Apoptosis

Cell death via apoptosis is a fundamental cellular function triggered by the cell death receptor family and their ligands which signal through downstream adaptor molecules and the caspase protease family. All caspases exist in a precursor form composed of a prodomain, and large and small catalytic subunits. Caspases require a cleavage adjacent to an aspartate to liberate one large and one small subunit, which can then associate into an a2b2 tetramer.

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.

The CXCR7 (C-X-C chemokine receptor type 7) proinflammatory protein is a member of the G-protein coupled receptor (GPCR) family. It is a transmembrane protein first identified as the EBV-induced gene-1, and while it was originally classified as an orphan receptor, it is now known to be a novel and alternate receptor for the chemokines CXCL11 and CXCL12.

Cells undergo apoptotic programmed cell death in response to various stimuli. The process is required for morphogenesis, tissue homeostasis, and host defense. Certain cytokines such as tumor necrosis factor (TNF) and Fas ligand signal through death domain-containing receptors such as tumor necrosis factor receptor 1 (TNFR1) and Fas.

Nur77 is a member of the steroid/thyroid hormone phosphoprotein receptor superfamily. It is heavily post-translationally modified and rapidly induced in response to androgens and growth factors. It governs fundamental processes such as cell proliferation, differentiation, and apoptosis. For some time, it was classified as an orphan receptor with no identifiable or known ligand, but scientists finally were able to identify a novel class of methylene-substituted diindolylmethanes (C-DIM) as its endogenous ligand.

Livin is a member of the inhibitor of apoptosis proteins (IAP) family that regulates programmed cell death. The Livin protein contains a single baculovirus IAP repeat (BIR) essential for function, along with a COOH-terminal RING-type zinc finger domain. In general, IAP proteins block apoptosis by binding and inhibiting caspases through this BIR domain. Two Livin splicing variants, alpha and beta, have been identified, and each has different anti-apoptotic properties. With Livin expression low in adult tissues, it is somewhat higher in developmental tissues.

Apoptosis, or programmed cell death, is a normal component of cellular differentiation and the development of multicellular organisms. Receptor activator of NF-kB (RANK) lacks significant homology with the other family members of the tumor necrosis factor receptor (TNFR) superfamily. The cytoplasmic domain of RANK interacts with the tumor necrosis factor receptor associated factors, adaptor proteins such as TRAF2, TRAF5 and TRAF6.

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.

Cells undergo apoptotic programmed cell death in response to various stimuli, and this key mechanism is necessary for cellular morphogenesis, tissue homeostasis, and host defense. Particular cytokines such as tumor necrosis factor (TNF) and the Fas ligand signal through their cooperative death domain-containing receptors tumor necrosis factor receptor 1 (TNFR1) and Fas. Like its cousin TRAIL-R1, TRAIL-R2 is widely expressed in both normal tissues as well as in many types of tumor cells.