Leukemia Inhibitory Factor (LIF) is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. LIF has a number of other activities including cholinergic neuron differentiation; control of stem cell pluripotency; bone and fat metabolism; mitogenesis of certain factor dependent cell lines and promotion of megakaryocyte production in vivo. Human and murine mature LIF exhibit a 78% sequence identity at the amino acid level. Human LIF is equally active on human and mouse cells. Murine LIF is approximately 1000 fold less active on human cells than human LIF.
Leukemia inhibitory factor (LIF) is a pleiotropic glycoprotein belonging to the IL-6 family of cytokines. It’s involved in growth promotion and cell differentiation of different types of target cells; influence on bone metabolism; cachexia; neural development; embryogenesis and inflammation. LIF has potent proinflammatory property; being the inducer of the acute phase protein synthesis and affecting the cell recruitment into the area of damage or inflammation. LIF is also one of the cytokines that are capable to regulate the differentiation of embryonic stem cells; hematopoietic and neuronal cells. LIF binds to the specific LIF receptor (LIFR-α) which forms a heterodimer with a specific subunit common to all members of that family of receptors; the GP130 signal transducing subunit. This leads to activation of the JAK/STAT and MAPK cascades. Due to its polyfunctional activities; LIF is involved in the pathogenic events and development of many diseases of various origin.
Leukemia inhibitory factor (LIF) is a pleiotropic glycoprotein belonging to the IL-6 family of cytokines. It&rsquo,s involved in growth promotion and cell differentiation of different types of target cells, influence on bone metabolism, cachexia, neural development, embryogenesis and inflammation. LIF has potent proinflammatory property, being the inducer of the acute phase protein synthesis and affecting the cell recruitment into the area of damage or inflammation. LIF is also one of the cytokines that are capable to regulate the differentiation of embryonic stem cells, hematopoietic and neuronal cells. LIF binds to the specific LIF receptor (LIFR-&alpha,) which forms a heterodimer with a specific subunit common to all members of that family of receptors, the GP130 signal transducing subunit. This leads to activation of the JAK/STAT and MAPK cascades. Due to its polyfunctional activities, LIF is involved in the pathogenic events and development of many diseases of various origin.
LIFR (leukemia inhibitory factor receptor) belongs to the family of cytokine receptors. LIFR forms a high-affinity receptor complex with gp130, which mediates the activity of LIF (leukemia inhibitory factor) and thus affects the differentiation, proliferation, and survival of a wide variety of cells in the adult and the embryo. Besides LIF, LIFR can also bind to and activate CNTF (ciliary neurotrophic factor) and CLC (cardiotrophin like cytokine). Evidence showed that in the retina, LIFR activating LIF, CT-1 and cardiotrophin like cytokine (CLC) are strongly upregulated in response to preconditioning with bright cyclic light leading to robust activation of signal transducer and activator of transcription-3 (STAT3) in a time-dependent manner. Further, blocking LIFR activation during preconditioning using a LIFR antagonist (LIF05) attenuated the induced STAT3 activation and also resulted in reduced preconditioning-induced protection of the retinal photoreceptors. These data demonstrate that LIFR and its ligands play an essential role in endogenous neuroprotective mechanisms triggered by preconditioning-induced stress. LIFR was newly found to be a suppressor of hepatocellular carcinoma (HCC), one of the world's top five causes of cancer-related deaths.
Human TNFSF14 Protein; also known as LIGHT; belongs to a member of the tumor necrosis factor (TNF) ligand family. It can bind to NFRSF3/LTBR. It is a ligand for TNFRSF14; which is a member of the tumor necrosis factor receptor superfamily; and it is also known as a herpesvirus entry mediator ligand (HVEML). TNFSF14 encodes a protein with a 37 aa cytoplasmic domain; 21aa transmembrane domain and 182 aa extracellular region. The gene is predominantly expressed in the spleen and also found in the brain. Weakly expressed in peripheral lymphoid tissues and in heart; placenta; liver; lung; appendix; and kidney; and no expression seen in fetal tissues; endocrine glands; or nonhematopoietic tumor lines. TNFSF14 protein was found to probably function as a costimulatory factor for the activation of lymphoid cells and as a deterrent to infection by herpesvirus. Studies have shown that this protein can prevent tumor necrosis factor alpha mediated apoptosis in primary hepatocyte. Two alternatively spliced transcript variant encoding distinct isoforms have been reported.
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