A receptor subunit that combines with CYTOKINE RECEPTOR GP130 to form the dual specificity receptor for LEUKEMIA INHIBITORY FACTOR and ONCOSTATIN M. The subunit is also a component of the CILIARY NEUROTROPHIC FACTOR RECEPTOR. Both membrane-bound and secreted isoforms of the receptor subunit exist due to ALTERNATIVE SPLICING of its mRNA. The secreted isoform is believed to act as an inhibitory receptor, while the membrane-bound form is a signaling receptor.
Cell surface receptors formed from the dimerization of LIF RECEPTOR ALPHA SUBUNIT with CYTOKINE RECEPTOR GP130. Although originally described as receptors for LEUKEMIA INHIBITORY FACTOR these receptors also bind the closely-related protein ONCOSTATIN M and are referred to as both LIF receptors and type I oncostatin M receptors.
An INTERLEUKIN-6 related cytokine that exhibits pleiotrophic effects on many physiological systems that involve cell proliferation, differentiation, and survival. Leukemia inhibitory factor binds to and acts through the lif receptor.
A ciliary neurotrophic factor receptor subunit. It is anchored to the cell surface via GLYCOSYLPHOSPHATIDYLINOSITOL LINKAGE and has specificity for binding to CILIARY NEUROTROPHIC FACTOR. It lacks signal transducing domains which are found on the other two subunits of the receptor.
Cell surface proteins that bind cytokines and trigger intracellular changes influencing the behavior of cells.
Endogenous or exogenous substances which inhibit the normal growth of human and animal cells or micro-organisms, as distinguished from those affecting plant growth (= PLANT GROWTH REGULATORS).
A cytokine receptor that acts through the formation of oligomeric complexes of itself with a variety of CYTOKINE RECEPTORS.
Cell surface receptors with specificity for ONCOSTATIN M. Two subtypes of receptors have been identified and are defined by their subunit composition.
A PDGF receptor that binds specifically to both PDGF-A chains and PDGF-B chains. It contains a protein-tyrosine kinase activity that is involved in SIGNAL TRANSDUCTION.
A neurotrophic factor that promotes the survival of various neuronal cell types and may play an important role in the injury response in the nervous system.
A cytokine with both pro- and anti-inflammatory actions that depend upon the cellular microenvironment. Oncostatin M is a 28 kDa monomeric glycoprotein that is similar in structure to LEUKEMIA INHIBITORY FACTOR. Its name derives from the the observation that it inhibited the growth of tumor cells and augmented the growth of normal fibroblasts.
Cell surface receptors for CILIARY NEUROTROPHIC FACTOR. They are heterotrimeric proteins formed by the association of the CILIARY NEUROTROPHIC FACTOR RECEPTOR ALPHA SUBUNIT with the LEUKEMIA INHIBITORY FACTOR RECEPTOR ALPHA SUBUNIT and the CYTOKINE RECEPTOR GP130. Although the receptor regulates neuronal development, it is structurally similar to the cytokine receptor for INTERLEUKIN-6; (RECEPTORS, INTERLEUKIN-6).
Soluble protein factors generated by activated lymphocytes that affect other cells, primarily those involved in cellular immunity.
An ONCOSTATIN M-specific receptor subunit that combines with CYTOKINE RECEPTOR GP130 to form the ONCOSTATIN M TYPE II RECEPTOR.
A cytokine that stimulates the growth and differentiation of B-LYMPHOCYTES and is also a growth factor for HYBRIDOMAS and plasmacytomas. It is produced by many different cells including T-LYMPHOCYTES; MONOCYTES; and FIBROBLASTS.
A signal transducer and activator of transcription that mediates cellular responses to INTERLEUKIN-6 family members. STAT3 is constitutively activated in a variety of TUMORS and is a major downstream transducer for the CYTOKINE RECEPTOR GP130.
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Proteins released by sensitized LYMPHOCYTES and possibly other cells that inhibit the migration of MACROPHAGES away from the release site. The structure and chemical properties may vary with the species and type of releasing cell.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Differentiation antigens residing on mammalian leukocytes. CD stands for cluster of differentiation, which refers to groups of monoclonal antibodies that show similar reactivity with certain subpopulations of antigens of a particular lineage or differentiation stage. The subpopulations of antigens are also known by the same CD designation.
Glycoproteins found on the membrane or surface of cells.
A heterogeneous group of disorders with the common feature of prolonged eosinophilia of unknown cause and associated organ system dysfunction, including the heart, central nervous system, kidneys, lungs, gastrointestinal tract, and skin. There is a massive increase in the number of EOSINOPHILS in the blood, mimicking leukemia, and extensive eosinophilic infiltration of the various organs.
A progressive, malignant disease of the blood-forming organs, characterized by distorted proliferation and development of leukocytes and their precursors in the blood and bone marrow. Leukemias were originally termed acute or chronic based on life expectancy but now are classified according to cellular maturity. Acute leukemias consist of predominately immature cells; chronic leukemias are composed of more mature cells. (From The Merck Manual, 2006)
A cell surface receptor involved in regulation of cell growth and differentiation. It is specific for EPIDERMAL GROWTH FACTOR and EGF-related peptides including TRANSFORMING GROWTH FACTOR ALPHA; AMPHIREGULIN; and HEPARIN-BINDING EGF-LIKE GROWTH FACTOR. The binding of ligand to the receptor causes activation of its intrinsic tyrosine kinase activity and rapid internalization of the receptor-ligand complex into the cell.
Non-antibody proteins secreted by inflammatory leukocytes and some non-leukocytic cells, that act as intercellular mediators. They differ from classical hormones in that they are produced by a number of tissue or cell types rather than by specialized glands. They generally act locally in a paracrine or autocrine rather than endocrine manner.
A low affinity interleukin-6 receptor subunit that combines with the CYTOKINE RECEPTOR GP130 to form a high affinity receptor for INTERLEUKIN-6.
One of the ESTROGEN RECEPTORS that has marked affinity for ESTRADIOL. Its expression and function differs from, and in some ways opposes, ESTROGEN RECEPTOR BETA.
Cell surface receptors that are specific for INTERLEUKIN-5. They are heterodimeric proteins consisting of the INTERLEUKIN-5 RECEPTOR ALPHA SUBUNIT and the CYTOKINE RECEPTOR COMMON BETA SUBUNIT. Signaling from interleukin-5 receptors can occur through interaction of their cytoplasmic domains with SYNTENINS.
All tumors in the GASTROINTESTINAL TRACT arising from mesenchymal cells (MESODERM) except those of smooth muscle cells (LEIOMYOMA) or Schwann cells (SCHWANNOMA).
Receptors that bind and internalize the granulocyte-macrophage stimulating factor. Their MW is believed to be 84 kD. The most mature myelomonocytic cells, specifically human neutrophils, macrophages, and eosinophils, express the highest number of affinity receptors for this growth factor.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Established cell cultures that have the potential to propagate indefinitely.
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
A low affinity interleukin-5 receptor subunit that combines with the CYTOKINE RECEPTOR COMMON BETA SUBUNIT to form a high affinity receptor for INTERLEUKIN-5. Several isoforms of the interleukin-5 receptor alpha subunit exist due to multiple ALTERNATIVE SPLICING.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
Clonal expansion of myeloid blasts in bone marrow, blood, and other tissue. Myeloid leukemias develop from changes in cells that normally produce NEUTROPHILS; BASOPHILS; EOSINOPHILS; and MONOCYTES.
A protein-tyrosine kinase receptor that is specific for STEM CELL FACTOR. This interaction is crucial for the development of hematopoietic, gonadal, and pigment stem cells. Genetic mutations that disrupt the expression of PROTO-ONCOGENE PROTEINS C-KIT are associated with PIEBALDISM, while overexpression or constitutive activation of the c-kit protein-tyrosine kinase is associated with tumorigenesis.
High molecular weight polymers containing a mixture of purine and pyrimidine nucleotides chained together by ribose or deoxyribose linkages.
Hereditary diseases that are characterized by the progressive expansion of a large number of tightly packed CYSTS within the KIDNEYS. They include diseases with autosomal dominant and autosomal recessive inheritance.
A family of MEMBRANE TRANSPORT PROTEINS that require ATP hydrolysis for the transport of substrates across membranes. The protein family derives its name from the ATP-binding domain found on the protein.
The soft tissue filling the cavities of bones. Bone marrow exists in two types, yellow and red. Yellow marrow is found in the large cavities of large bones and consists mostly of fat cells and a few primitive blood cells. Red marrow is a hematopoietic tissue and is the site of production of erythrocytes and granular leukocytes. Bone marrow is made up of a framework of connective tissue containing branching fibers with the frame being filled with marrow cells.
Kidney disorders with autosomal dominant inheritance and characterized by multiple CYSTS in both KIDNEYS with progressive deterioration of renal function.
Cells contained in the bone marrow including fat cells (see ADIPOCYTES); STROMAL CELLS; MEGAKARYOCYTES; and the immediate precursors of most blood cells.
Methods of implanting a CELL NUCLEUS from a donor cell into an enucleated acceptor cell.

