composed of a prodomain, and large and small catalytic subunit, and are activated through a cleavage adjacent to an aspartate to liberate units and allow formation of an a2b2 tetramer. Caspase 3 is a cytoplasmic caspase with two isoforms (one acts as a dominant negative inhibitor), and is involved in the activation cascade for apoptosis execution.

Cell death via apoptosis is a key cellular function triggered by the cell death receptor family and their ligands which signal through downstream adaptor molecules and the caspase protease family. Among the subclass of initiator caspases that include subtypes -2, -8 and -9, caspase 9 is expressed in a variety of human tissues.

Caspase 9 (also termed ICE-LAP6, Mch6, Apaf-3) is a member of cysteine protease family of caspases and is encoded by the CASP9 gene in humans. Caspase-9 is involved in mitochondrial apoptosis pathway and is an initiator caspase.

Caspase 7 (also known as CASP7, Mch3, ICE-LAP3, CMH-1) is a member of caspase family of cysteine proteases. It is an apoptosis-related cystein peptidase encoded by the CASP7 gene in humans. CASP7 homologous sequences have been identified in nearly all mammals. Similar to Caspase 3, Caspase-7 is an effector caspase and plays a key role in apoptotic execution.

Apoptosis is one of the main types of programmed cell death which involves a cascade of biochemical events leading to specific cell morphology characteristics and ultimately death of cells.