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Few Aspects Regarding Leukemia Inhibitory Factor (LIF)

Fas ligand or FasL (CD178 or CD95L) is a type II transmembrane protein. Cytotoxic T lymphocytes express FasL on their surfaces that belong to the TNF family of proteins. By binding to its receptors, FasL induces apoptosis in cells. A matrix metalloproteinase MMP-7 cleaves membrane-bound FasL and generates a soluble FasL. FasL interacts with its receptors and plays a crucial role in immune system regulation and cancer progression. Fas ligand or FasL (CD178 or CD95L) is a homotrimeric human type II transmembrane protein. The Fas ligand gene (FASLG) on chromosome 1q24.3 encodes the Fas ligand protein. Cytotoxic T lymphocytes express FasL on their surfaces that belong to the TNF family of proteins. By binding to its receptors, FasL induces apoptosis in cells.

Fas fasl system (CD178) is a membrane protein that belongs to the tumor necrosis factor (TNF) superfamily. In its membrane-bound form, it is a transmembrane protein expressed by some T cells, NK cells and several cell types of the immune system. Fas ligand induces apoptosis in the apoptosis-inducing receptor Fas receptor, which belongs to the TNF receptor family. It does this by forming a death-inducing signaling complex (DISC) after binding to its receptors. DISC can be formed with FasR or TRAILR or DR5. 

This gene encodes a member of the TNF-receptor superfamily. This receptor can activate apoptosis and cellular proliferation, or inhibit cellular proliferation, depending on the cell type. The protein containing a death domain has been shown to mediate apoptosis when it forms a death-inducing signaling complex (DISC). It is likely that the different functions of this receptor are mediated by interactions with different target proteins. Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been identified. As with other members of the TNF superfamily, the encoded protein undergoes proteolytic cleavage to produce mature forms of soluble ligand and transmembrane ligand bound to p75.

Leukemia inhibitory factor (LIF) is a cytokine encoded by the LIF gene. LIF is an IL-6 class protein that inhibits cell differentiation, affecting cell growth. A decrease in LIF levels signals the cells to differentiate. In developing embryos, trophectoderm expresses LIF. LIF binds to LIF-receptor (LIFR), present throughout the embryonic inner cell mass. During the blastocyst stage, the inner cell mass produces embryonic stem cells, and if we remove these cells from the inner cell mass, the embryo loses its LIF source.

LIF binds to LIF-receptor (LIFR), present throughout the embryonic inner cell mass. During the blastocyst stage, the inner cell mass produces embryonic stem cells, and if we remove these cells from the inner cell mass, the embryo loses its LIF source. LIF is produced as a 202 amino acid precursor protein. Upon removing 22 amino acids post-translationally, it processes the precursor protein into a 20 kilodalton active form. 

Leukemia inhibitory factor (LIF) is a cytokine that is encoded by the LIF gene. It is an interleukin-6 class cytokine that inhibits cell differentiation, thus affecting cell growth. Its function varies with its concentration.[1] In developing embryos, trophectoderm expresses LIF. LIF binds to leukemia inhibitory factor receptor (LIFR), which is found throughout the embryonic inner cell mass. During the blastocyst stage, the inner cell mass produces embryonic stem cells, and if we remove these cells from the inner cell mass, the embryo loses its LIF source.

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