Cytoplasmic domains of the leukemia inhibitory factor receptor required for STAT3 activation, differentiation, and growth arrest of myeloid leukemic cells. (1/181)

Leukemia inhibitory factor (LIF) induces growth arrest and macrophage differentiation of mouse myeloid leukemic cells through the functional LIF receptor (LIFR), which comprises a heterodimeric complex of the LIFR subunit and gp130. To identify the regions within the cytoplasmic domain of LIFR that generate the signals for growth arrest, macrophage differentiation, and STAT3 activation independently of gp130, we constructed chimeric receptors by linking the transmembrane and intracellular regions of mouse LIFR to the extracellular domains of the human granulocyte macrophage colony-stimulating factor receptor (hGM-CSFR) alpha and betac chains. Using the full-length cytoplasmic domain and mutants with progressive C-terminal truncations or point mutations, we show that the two membrane-distal tyrosines with the YXXQ motif of LIFR are critical not only for STAT3 activation, but also for growth arrest and differentiation of WEHI-3B D+ cells. A truncated STAT3, which acts in a dominant negative manner was introduced into WEHI-3B D+ cells expressing GM-CSFRalpha-LIFR and GM-CSFRbetac-LIFR. These cells were not induced to differentiate by hGM-CSF. The results indicate that STAT3 plays essential roles in the signals for growth arrest and differentiation mediated through LIFR.  (+info)

Identification of a Leu-lle internalization motif within the cytoplasmic domain of the leukaemia inhibitory factor receptor. (2/181)

Leukaemia inhibitory factor (LIF) signals via a heterodimeric receptor complex comprised of the LIF receptor (LIFR) and the interleukin (IL)-6 signal transducer gp130. Upon binding to its cognate receptor LIF is internalized. In this study, we show that the LIFR is endocytosed independently of gp130. By using a heterochimaeric receptor system we identified a dileucine-based internalization motif within the cytoplasmic domain of the LIFR. Our findings suggest that a heterodimeric LIFR/gp130 complex and homodimeric gp130/gp130 complex are endocytosed via distinct internalization signals.  (+info)

The carboxyl-terminal domains of gp130-related cytokine receptors are necessary for suppressing embryonic stem cell differentiation. Involvement of STAT3. (3/181)

Cell type-specific responses to the leukemia inhibitory factor (LIF)/interleukin 6 cytokine family are mediated by dimerization of the LIF receptor alpha-chain (LIFRalpha) with the signal transducer gp130 or of two gp130 molecules followed by activation of the JAK/STAT and Ras/mitogen-activated protein kinase cascades. In order to dissect the contribution of gp130 and LIFRalpha individually, chimeric molecules consisting of the extracellular domain of the granulocyte colony stimulating factor receptor (GCSF-R) and various mutant forms of the cytoplasmic domains of gp130 or LIFRalpha were expressed in embryonic stem (ES) cells to test for suppression of differentiation, or in a factor-dependent plasma cytoma cell line to assess for induction of proliferation. Carboxyl-terminal domains downstream of the phosphatase (SHP2)-binding sites were dispensable for mitogen-activated protein kinase activation and the transduction of proliferative signals. Moreover, carboxyl-terminal truncation mutants which lacked intact Box 3 homology domains showed decreased STAT3 activation, failed to induce Hck kinase activity and suppress ES cell differentiation. Moreover, STAT3 antisense oligonucleotides impaired LIF-dependent inhibition of differentiation. Substitution of the tyrosine residue within the Box 3 region of the GSCF-R abolished receptor-mediated suppression of differentiation without affecting the transduction of proliferative signals. Thus, distinct cytoplasmic domains within the LIFRalpha, gp130, and GCSF-R transduce proliferative and differentiation suppressing signals.  (+info)

Complex conserved organization of the mammalian leukemia inhibitory factor gene: regulated expression of intracellular and extracellular cytokines. (4/181)

Leukemia inhibitory factor (LIF) is a member of the IL-6 family of pleiotropic cytokines, which are extensively involved in modulating hematopoiesis and immunity. We have undertaken a detailed analysis of LIF genomic organization and gene transcription and investigated the proteins expressed from alternate transcripts. Previously unidentified LIF transcripts, containing alternate first exons spliced onto common second and third exons, were cloned from murine embryonic stem cells, human embryonal carcinoma cells, and primary porcine fibroblasts. Based on sequence homology and position within the genomic sequence, this confirmed the existence of the LIF-M transcript in species other than the mouse and identified a new class of transcript, designated LIF-T. Thus, a complex genomic organization of the LIF gene, conserved among eutherian mammals, results in the expression of three LIF transcripts (LIF-D, LIF-M, and LIF-T) differentially expressed from alternate promoters. The first exon of the LIF-T transcript contained no in-frame AUG, causing translation to initiate downstream of the secretory signal sequence at the first AUG in exon two, producing a truncated LIF protein that was localized within the cell. Enforced secretion of this protein demonstrated that it could act as a LIF receptor agonist. Regulated expression of biologically active intracellular and extracellular LIF cytokine could thus provide alternate mechanisms for the modulation of hematopoiesis and immune system function.  (+info)

Synergistic signaling in fetal brain by STAT3-Smad1 complex bridged by p300. (5/181)

The cytokines LIF (leukemia inhibitory factor) and BMP2 (bone morphogenetic protein-2) signal through different receptors and transcription factors, namely STATs (signal transducers and activators of transcription) and Smads. LIF and BMP2 were found to act in synergy on primary fetal neural progenitor cells to induce astrocytes. The transcriptional coactivator p300 interacts physically with STAT3 at its amino terminus in a cytokine stimulation-independent manner, and with Smad1 at its carboxyl terminus in a cytokine stimulation-dependent manner. The formation of a complex between STAT3 and Smad1, bridged by p300, is involved in the cooperative signaling of LIF and BMP2 and the subsequent induction of astrocytes from neural progenitors.  (+info)

Receptor recognition sites of cytokines are organized as exchangeable modules. Transfer of the leukemia inhibitory factor receptor-binding site from ciliary neurotrophic factor to interleukin-6. (6/181)

Interleukin-6 (IL-6) and ciliary neurotrophic factor (CNTF) are "4-helical bundle" cytokines of the IL-6 type family of neuropoietic and hematopoietic cytokines. IL-6 signals by induction of a gp130 homodimer (e.g. IL-6), whereas CNTF and leukemia inhibitory factor (LIF) signal via a heterodimer of gp130 and LIF receptor (LIFR). Despite binding to the same receptor component (gp130) and a similar protein structure, IL-6 and CNTF share only 6% sequence identity. Using molecular modeling we defined a putative LIFR binding epitope on CNTF that consists of three distinct regions (C-terminal A-helix/N-terminal AB loop, BC loop, C-terminal CD-loop/N-terminal D-helix). A corresponding gp130-binding site on IL-6 was exchanged with this epitope. The resulting IL-6/CNTF chimera lost the capacity to signal via gp130 on cells without LIFR, but acquired the ability to signal via the gp130/LIFR heterodimer and STAT3 on responsive cells. Besides identifying a specific LIFR binding epitope on CNTF, our results suggest that receptor recognition sites of cytokines are organized as modules that are exchangeable even between cytokines with limited sequence homology.  (+info)

Binding of leukemia inhibitory factor (LIF) to mutants of its low affinity receptor, gp190, reveals a LIF binding site outside and interactions between the two cytokine binding domains. (7/181)

The gp190 transmembrane protein, the low affinity receptor for the leukemia inhibitory factor (LIF), belongs to the hematopoietin family of receptors characterized by the cytokine binding domain (CBD). gp190 is one of the very few members of this family to contain two such domains. The membrane-proximal CBD (herein called D2) is separated from the membrane-distal one (called D1) by an immunoglobulin-like (Ig) domain and is followed by three fibronectin type III repeats. We used truncated gp190 mutants and a blocking anti-gp190 monoclonal antibody to study the role of these repeats in low affinity receptor function. Our results showed that the D1Ig region was involved in LIF binding, while D2 appeared to be crucial for the proper folding of D1, suggesting functionally important interactions between the two CBDs in the wild-type protein. In addition, a point mutation in the carboxyl terminus of the Ig region strongly impaired ligand binding. These findings suggest that at least two distinct sites, both located within the D1Ig region, are involved in LIF binding to gp190, and more generally, that ligand binding sites on these receptors may well be located outside the canonical CBDs.  (+info)

Leukemia inhibitory factor and its receptor promote adipocyte differentiation via the mitogen-activated protein kinase cascade. (8/181)

Extracellular factors and intracellular signaling pathways involved in early events of adipocyte differentiation are poorly defined. It is shown herein that expression of leukemia inhibitory factor (LIF) and LIF receptor is developmentally regulated during adipocyte differentiation. Preadipocytes secrete bioactive LIF, and an antagonist of LIF receptor inhibits adipogenesis. Genetically modified embryonic stem (ES) cells combined with culture conditions to commit stem cells into the adipocyte lineage were used to examine the requirement of LIF receptor during in vitro development of adipose cells. The capacity of embryoid bodies derived from lifr(-/-) ES cells to undergo adipocyte differentiation is dramatically reduced. LIF addition stimulates adipocyte differentiation of Ob1771 and 3T3-F442A preadipocytes and that of peroxisome proliferator-activated receptor gamma2 ligand-treated mouse embryonic fibroblasts. Expression of the early adipogenic transcription factors C/EBPbeta and C/EBPdelta is rapidly stimulated following exposure of preadipose cells to LIF. The selective inhibitors of mitogen-activated protein kinase kinase, i.e. PD98059 and U0126, inhibit LIF-induced C/EBP gene expression and prevent adipocyte differentiation induced by LIF. These results are in favor of a model that implicates stimulation of LIF receptor in the commitment of preadipocytes to undergo terminal differentiation by controlling the early expression of C/EBPbeta and C/EBPdelta genes via the mitogen-activated protein kinase cascade.  (+info)

Leukemia Inhibitory Factor Receptor alpha Subunit (LIFR-α) is a protein that forms part of the Leukemia Inhibitory Factor (LIF) receptor complex. LIF is a cytokine, or signaling molecule, that plays important roles in various biological processes such as cell differentiation, survival, and proliferation.

The LIFR-α subunit combines with the glycoprotein 130 (gp130) subunit to form a functional receptor for LIF. When LIF binds to this receptor complex, it triggers a series of intracellular signaling events that ultimately regulate gene expression and cell behavior.

