Fas receptor

Multiple isoforms of the Fas receptor protein are produced by alternative splicing.

Fas receptor has been shown to interact with:

The mechanism by which bile acids stimulate the activation of Fas receptor remains unclear.

The Fas receptor contains a death domain and has been shown to play a central role in the physiological regulation of programmed cell death.

The Fas receptor is a death receptor on the surface of cells that leads to programmed cell death (apoptosis).

Apoptosis-inducing Fas receptor is dubbed isoform 1 and is a type 1 transmembrane protein.

Some children with autoimmune lymphoproliferative disorders are heterozygous for a mutation in the gene that codes for the Fas receptor.

In cultured cells, FasL induces various types of cancer cell apoptosis through the Fas receptor.

It is associated with programmed cell death (apoptosis) and regulates alternative splicing of the gene encoding the Fas receptor, an apoptosis-promoting protein.

An mRNA including exon 6 encodes the membrane-bound form of the Fas receptor, which promotes apoptosis, or programmed cell death.

Membrane-anchored Fas ligand trimer on the surface of an adjacent cell causes trimerization of Fas receptor.

Furthermore, the Fas receptor also mediates tumor-specific cytotoxic T lymphocyte (CTL) anti-tumor cytotoxicity.

FAF interacts with the cytoplasmic domain of the Fas receptor to potentiate Fas-mediated apoptosis [ 56 57 ] .

Normally, stimulation of recently activated T cells by antigen leads to coexpression of Fas and Fas receptor on the T cell surface.

APO010 causes cell death of cancerous cells through a mechanism of targeting Fas receptors on the surface of cancer cells inducing cell apoptosis.

FasR: The Fas receptor (FasR), or CD95, is the most intensely studied member of the death receptor family.

Infected lymphocytes express the Fas ligand, a cell-surface protein that triggers the death of neighboring uninfected T-cells expressing the Fas receptor.

The engagement of Fas by Fas receptor results in apoptosis of the cell and is important for eliminating T cells that are repeatedly stimulated by antigens.

In order for a tumor cell to survive, it must decrease its expression of tumor suppressor genes such as p53, BRCA1, BRCA2, RB1 or the fas receptor.

Fas receptor, an important cell surface receptor protein of the TNF receptor family known also as CD95, that induces apoptosis on binding Fas ligand.

In this pathway, a Fas ligand (FasL) on the CTL binds to Fas receptor (FasR) on the target cell.

In contrast, glycine-conjugated bile acids induce apoptosis in McNtcp.24 cells and primary mouse hepatocytes, through activation of the Fas receptor in a FasL-independent manner [ 19 25 ] .

Lack of a functional Fas ligand / Fas receptor system has been linked to abnormal follicle development, and greater numbers of secondary follicles as a result of the inability to induce apoptosis.

This leaves the possibility that conjugated bile acids may activate the apoptotic cascade through Fas receptor in this cell line, as glycine-conjugated bile acids do in hepatocytes [ 25 ] .

Increased expression of Fas receptor in skin cells chronically exposed to the sun, and absence of expression in skin cancer cells, suggests that this mechanism may be important in elimination of pre-cancerous cells in humans.