Mutations in the LIFR-α gene have been associated with certain diseases, including some forms of cancer. For example, reduced expression of LIFR-α has been observed in leukemia cells, suggesting that it may play a role in the development or progression of this disease. However, more research is needed to fully understand the functional significance of LIFR-α and its role in human health and disease.

OSM-LIF receptors are a type of cell surface receptor that bind to the cytokines Oncostatin M (OSM) and Leukemia Inhibitory Factor (LIF). These receptors are part of the class I cytokine receptor family, which share a common structure and signaling mechanism.

The OSM-LIF receptor is composed of two subunits: gp130 and LIFR (LIF receptor beta). The binding of OSM or LIF to the extracellular domain of the LIFR subunit results in the recruitment of gp130, which then activates a series of intracellular signaling pathways, including the JAK-STAT and MAPK pathways.

OSM-LIF receptors play important roles in various biological processes, such as cell proliferation, differentiation, survival, and inflammation. Dysregulation of OSM-LIF signaling has been implicated in several diseases, including cancer, autoimmune disorders, and neurological disorders. Therefore, targeting OSM-LIF receptors has emerged as a potential therapeutic strategy for these conditions.

Leukemia Inhibitory Factor (LIF) is a protein with pleiotropic functions, acting as a cytokine that plays a crucial role in various biological processes. Its name originates from its initial discovery as a factor that inhibits the proliferation of certain leukemic cells. However, LIF has been found to have a much broader range of activities beyond just inhibiting leukemia cells.

LIF is a member of the interleukin-6 (IL-6) family of cytokines and binds to a heterodimeric receptor complex consisting of the LIF receptor (LIFR) and glycoprotein 130 (gp130). The activation of this receptor complex triggers several downstream signaling pathways, including the Janus kinase (JAK)-signal transducer and activator of transcription (STAT), mitogen-activated protein kinase (MAPK), and phosphoinositide 3-kinase (PI3K) pathways.

Some of the key functions of LIF include:

1. Embryonic development: During embryogenesis, LIF is essential for maintaining the pluripotency of embryonic stem cells and promoting their self-renewal in the early stages of development. It also plays a role in implantation and trophoblast differentiation during pregnancy.
2. Hematopoiesis: In the hematopoietic system, LIF supports the survival and proliferation of hematopoietic stem cells (HSCs) and regulates their differentiation into various blood cell lineages.
3. Neuroprotection and neurogenesis: LIF has been shown to have neuroprotective effects in various models of neuronal injury and disease, including spinal cord injury, stroke, and Alzheimer's disease. It also promotes the survival and differentiation of neural progenitor cells, contributing to adult neurogenesis.
4. Inflammation: LIF is involved in regulating immune responses and inflammation by modulating the activation and function of various immune cells, such as T cells, B cells, macrophages, and dendritic cells.
5. Pain regulation: LIF has been implicated in pain processing and modulation, with studies suggesting that it may contribute to both acute and chronic pain conditions.
6. Cancer: LIF has complex roles in cancer biology, acting as a tumor suppressor in some contexts while promoting tumor growth and progression in others. It can regulate various aspects of cancer cell behavior, including proliferation, survival, migration, and invasion.

In summary, LIF is a pleiotropic cytokine with diverse functions in various biological processes, including embryonic development, hematopoiesis, neuroprotection, inflammation, pain regulation, and cancer. Its multifaceted roles highlight the importance of understanding its precise mechanisms of action in different contexts to harness its therapeutic potential for various diseases.

Ciliary Neurotrophic Factor Receptor alpha Subunit (CNTFRα) is a protein that forms part of the Ciliary Neurotrophic Factor (CNTF) receptor complex. CNTF is a neurotrophin, which is a type of signaling molecule that supports the survival and differentiation of neurons. The CNTF receptor complex consists of three subunits: CNTFRα, LIFRβ, and gp130.

CNTFRα is a transmembrane protein that is primarily expressed in cells of the nervous system, including neurons and glial cells. It serves as the primary binding site for CNTF, allowing the neurotrophin to initiate signaling pathways within the cell. The interaction between CNTF and CNTFRα leads to the recruitment of LIFRβ and gp130, which form a functional receptor complex that activates various intracellular signaling cascades, including the JAK-STAT and MAPK pathways.

CNTF and its receptor complex play critical roles in the development and maintenance of the nervous system, particularly in the survival and differentiation of motor neurons. Mutations in the genes encoding CNTFRα or other components of the CNTF receptor complex have been associated with various neurodevelopmental disorders, including hereditary sensory neuropathies and forms of spinal muscular atrophy.

Cytokine receptors are specialized protein molecules found on the surface of cells that selectively bind to specific cytokines. Cytokines are signaling molecules used for communication between cells, and they play crucial roles in regulating immune responses, inflammation, hematopoiesis, and cell survival.

Cytokine receptors have specific binding sites that recognize and interact with the corresponding cytokines. This interaction triggers a series of intracellular signaling events that ultimately lead to changes in gene expression and various cellular responses. Cytokine receptors can be found on many different types of cells, including immune cells, endothelial cells, and structural cells like fibroblasts.

Cytokine receptors are typically composed of multiple subunits, which may include both extracellular and intracellular domains. The extracellular domain is responsible for cytokine binding, while the intracellular domain is involved in signal transduction. Cytokine receptors can be classified into several families based on their structural features and signaling mechanisms, such as the hematopoietic cytokine receptor family, the interferon receptor family, the tumor necrosis factor receptor family, and the interleukin-1 receptor family.

Dysregulation of cytokine receptors and their signaling pathways has been implicated in various diseases, including autoimmune disorders, chronic inflammation, and cancer. Therefore, understanding the biology of cytokine receptors is essential for developing targeted therapies to treat these conditions.

Growth inhibitors, in a medical context, refer to substances or agents that reduce or prevent the growth and proliferation of cells. They play an essential role in regulating normal cellular growth and can be used in medical treatments to control the excessive growth of unwanted cells, such as cancer cells.

There are two main types of growth inhibitors:

1. Endogenous growth inhibitors: These are naturally occurring molecules within the body that help regulate cell growth and division. Examples include retinoids, which are vitamin A derivatives, and interferons, which are signaling proteins released by host cells in response to viruses.

2. Exogenous growth inhibitors: These are synthetic or natural substances from outside the body that can be used to inhibit cell growth. Many chemotherapeutic agents and targeted therapies for cancer treatment fall into this category. They work by interfering with specific pathways involved in cell division, such as DNA replication or mitosis, or by inducing apoptosis (programmed cell death) in cancer cells.

It is important to note that growth inhibitors may also affect normal cells, which can lead to side effects during treatment. The challenge for medical researchers is to develop targeted therapies that specifically inhibit the growth of abnormal cells while minimizing harm to healthy cells.

Cytokine receptor gp130 is a protein that is a component of several cytokine receptors, including those for interleukin-6 (IL-6), IL-11, leukemia inhibitory factor (LIF), oncostatin M (OSM), cardiotrophin-1 (CT-1), and ciliary neurotrophic factor (CNTF). It is a transmembrane protein that plays an important role in signal transduction and activation of various cellular responses, such as immune response, cell growth, differentiation, and apoptosis.

The gp130 receptor forms a complex with other cytokine-specific receptors when a ligand binds to them. This interaction leads to the activation of intracellular signaling pathways, including the JAK/STAT (Janus kinase/signal transducer and activator of transcription) pathway, which ultimately regulates gene expression and cellular responses.

Mutations in the gp130 receptor have been associated with various diseases, such as primary immunodeficiency, leukemia, and solid tumors. Therefore, understanding the structure and function of gp130 is crucial for developing new therapeutic strategies to target cytokine-mediated signaling pathways in disease treatment.

Oncostatin M (OSM) receptors are a type of cell surface receptor that bind to and mediate the effects of the cytokine Oncostatin M. OSM is a member of the interleukin-6 (IL-6) family of cytokines, which play important roles in the regulation of immune responses, inflammation, and hematopoiesis.

There are two types of OSM receptors: type I and type II. Type I OSM receptors are found on a variety of cells, including fibroblasts, endothelial cells, and some hematopoietic cells. They consist of a complex of the OSM receptor beta (OSMRβ) chain and the gp130 chain, which is also a component of other IL-6 family receptors. Type II OSM receptors are found on hematopoietic cells, such as monocytes and macrophages, and consist of a complex of the OSMRβ chain and the leukemia inhibitory factor receptor alpha (LIFRα) chain.

Activation of OSM receptors leads to the activation of several signaling pathways, including the Janus kinase (JAK)/signal transducer and activator of transcription (STAT), mitogen-activated protein kinase (MAPK), and phosphoinositide 3-kinase (PI3K) pathways. These pathways regulate a variety of cellular responses, including proliferation, differentiation, survival, and inflammatory responses.

Dysregulation of OSM signaling has been implicated in several diseases, including cancer, fibrosis, and autoimmune disorders. Therefore, targeting OSM receptors or their downstream signaling pathways may represent a potential therapeutic strategy for these conditions.

The platelet-derived growth factor receptor alpha (PDGFR-α) is a type of cell surface receptor that binds to specific proteins called platelet-derived growth factors (PDGFs). PDGFR-α is a transmembrane tyrosine kinase receptor, which means it has an intracellular portion containing tyrosine kinase enzymatic activity.

When PDGFs bind to PDGFR-α, they induce receptor dimerization and activation of the tyrosine kinase domain, leading to autophosphorylation of specific tyrosine residues on the receptor. This triggers a signaling cascade that promotes cell growth, proliferation, survival, and migration. PDGFR-α is primarily expressed in cells of mesenchymal origin, such as fibroblasts, smooth muscle cells, and glial cells.

PDGFR-α plays crucial roles during embryonic development, wound healing, and tissue repair. However, aberrant activation or mutations in PDGFR-α have been implicated in various pathological conditions, including cancer, atherosclerosis, and fibrotic disorders. Therefore, PDGFR-α is an important target for therapeutic interventions in these diseases.

Ciliary Neurotrophic Factor (CNTF) is a protein that belongs to the neurotrophin family and plays a crucial role in the survival, development, and maintenance of certain neurons in the nervous system. It was initially identified as a factor that supports the survival of ciliary ganglion neurons, hence its name.

CNTF has a broad range of effects on various types of neurons, including motor neurons, sensory neurons, and autonomic neurons. It promotes the differentiation and survival of these cells during embryonic development and helps maintain their function in adulthood. CNTF also exhibits neuroprotective properties, protecting neurons from various forms of injury and degeneration.

In addition to its role in the nervous system, CNTF has been implicated in the regulation of immune responses and energy metabolism. It is primarily produced by glial cells, such as astrocytes and microglia, in response to inflammation or injury. The receptors for CNTF are found on various cell types, including neurons, muscle cells, and immune cells.

Overall, CNTF is an essential protein that plays a critical role in the development, maintenance, and protection of the nervous system. Its functions have attracted significant interest in the context of neurodegenerative diseases and potential therapeutic applications.

Oncostatin M is a cytokine, specifically a member of the interleukin-6 (IL-6) family. It is produced by various cells including T lymphocytes, natural killer cells, and some tumor cells. Oncostatin M plays roles in several biological processes such as inflammation, hematopoiesis, and immune responses. In the context of cancer, it can have both pro-tumoral and anti-tumoral effects depending on the type of cancer and microenvironment. It has been studied for its potential role in cancer therapy due to its ability to inhibit the growth of some tumor cells.

Ciliary Neurotrophic Factor (CNTF) is a neurotrophic factor, which is a type of protein that supports the growth, survival, and differentiation of neurons. CNTF specifically plays a role in the survival and maintenance of motor neurons, which are nerve cells that control voluntary muscle movements.

A receptor is a molecule on the surface of a cell that receives chemical signals from outside the cell. The Ciliary Neurotrophic Factor Receptor (CNTFR) is a complex of three proteins: CNTFRα, LIFRβ, and gp130. When CNTF binds to its receptor, it activates a series of intracellular signaling pathways that promote the survival and differentiation of motor neurons.

In summary, the medical definition of 'Receptor, Ciliary Neurotrophic Factor' is a protein complex on the surface of a cell that binds to CNTF and activates signaling pathways that support the survival and maintenance of motor neurons.

Lymphokines are a type of cytokines that are produced and released by activated lymphocytes, a type of white blood cell, in response to an antigenic stimulation. They play a crucial role in the regulation of immune responses and inflammation. Lymphokines can mediate various biological activities such as chemotaxis, activation, proliferation, and differentiation of different immune cells including lymphocytes, monocytes, macrophages, and eosinophils. Examples of lymphokines include interleukins (ILs), interferons (IFNs), tumor necrosis factor (TNF), and colony-stimulating factors (CSFs).

The oncostatin M receptor beta subunit (OSMRβ) is a protein that forms part of the oncostatin M receptor complex. Oncostatin M is a cytokine, a type of signaling molecule used for communication between cells, and OSMRβ is one of the proteins that helps to transmit those signals into the cell. Specifically, OSMRβ combines with the glycoprotein 130 (gp130) protein to form a functional receptor for oncostatin M. This receptor complex activates several signaling pathways within the cell, most notably the JAK-STAT and MAPK/ERK pathways, which can influence various cellular processes such as proliferation, differentiation, and apoptosis (programmed cell death). OSMRβ is found on the surface of many types of cells, and its dysregulation has been implicated in several diseases, including cancer and inflammatory disorders.

Interleukin-6 (IL-6) is a cytokine, a type of protein that plays a crucial role in communication between cells, especially in the immune system. It is produced by various cells including T-cells, B-cells, fibroblasts, and endothelial cells in response to infection, injury, or inflammation.

IL-6 has diverse effects on different cell types. In the immune system, it stimulates the growth and differentiation of B-cells into plasma cells that produce antibodies. It also promotes the activation and survival of T-cells. Moreover, IL-6 plays a role in fever induction by acting on the hypothalamus to raise body temperature during an immune response.

In addition to its functions in the immune system, IL-6 has been implicated in various physiological processes such as hematopoiesis (the formation of blood cells), bone metabolism, and neural development. However, abnormal levels of IL-6 have also been associated with several diseases, including autoimmune disorders, chronic inflammation, and cancer.

STAT3 (Signal Transducer and Activator of Transcription 3) is a transcription factor protein that plays a crucial role in signal transduction and gene regulation. It is activated through phosphorylation by various cytokines and growth factors, which leads to its dimerization, nuclear translocation, and binding to specific DNA sequences. Once bound to the DNA, STAT3 regulates the expression of target genes involved in various cellular processes such as proliferation, differentiation, survival, and angiogenesis. Dysregulation of STAT3 has been implicated in several diseases, including cancer, autoimmune disorders, and inflammatory conditions.

Signal transduction is the process by which a cell converts an extracellular signal, such as a hormone or neurotransmitter, into an intracellular response. This involves a series of molecular events that transmit the signal from the cell surface to the interior of the cell, ultimately resulting in changes in gene expression, protein activity, or metabolism.

The process typically begins with the binding of the extracellular signal to a receptor located on the cell membrane. This binding event activates the receptor, which then triggers a cascade of intracellular signaling molecules, such as second messengers, protein kinases, and ion channels. These molecules amplify and propagate the signal, ultimately leading to the activation or inhibition of specific cellular responses.

Signal transduction pathways are highly regulated and can be modulated by various factors, including other signaling molecules, post-translational modifications, and feedback mechanisms. Dysregulation of these pathways has been implicated in a variety of diseases, including cancer, diabetes, and neurological disorders.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Macrophage migration-inhibitory factors (MIFs) are a group of proteins that were initially identified for their ability to inhibit the random migration of macrophages. However, subsequent research has revealed that MIFs have diverse functions in the immune system and other biological processes. They play crucial roles in inflammation, immunoregulation, and stress responses.

MIF is constitutively expressed and secreted by various cell types, including T-cells, macrophages, epithelial cells, endothelial cells, and neurons. It functions as a proinflammatory cytokine that can counteract the anti-inflammatory effects of glucocorticoids. MIF is involved in several signaling pathways and contributes to various physiological and pathophysiological processes, such as cell growth, differentiation, and survival.

Dysregulation of MIF has been implicated in numerous diseases, including autoimmune disorders, cancer, cardiovascular diseases, and neurodegenerative conditions. Therefore, understanding the functions and regulation of MIFs is essential for developing novel therapeutic strategies to target these diseases.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

CD (cluster of differentiation) antigens are cell-surface proteins that are expressed on leukocytes (white blood cells) and can be used to identify and distinguish different subsets of these cells. They are important markers in the field of immunology and hematology, and are commonly used to diagnose and monitor various diseases, including cancer, autoimmune disorders, and infectious diseases.

CD antigens are designated by numbers, such as CD4, CD8, CD19, etc., which refer to specific proteins found on the surface of different types of leukocytes. For example, CD4 is a protein found on the surface of helper T cells, while CD8 is found on cytotoxic T cells.

CD antigens can be used as targets for immunotherapy, such as monoclonal antibody therapy, in which antibodies are designed to bind to specific CD antigens and trigger an immune response against cancer cells or infected cells. They can also be used as markers to monitor the effectiveness of treatments and to detect minimal residual disease (MRD) after treatment.

It's important to note that not all CD antigens are exclusive to leukocytes, some can be found on other cell types as well, and their expression can vary depending on the activation state or differentiation stage of the cells.

Membrane glycoproteins are proteins that contain oligosaccharide chains (glycans) covalently attached to their polypeptide backbone. They are integral components of biological membranes, spanning the lipid bilayer and playing crucial roles in various cellular processes.

The glycosylation of these proteins occurs in the endoplasmic reticulum (ER) and Golgi apparatus during protein folding and trafficking. The attached glycans can vary in structure, length, and composition, which contributes to the diversity of membrane glycoproteins.

Membrane glycoproteins can be classified into two main types based on their orientation within the lipid bilayer:

1. Type I (N-linked): These glycoproteins have a single transmembrane domain and an extracellular N-terminus, where the oligosaccharides are predominantly attached via asparagine residues (Asn-X-Ser/Thr sequon).
2. Type II (C-linked): These glycoproteins possess two transmembrane domains and an intracellular C-terminus, with the oligosaccharides linked to tryptophan residues via a mannose moiety.

Membrane glycoproteins are involved in various cellular functions, such as:

* Cell adhesion and recognition
* Receptor-mediated signal transduction
* Enzymatic catalysis
* Transport of molecules across membranes
* Cell-cell communication
* Immunological responses

Some examples of membrane glycoproteins include cell surface receptors (e.g., growth factor receptors, cytokine receptors), adhesion molecules (e.g., integrins, cadherins), and transporters (e.g., ion channels, ABC transporters).

Hypereosinophilic Syndrome (HES) is a group of disorders characterized by persistent eosinophilia (an abnormal increase in the number of eosinophils, a type of white blood cell) leading to organ damage. The eosinophil count in the peripheral blood is typically greater than 1500 cells/μL. HES can affect various organs, including the heart, skin, nervous system, and digestive tract, causing symptoms such as shortness of breath, cough, fatigue, skin rashes, muscle weakness, and abdominal pain. The exact cause of HES is not fully understood, but it is thought to be related to abnormal production or activation of eosinophils. Treatment may include corticosteroids, immunosuppressive drugs, and targeted therapies that reduce eosinophil levels.

Leukemia is a type of cancer that originates from the bone marrow - the soft, inner part of certain bones where new blood cells are made. It is characterized by an abnormal production of white blood cells, known as leukocytes or blasts. These abnormal cells accumulate in the bone marrow and interfere with the production of normal blood cells, leading to a decrease in red blood cells (anemia), platelets (thrombocytopenia), and healthy white blood cells (leukopenia).

There are several types of leukemia, classified based on the specific type of white blood cell affected and the speed at which the disease progresses:

1. Acute Leukemias - These types of leukemia progress rapidly, with symptoms developing over a few weeks or months. They involve the rapid growth and accumulation of immature, nonfunctional white blood cells (blasts) in the bone marrow and peripheral blood. The two main categories are:
- Acute Lymphoblastic Leukemia (ALL) - Originates from lymphoid progenitor cells, primarily affecting children but can also occur in adults.
- Acute Myeloid Leukemia (AML) - Develops from myeloid progenitor cells and is more common in older adults.

2. Chronic Leukemias - These types of leukemia progress slowly, with symptoms developing over a period of months to years. They involve the production of relatively mature, but still abnormal, white blood cells that can accumulate in large numbers in the bone marrow and peripheral blood. The two main categories are:
- Chronic Lymphocytic Leukemia (CLL) - Affects B-lymphocytes and is more common in older adults.
- Chronic Myeloid Leukemia (CML) - Originates from myeloid progenitor cells, characterized by the presence of a specific genetic abnormality called the Philadelphia chromosome. It can occur at any age but is more common in middle-aged and older adults.

Treatment options for leukemia depend on the type, stage, and individual patient factors. Treatments may include chemotherapy, targeted therapy, immunotherapy, stem cell transplantation, or a combination of these approaches.

The Epidermal Growth Factor Receptor (EGFR) is a type of receptor found on the surface of many cells in the body, including those of the epidermis or outer layer of the skin. It is a transmembrane protein that has an extracellular ligand-binding domain and an intracellular tyrosine kinase domain.

EGFR plays a crucial role in various cellular processes such as proliferation, differentiation, migration, and survival. When EGF (Epidermal Growth Factor) or other ligands bind to the extracellular domain of EGFR, it causes the receptor to dimerize and activate its intrinsic tyrosine kinase activity. This leads to the autophosphorylation of specific tyrosine residues on the receptor, which in turn recruits and activates various downstream signaling molecules, resulting in a cascade of intracellular signaling events that ultimately regulate gene expression and cell behavior.

Abnormal activation of EGFR has been implicated in several human diseases, including cancer. Overexpression or mutation of EGFR can lead to uncontrolled cell growth and division, angiogenesis, and metastasis, making it an important target for cancer therapy.

Cytokines are a broad and diverse category of small signaling proteins that are secreted by various cells, including immune cells, in response to different stimuli. They play crucial roles in regulating the immune response, inflammation, hematopoiesis, and cellular communication.

Cytokines mediate their effects by binding to specific receptors on the surface of target cells, which triggers intracellular signaling pathways that ultimately result in changes in gene expression, cell behavior, and function. Some key functions of cytokines include:

1. Regulating the activation, differentiation, and proliferation of immune cells such as T cells, B cells, natural killer (NK) cells, and macrophages.
2. Coordinating the inflammatory response by recruiting immune cells to sites of infection or tissue damage and modulating their effector functions.
3. Regulating hematopoiesis, the process of blood cell formation in the bone marrow, by controlling the proliferation, differentiation, and survival of hematopoietic stem and progenitor cells.
4. Modulating the development and function of the nervous system, including neuroinflammation, neuroprotection, and neuroregeneration.

Cytokines can be classified into several categories based on their structure, function, or cellular origin. Some common types of cytokines include interleukins (ILs), interferons (IFNs), tumor necrosis factors (TNFs), chemokines, colony-stimulating factors (CSFs), and transforming growth factors (TGFs). Dysregulation of cytokine production and signaling has been implicated in various pathological conditions, such as autoimmune diseases, chronic inflammation, cancer, and neurodegenerative disorders.

Interleukin-6 Receptor alpha subunit (IL-6Rα or CD126) is a protein that plays a crucial role in the immune response and inflammation. It is a transmembrane receptor component responsible for binding to the cytokine Interleukin-6 (IL-6), which then forms a complex that activates intracellular signaling pathways, primarily through the Janus kinase (JAK) and signal transducer and activator of transcription 3 (STAT3) signaling cascade.

The activation of these pathways leads to various cellular responses, including the regulation of immune cells, hematopoiesis, inflammation, and acute phase protein synthesis in the liver. IL-6Rα is expressed on a variety of cells, such as hepatocytes, leukocytes, and some epithelial cells.

Interleukin-6 Receptor alpha subunit also exists in a soluble form (sIL-6R), which can be generated by proteolytic cleavage or alternative splicing of the membrane-bound receptor. The soluble receptor can bind to IL-6 and facilitate its interaction with gp130, another component of the IL-6 receptor complex, on cells that do not express IL-6Rα. This process is called trans-signaling and allows for a broader range of cellular responses to IL-6 signaling.

Dysregulation of IL-6 and its signaling pathways have been implicated in various diseases, such as autoimmune disorders, chronic inflammation, and cancer. Therefore, targeting the IL-6/IL-6Rα signaling axis has emerged as a potential therapeutic strategy for treating these conditions.

Estrogen Receptor alpha (ERα) is a type of nuclear receptor protein that is activated by the hormone estrogen. It is encoded by the gene ESR1 and is primarily expressed in the cells of the reproductive system, breast, bone, liver, heart, and brain tissue.

When estrogen binds to ERα, it causes a conformational change in the receptor, which allows it to dimerize and translocate to the nucleus. Once in the nucleus, ERα functions as a transcription factor, binding to specific DNA sequences called estrogen response elements (EREs) and regulating the expression of target genes.

ERα plays important roles in various physiological processes, including the development and maintenance of female reproductive organs, bone homeostasis, and lipid metabolism. It is also a critical factor in the growth and progression of certain types of breast cancer, making ERα status an important consideration in the diagnosis and treatment of this disease.

Interleukin-5 (IL-5) receptors are a type of cell surface receptor that bind to and respond to the cytokine IL-5. These receptors are found on the surface of certain immune cells, including eosinophils, basophils, and some types of T cells.

The IL-5 receptor is a heterodimer, meaning it is composed of two different subunits: the alpha (IL-5Rα) and beta (IL-5Rβ) chains. The alpha chain is specific to IL-5 and confers binding specificity, while the beta chain is shared with other cytokine receptors and mediates signal transduction.

Activation of the IL-5 receptor leads to a variety of cellular responses, including proliferation, differentiation, and survival of eosinophils and basophils. These cells play important roles in the immune response, particularly in the defense against parasitic infections and in allergic reactions. Dysregulation of IL-5 signaling has been implicated in several diseases, including asthma, chronic obstructive pulmonary disease (COPD), and eosinophilic disorders.

Gastrointestinal Stromal Tumors (GISTs) are rare, but potentially aggressive neoplasms that arise from the interstitial cells of Cajal or their precursors in the gastrointestinal tract. These tumors can be found anywhere along the digestive tract, including the stomach, small intestine, colon, and rectum. They are usually characterized by the presence of specific genetic mutations, most commonly involving the KIT (CD117) or PDGFRA genes. GISTs can vary in size and may present with a range of symptoms, such as abdominal pain, bleeding, or obstruction, depending on their location and size. Treatment typically involves surgical resection, and in some cases, targeted therapy with kinase inhibitors.

Granulocyte-macrophage colony-stimulating factor (GM-CSF) receptors are a type of cell surface receptor found on hematopoietic cells, which are involved in the production and activation of white blood cells, specifically granulocytes and macrophages.

The GM-CSF receptor is a heterodimer, composed of two distinct subunits: the alpha (GM-CSF RA) and the beta (GM-CSF RB or CD131) chains. The alpha chain is specific to GM-CSF and binds to it with low affinity, while the beta chain is shared with other cytokine receptors, such as IL-3 and IL-5 receptors, and increases the binding affinity and signal transduction of the receptor complex.

Once GM-CSF binds to its receptor, it triggers a series of intracellular signaling events that promote the proliferation, differentiation, and activation of granulocytes and macrophages. These cells play crucial roles in the immune system's response to infection and inflammation, making GM-CSF and its receptors important targets for therapeutic intervention in various immunological disorders.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.

Macromolecular substances, also known as macromolecules, are large, complex molecules made up of repeating subunits called monomers. These substances are formed through polymerization, a process in which many small molecules combine to form a larger one. Macromolecular substances can be naturally occurring, such as proteins, DNA, and carbohydrates, or synthetic, such as plastics and synthetic fibers.

In the context of medicine, macromolecular substances are often used in the development of drugs and medical devices. For example, some drugs are designed to bind to specific macromolecules in the body, such as proteins or DNA, in order to alter their function and produce a therapeutic effect. Additionally, macromolecular substances may be used in the creation of medical implants, such as artificial joints and heart valves, due to their strength and durability.

It is important for healthcare professionals to have an understanding of macromolecular substances and how they function in the body, as this knowledge can inform the development and use of medical treatments.

The Interleukin-5 Receptor alpha Subunit (IL-5Rα) is a protein that forms part of the Type I cytokine receptor, specifically for the interleukin-5 (IL-5) cytokine. This receptor is found on the surface of hematopoietic cells, such as eosinophils and basophils. The binding of IL-5 to the IL-5Rα subunit initiates intracellular signaling cascades that regulate the growth, activation, differentiation, and survival of eosinophils and basophils, which are crucial in the immune response against parasitic infections and allergic reactions. Mutations in the gene encoding IL-5Rα can lead to altered immune responses and diseases such as hypereosinophilic syndromes.

"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.

Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.

It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.

Acute myeloid leukemia (AML) is a type of cancer that originates in the bone marrow, the soft inner part of certain bones where new blood cells are made. In AML, the immature cells, called blasts, in the bone marrow fail to mature into normal blood cells. Instead, these blasts accumulate and interfere with the production of normal blood cells, leading to a shortage of red blood cells (anemia), platelets (thrombocytopenia), and normal white blood cells (leukopenia).

AML is called "acute" because it can progress quickly and become severe within days or weeks without treatment. It is a type of myeloid leukemia, which means that it affects the myeloid cells in the bone marrow. Myeloid cells are a type of white blood cell that includes monocytes and granulocytes, which help fight infection and defend the body against foreign invaders.

In AML, the blasts can build up in the bone marrow and spread to other parts of the body, including the blood, lymph nodes, liver, spleen, and brain. This can cause a variety of symptoms, such as fatigue, fever, frequent infections, easy bruising or bleeding, and weight loss.

AML is typically treated with a combination of chemotherapy, radiation therapy, and/or stem cell transplantation. The specific treatment plan will depend on several factors, including the patient's age, overall health, and the type and stage of the leukemia.

Proto-oncogene proteins c-kit, also known as CD117 or stem cell factor receptor, are transmembrane receptor tyrosine kinases that play crucial roles in various biological processes, including cell survival, proliferation, differentiation, and migration. They are encoded by the c-KIT gene located on human chromosome 4q12.

These proteins consist of an extracellular ligand-binding domain, a transmembrane domain, and an intracellular tyrosine kinase domain. The binding of their ligand, stem cell factor (SCF), leads to receptor dimerization, autophosphorylation, and activation of several downstream signaling pathways such as PI3K/AKT, MAPK/ERK, and JAK/STAT.

Abnormal activation or mutation of c-kit proto-oncogene proteins has been implicated in the development and progression of various malignancies, including gastrointestinal stromal tumors (GISTs), acute myeloid leukemia (AML), mast cell diseases, and melanoma. Targeted therapies against c-kit, such as imatinib mesylate (Gleevec), have shown promising results in the treatment of these malignancies.

Nucleic acids are biological macromolecules composed of linear chains of nucleotides. They play crucial roles in the structure and function of cells, serving as the primary information-carrying molecules in all known forms of life. The two main types of nucleic acids are deoxyribonucleic acid (DNA) and ribonucleic acid (RNA). DNA is responsible for storing genetic information in a stable form that can be passed down from generation to generation, while RNA plays a key role in translating the genetic code stored in DNA into functional proteins.

Each nucleotide consists of a sugar molecule, a phosphate group, and a nitrogenous base. The sugar in DNA is deoxyribose, while in RNA it is ribose. The nitrogenous bases found in both DNA and RNA include adenine (A), guanine (G), and cytosine (C). Thymine (T) is found in DNA, but uracil (U) takes its place in RNA. These nucleotides are linked together by phosphodiester bonds between the sugar of one nucleotide and the phosphate group of another, forming a long, helical structure with backbones made up of alternating sugar and phosphate groups.

The sequence of these nitrogenous bases along the nucleic acid chain encodes genetic information in the form of codons, which are sets of three consecutive bases that specify particular amino acids or signals for protein synthesis. This information is used to direct the synthesis of proteins through a process called transcription (converting DNA to RNA) and translation (converting RNA to protein).

In summary, nucleic acids are essential biomolecules composed of chains of nucleotides that store, transmit, and express genetic information in cells. They consist of two main types: DNA and RNA, which differ in their sugar type, nitrogenous bases, and functions.

Polycystic Kidney Disease (PKD) is a genetic disorder characterized by the growth of multiple cysts in the kidneys. These cysts are fluid-filled sacs that can vary in size and can multiply, leading to enlarged kidneys. The increased size and number of cysts can result in reduced kidney function, high blood pressure, and eventually kidney failure.

There are two main types of PKD: Autosomal Dominant Polycystic Kidney Disease (ADPKD) and Autosomal Recessive Polycystic Kidney Disease (ARPKD). ADPKD is the most common form, affecting approximately 1 in every 500 people. It typically develops in adulthood. On the other hand, ARPKD is a rarer form, affecting about 1 in every 20,000 children, and it often presents in infancy or early childhood.

In addition to kidney problems, PKD can also affect other organs, such as the liver and the heart. It's important to note that while there is no cure for PKD, various treatments can help manage symptoms and slow down the progression of the disease.

ATP-binding cassette (ABC) transporters are a family of membrane proteins that utilize the energy from ATP hydrolysis to transport various substrates across extra- and intracellular membranes. These transporters play crucial roles in several biological processes, including detoxification, drug resistance, nutrient uptake, and regulation of cellular cholesterol homeostasis.

The structure of ABC transporters consists of two nucleotide-binding domains (NBDs) that bind and hydrolyze ATP, and two transmembrane domains (TMDs) that form the substrate-translocation pathway. The NBDs are typically located adjacent to each other in the cytoplasm, while the TMDs can be either integral membrane domains or separate structures associated with the membrane.

The human genome encodes 48 distinct ABC transporters, which are classified into seven subfamilies (ABCA-ABCG) based on their sequence similarity and domain organization. Some well-known examples of ABC transporters include P-glycoprotein (ABCB1), multidrug resistance protein 1 (ABCC1), and breast cancer resistance protein (ABCG2).

Dysregulation or mutations in ABC transporters have been implicated in various diseases, such as cystic fibrosis, neurological disorders, and cancer. In cancer, overexpression of certain ABC transporters can contribute to drug resistance by actively effluxing chemotherapeutic agents from cancer cells, making them less susceptible to treatment.

Bone marrow is the spongy tissue found inside certain bones in the body, such as the hips, thighs, and vertebrae. It is responsible for producing blood-forming cells, including red blood cells, white blood cells, and platelets. There are two types of bone marrow: red marrow, which is involved in blood cell production, and yellow marrow, which contains fatty tissue.

Red bone marrow contains hematopoietic stem cells, which can differentiate into various types of blood cells. These stem cells continuously divide and mature to produce new blood cells that are released into the circulation. Red blood cells carry oxygen throughout the body, white blood cells help fight infections, and platelets play a crucial role in blood clotting.

Bone marrow also serves as a site for immune cell development and maturation. It contains various types of immune cells, such as lymphocytes, macrophages, and dendritic cells, which help protect the body against infections and diseases.

Abnormalities in bone marrow function can lead to several medical conditions, including anemia, leukopenia, thrombocytopenia, and various types of cancer, such as leukemia and multiple myeloma. Bone marrow aspiration and biopsy are common diagnostic procedures used to evaluate bone marrow health and function.

Autosomal Dominant Polycystic Kidney Disease (ADPKD) is a genetic disorder characterized by the growth of multiple cysts in the kidneys. These cysts are fluid-filled sacs that can vary in size and can multiply, leading to enlarged kidneys. The increased size and number of cysts can eventually result in reduced kidney function, high blood pressure, and potentially kidney failure.

ADPKD is an autosomal dominant disorder, meaning it only requires one copy of the altered gene (from either the mother or father) to have the disease. Each child of an affected individual has a 50% chance of inheriting the mutated gene. The two genes most commonly associated with ADPKD are PKD1 and PKD2, located on chromosomes 16 and 4, respectively.

Symptoms can vary widely among individuals with ADPKD, but they often include high blood pressure, back or side pain, headaches, increased abdominal size due to enlarged kidneys, blood in the urine, and kidney failure. Other complications may include cysts in the liver, pancreas, and/or brain (berries aneurysms).

Early diagnosis and management of ADPKD can help slow down disease progression and improve quality of life. Treatment typically includes controlling high blood pressure, managing pain, monitoring kidney function, and addressing complications as they arise. In some cases, dialysis or a kidney transplant may be necessary if kidney failure occurs.

Bone marrow cells are the types of cells found within the bone marrow, which is the spongy tissue inside certain bones in the body. The main function of bone marrow is to produce blood cells. There are two types of bone marrow: red and yellow. Red bone marrow is where most blood cell production takes place, while yellow bone marrow serves as a fat storage site.

The three main types of bone marrow cells are:

1. Hematopoietic stem cells (HSCs): These are immature cells that can differentiate into any type of blood cell, including red blood cells, white blood cells, and platelets. They have the ability to self-renew, meaning they can divide and create more hematopoietic stem cells.
2. Red blood cell progenitors: These are immature cells that will develop into mature red blood cells, also known as erythrocytes. Red blood cells carry oxygen from the lungs to the body's tissues and carbon dioxide back to the lungs.
3. Myeloid and lymphoid white blood cell progenitors: These are immature cells that will develop into various types of white blood cells, which play a crucial role in the body's immune system by fighting infections and diseases. Myeloid progenitors give rise to granulocytes (neutrophils, eosinophils, and basophils), monocytes, and megakaryocytes (which eventually become platelets). Lymphoid progenitors differentiate into B cells, T cells, and natural killer (NK) cells.

Bone marrow cells are essential for maintaining a healthy blood cell count and immune system function. Abnormalities in bone marrow cells can lead to various medical conditions, such as anemia, leukopenia, leukocytosis, thrombocytopenia, or thrombocytosis, depending on the specific type of blood cell affected. Additionally, bone marrow cells are often used in transplantation procedures to treat patients with certain types of cancer, such as leukemia and lymphoma, or other hematologic disorders.

Nuclear transfer techniques are scientific procedures that involve the transfer of the nucleus of a cell, containing its genetic material, from one cell to another. The most well-known type of nuclear transfer is somatic cell nuclear transfer (SCNT), which is used in therapeutic cloning and reproductive cloning.

In SCNT, the nucleus of a somatic cell (a body cell, not an egg or sperm cell) is transferred into an enucleated egg cell (an egg cell from which the nucleus has been removed). The egg cell with the new nucleus is then stimulated to divide and grow, creating an embryo that is genetically identical to the donor of the somatic cell.

Nuclear transfer techniques have various potential applications in medicine, including the creation of patient-specific stem cells for use in regenerative medicine, drug development and testing, and the study of genetic diseases. However, these procedures are also associated with ethical concerns, particularly in relation to reproductive cloning and the creation of human embryos for research purposes.

LIF+Receptor+alpha+Subunit at the U.S. National Library of Medicine Medical Subject Headings (MeSH) This article incorporates ... is a subunit of a receptor for leukemia inhibitory factor. The leukemia inhibitory factor (LIF) is a polyfunctional cytokine ... "Entrez Gene: LIFR leukemia inhibitory factor receptor alpha". Timmermann A, Küster A, Kurth I, Heinrich PC, Müller-Newen G ( ... "The leukemia inhibitory factor receptor (LIFR) gene is located within a cluster of cytokine receptor loci on mouse chromosome ...
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"Molecular cloning of rat leukemia inhibitory factor receptor alpha-chain gene and its expression during pregnancy". Biochimica ... receptor: molecular cloning of the mouse OSM receptor beta subunit". Blood. 93 (3): 804-15. doi:10.1182/blood.V93.3.804. PMID ... Factor at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Source of Recombiant Leukemia Inhibitory Factor ... "The gene for human leukemia inhibitory factor (LIF) maps to 22q12". Leukemia. 3 (1): 9-13. PMID 2491897. Mori M, Yamaguchi K, ...
"Box 3-independent signaling mechanisms are involved in leukemia inhibitory factor receptor alpha- and gp130-mediated ... It forms one subunit of the type I cytokine receptor within the IL-6 receptor family. It is often referred to as the common ... Glycoprotein 130 has been shown to interact with: Grb2, HER2/neu, Janus kinase 1 Leukemia inhibitory factor receptor, PTPN11, ... leukemia-inhibitory factor, and oncostatin M: structural receptor requirements for signal attenuation". J. Immunol. 165 (5): ...
"Distinct roles for leukemia inhibitory factor receptor alpha-chain and gp130 in cell type-specific signal transduction". J. ... "Influence of subunit combinations on signaling by receptors for oncostatin M, leukemia inhibitory factor, and interleukin-6". J ... specific receptor but not leukemia inhibitory factor/OM receptor or interleukin-6 receptor. Complete block of OM-induced KS ... "Contributions of leukemia inhibitory factor receptor and oncostatin M receptor to signal transduction in heterodimeric ...
... and leukemia inhibitory factor utilize insulin receptor substrate-2 in intracellular signaling". J. Biol. Chem. 271 (46): 29415 ... Phosphatidylinositol 3-kinase regulatory subunit alpha is an enzyme that in humans is encoded by the PIK3R1 gene. ... Serve H, Hsu YC, Besmer P (1994). "Tyrosine residue 719 of the c-kit receptor is essential for binding of the P85 subunit of ... Zhang S, Broxmeyer HE (1999). "p85 subunit of PI3 kinase does not bind to human Flt3 receptor, but associates with SHP2, SHIP, ...
... encoding protein T cell receptor alpha joining 56 TRAV12-2: encoding protein T cell receptor alpha variable 12-2 TSHR: thyroid ... coagulation factor C homolog, cochlin (Limulus polyphemus) CRIP2: Cysteine-rich protein 2 DDX24: encoding enzyme ATP-dependent ... encoding protein Melanoma inhibitory activity protein 2 MIR494 encoding protein MicroRNA 494 MIR495: encoding protein MicroRNA ... encoding protein T-cell leukemia/lymphoma protein 1B TIMM9: encoding enzyme Mitochondrial import inner membrane translocase ...
... leukemia inhibitory factor receptor alpha, and oncostatin M receptor beta by distinct mechanisms". The Journal of Biological ... Oncostatin-M specific receptor subunit beta also known as the Oncostatin M receptor (OSMR) , is one of the receptor proteins ... "Oncostatin M promotes bone formation independently of resorption when signaling through leukemia inhibitory factor receptor in ... receptors. Cloning and characterization of an alternative signaling subunit conferring OSM-specific receptor activation". The ...
... muscarinic acetylcholine receptor, α2 subunit of GlyR, and SAMHD1. GRCh38: Ensembl release 89: ENSG00000156508 - Ensembl, May ... "Effects of two elongation factor 1A isoforms on the formation of gephyrin clusters at inhibitory synapses in hippocampal ... In the case of acute T lymphocytic leukemia, knocking down the eEF1A1 gene produces inhibited proliferation and induced ... The eEF1A1 protein is an isoform of the eEF-1 complex alpha subunit, an elongation factor protein, a GTPase, and an actin ...
Lck Lectin Leukemia inhibitory factor Leukemia inhibitory factor receptor Leukocyte extravasation Leukocyte-promoting factor ... alpha subunit Interleukin 23 subunit alpha Interleukin 28 receptor, alpha subunit Interleukin 34 Interleukin 35 Interleukin 6 ... necrosis factor alpha Tumor necrosis factor receptor Tumor necrosis factors Type I cytokine receptor Type II cytokine receptor ... 4 receptor Interleukin-5 receptor Interleukin-6 receptor Interleukin-7 receptor Interleukin-7 receptor-α Interleukin-8 receptor ...
BCMA is a tumor necrosis factor receptor family protein expressed on mature B cells and plasma cells and can be targeted on ... chronic lymphocytic leukemia and acute lymphoblastic leukemia. Toxicity against CD19 results in B cell loss in circulation and ... The latter targets the epsilon subunit within the human CD3 complex of the TCR. 5-6 weeks after resecting the tumor, up to 1011 ... T cells can be redirected by the integration of genes encoding either conventional alpha-beta TCRs or CARs. CARs (Chimeric ...
A direct connection between the PTEN-Akt-FOXO axis (suppressive) and the leukemia inhibitory factor receptor beta (LIFRbeta)- ... Kim J, Kim D, Chung J (2000). "Replication protein a 32 kDa subunit (RPA p32) binds the SH2 domain of STAT3 and regulates its ... Kawasaki A, Matsumura I, Kataoka Y, Takigawa E, Nakajima K, Kanakura Y (May 2003). "Opposing effects of PML and PML/RAR alpha ... In response to cytokines and growth factors, STAT3 is phosphorylated by receptor-associated Janus kinases (JAK), forms homo- or ...
... by phosphorylating its inhibitory subunit, IkB. This leads to the expression of adhesion molecules and transcription factors ... "Entrez Gene: EIF2AK2 eukaryotic translation initiation factor 2-alpha kinase 2". Feng GS, Chong K, Kumar A, Williams BR (June ... PKR contributes to this response by interacting with several inflammatory kinases such as IKK, JNK, ElF2α, insulin receptors ... This leads to cancers such as Burkitt's lymphoma, Hodgkin's disease, nasopharyngeal carcinoma and various leukemias. PKR ...
"Induction of prostaglandin E2 production by leukemia inhibitory factor promotes migration of first trimester extravillous ... EP1 mobilizes G proteins containing the Gq alpha subunit (Gαq/11)-G beta-gamma complex. These two subunits in turn stimulate ... Prostaglandin receptors Prostanoid receptors Prostaglandin E2 receptor 2 (EP2) Prostaglandin E2 receptor 3 (EP3) Prostaglandin ... of available EP1 receptors) is ~20 nM and that of PGE1 ~40 for the mouse receptor and ~25 nM for PGE2 with the human receptor. ...
"Steroid receptor coactivator-1 interacts with the p50 subunit and coactivates nuclear factor kappaB-mediated transactivations ... Garg A, Aggarwal BB (2002). "Nuclear transcription factor-kappaB as a target for cancer drug development". Leukemia. 16 (6): ... the level of its mRNA is strongly regulated by phorbol ester or tumor necrosis factor alpha". Proc Natl Acad Sci U S A. 88 (3 ... "TPL-2 kinase regulates the proteolysis of the NF-kappaB-inhibitory protein NF-kappaB1 p105". Nature. 397 (6717): 363-8. Bibcode ...
... of leukemia inhibitory factor and ciliary neurotrophic factor with the different subunits of their high affinity receptors". J ... "Signaling of human ciliary neurotrophic factor (CNTF) revisited. The interleukin-6 receptor can serve as an alpha-receptor for ... 2000). "The ciliary neurotrophic factor and its receptor, CNTFR alpha". Pharmaceutica Acta Helvetiae. 74 (2-3): 265-72. doi: ... Human ciliary neurotrophic factor has been shown to interact with the Interleukin 6 receptor. Ciliary neurotrophic factor ...
It induces tyrosine phosphorylation of the IL-6 receptor common subunit glycoprotein 130 (gp130), leukemia inhibitory factor ... 2001). "The ciliary neurotrophic factor receptor alpha component induces the secretion of and is required for functional ... specific requirement of the membrane-bound form of ciliary neurotrophic factor receptor alpha component". J. Biol. Chem. 276 ( ... 2007). "Mutations in cytokine receptor-like factor 1 (CRLF1) account for both Crisponi and cold-induced sweating syndromes". Am ...
June 1994). "Association between atopy and variants of the beta subunit of the high-affinity immunoglobulin E receptor". Nature ... It is found on B-cell lymphomas, hairy cell leukemia, B-cell chronic lymphocytic leukemia, and melanoma cancer stem cells. ... "Activation of the calcium-permeable cation channel CD20 by alpha subunits of the Gi protein". The Journal of Biological ... Variants 1 and 2 are poorly translated due to inhibitory upstream open reading frames and stem-loop structures within their 5' ...
It is identified by its translocation into the immunoglobulin alpha-locus in some cases of B-cell leukemia. The protein encoded ... "Candidate proto-oncogene bcl-3 encodes a subunit-specific inhibitor of transcription factor NF-kappa B". Nature. 358 (6387): ... The virtual screening hit compound showed potent intracellular Bcl3-inhibitory activity, and led to reductions in NF-κB ... as a novel transcription coactivator of the retinoid X receptor". The Journal of Biological Chemistry. 273 (47): 30933-30938. ...
... platelet derived growth factor receptor A or alpha-type-platelet derived growth factor receptor) gene with the FIP1L1 gene (see ... Hart CE, Bowen-Pope DF (1990). "Platelet-derived growth factor receptor: current views of the two-subunit model". J. Invest. ... juvenile myelomonocytic leukemia, myelodysplastic syndrome, acute myelogenous leukemia, acute lymphoblastic leukemia, or T ... Upon PDGF binding the dimerization of receptor releases the inhibitory conformations due to auto-phosphorylation of regulatory ...
The BCR signaling pathway is initiated when the mIg subunits of the BCR bind a specific antigen. The initial triggering of the ... MALT1 itself is a caspase-like protein that cleaves A20, an inhibitory protein of NF-κB signaling (which acts by ... IKK/NF-κB Transcription Factor Pathway: CD79 and other proteins, microsignalosomes, go to activate PLC-γ after antigen ... Daneshek W, Schwartz RS (1959). "Leukemia and auto-immunization- some possible relationships" (PDF). Blood. 14: 1151-8. PMID ...
Crosslinking anti-Thy-1 Ab can promote neurite outgrowth which is dependent on G{alpha}i and L- and N-type calcium channel ... Thy-1 has been suggested to interact with G inhibitory proteins, the Src family kinase (SFK) member c-fyn, and tubulin within ... Thy-1 was discovered by Reif and Allen in 1964 during a search for heterologous antisera against mouse leukemia cells, and was ... Some believe that there may be a functional significance of both this gene and CD3 delta subunit (T3D) mapping to chromosome ...
"Identification of c-Cbl as a new ligase for insulin-like growth factor-I receptor with distinct roles from Mdm2 in receptor ... Chen D, Li M, Luo J, Gu W (April 2003). "Direct interactions between HIF-1 alpha and Mdm2 modulate p53 function". The Journal ... Zhao L, Samuels T, Winckler S, Korgaonkar C, Tompkins V, Horne MC, Quelle DE (January 2003). "Cyclin G1 has growth inhibitory ... Zhu H, Wu L, Maki CG (December 2003). "MDM2 and promyelocytic leukemia antagonize each other through their direct interaction ...
The amino terminus of the alpha helix portion of zinc fingers targets the major grooves of the DNA helix and binds near the ... iii) To deliver two different zinc finger nuclease subunits and donor DNA to the cell, the vectors that are used need to be ... Conceptually, targeting and editing could focus on host cellular co-receptors for HIV or on proviral HIV DNA. It has also been ... Frankel, A. D.; Berg, J. M.; Pabo, C. O. (1987). "Metal-dependent folding of a single zinc finger from transcription factor ...
... by regulating Leukemia Inhibitory Factor has been shown to facilitate implantation in the mouse and possibly humans ... "Identification of c-Cbl as a new ligase for insulin-like growth factor-I receptor with distinct roles from Mdm2 in receptor ... Chen D, Li M, Luo J, Gu W (April 2003). "Direct interactions between HIF-1 alpha and Mdm2 modulate p53 function". The Journal ... by a signalosome-like subunit and its role in DNA repair". Molecular Cell. 12 (5): 1087-99. doi:10.1016/S1097-2765(03)00424-6. ...
The second ubiquitin receptor identified to date, Rpn10, is positioned at the periphery of the lid, near subunits Rpn8 and Rpn9 ... Degradation of Aux/IAA proteins derepresses transcription factors in the auxin-response factor (ARF) family and induces ARF- ... which serve as docking domains for the regulatory particles and the alpha subunits N-termini (Pfam PF10584) form a gate that ... for B-cell acute lymphoblastic leukemia Proteasome inhibitors can kill some types of cultured leukemia cells that are resistant ...
Sentis S, Le Romancer M, Bianchin C, Rostan MC, Corbo L (2005). "Sumoylation of the estrogen receptor alpha hinge region ... was isolated and characterized as an inhibitory domain that binds and inhibits both the MITF and STAT3 transcription factors. ... "Requirement for high mobility group protein HMGI-C interaction with STAT3 inhibitor PIAS3 in repression of alpha-subunit of ... Leukemia Research. 28 (1): 71-82. doi:10.1016/S0145-2126(03)00158-9. PMID 14630083. Long J, Wang G, Matsuura I, He D, Liu F ( ...
"A degradation signal located in the C-terminus of p21WAF1/CIP1 is a binding site for the C8 alpha-subunit of the 20S proteasome ... "A conserved domain of the large subunit of replication factor C binds PCNA and acts like a dominant negative inhibitor of DNA ... Almond JB, Cohen GM (April 2002). "The proteasome: a novel target for cancer chemotherapy". Leukemia. 16 (4): 433-43. doi: ... vitamin D receptor and cyclin-dependent kinase inhibitors, p21 and p27". Nephrol. Dial. Transplant. 18 Suppl 3 (90003): iii9-12 ...
"Entrez Gene: THRA thyroid hormone receptor, alpha (erythroblastic leukemia viral (v-erb-a) oncogene homolog, avian)". Sakurai A ... detailed functional and structural analysis of a major thyroid hormone inhibitory element in the human thyrotropin beta-subunit ... "A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by ... "Entrez Gene: THRB thyroid hormone receptor, beta (erythroblastic leukemia viral (v-erb-a) oncogene homolog 2, avian)". Monden T ...
"The interleukin-3 receptor alpha chain is a unique marker for human acute myelogenous leukemia stem cells". Leukemia. 14 (10): ... 2005). "Leukemia inhibitory factor as an anti-apoptotic mitogen for pluripotent mouse embryonic stem cells in a serum-free ... April 2005). "Maintenance of spermatogenesis requires TAF4b, a gonad-specific subunit of TFIID". Genes & Development. 19 (7): ... Lane MA, Chen AC, Roman SD, Derguini F, Gudas LJ (November 1999). "Removal of LIF (leukemia inhibitory factor) results in ...
LIF+Receptor+alpha+Subunit at the U.S. National Library of Medicine Medical Subject Headings (MeSH) This article incorporates ... is a subunit of a receptor for leukemia inhibitory factor. The leukemia inhibitory factor (LIF) is a polyfunctional cytokine ... "Entrez Gene: LIFR leukemia inhibitory factor receptor alpha". Timmermann A, Küster A, Kurth I, Heinrich PC, Müller-Newen G ( ... "The leukemia inhibitory factor receptor (LIFR) gene is located within a cluster of cytokine receptor loci on mouse chromosome ...
The main chain fold conforms to the four alpha-helix bundle topology previously observed for several members of the ... A model for receptor binding based on the structure of the GH ligand-receptor complex requires additional, novel features to ... Analysis of the biological function and receptor specificity of a series of human-mouse LIF chimeras implicate two regions of ... Of these, LIF shows closest structural homology to granulocyte colony-stimulating factor and growth hormone (GH). Sequence ...
Its biological activities are shared by IL-6-family of cytokines such as leukemia inhibitory factor and oncostatin M. IL-6 ... IL-6 Receptor (IL-6R, gp80) is 80 kDa alpha subunit, transmembrane glycoprotein that is 449 aa long. It binds IL-6 with low ... Upon binding of IL-6 to the receptor (alpha subunit), gp130 is homodimerized and is subsequently involved in down-stream signal ... Soluble interleukin-6 receptor as a prognostic factor in numerous clinical disorders:. In healthy individuals, blood levels of ...
View Mouse LIFR alpha APC-conjugated Antibody (FAB5990A) datasheet. ... leukemia inhibitory factor receptor alpha; leukemia inhibitory factor receptor; LIF R alpha; LIF R beta; LIF receptor; LIFR ... Binding affinity is increased by the ligand-induced association of LIF R alpha with the signal transducing subunit gp130 (6, 7 ... Background: LIFR alpha. Leukemia Inhibitory Factor Receptor alpha (LIF R alpha ), also known as LIFR beta (due to its ...
Interleukin-6 Receptor alpha Subunit. *Interleukin-7 Receptor alpha Subunit. *Leukemia Inhibitory Factor Receptor alpha Subunit ... "Interleukin-5 Receptor alpha Subunit" by people in Harvard Catalyst Profiles by year, and whether "Interleukin-5 Receptor alpha ... Receptors, Interleukin-5 [D12.776.543.750.705.852.420.380]. *Interleukin-5 Receptor alpha Subunit [D12.776.543.750.705.852. ... A low affinity interleukin-5 receptor subunit that combines with the CYTOKINE RECEPTOR COMMON BETA SUBUNIT to form a high ...
Leukemia inhibitory factor receptor. $5.00. USD Add to cart. * Liprin-alpha-2. $5.00. USD Add to cart ... Eukaryotic initiation factor 4A-I. $5.00. USD Add to cart. * Eukaryotic translation initiation factor 3 subunit E. $5.00. USD ... Macrophage colony-stimulating factor 1 receptor. $5.00. USD Add to cart. * Macrophage migration inhibitory factor. $5.00. USD ... ATP synthase subunit d, mitochondrial. $5.00. USD Add to cart. * Atrial natriuretic peptide receptor 1. $5.00. USD Add to cart ...
Leukemia Inhibitory Factor Receptor alpha Subunit D12.776.543.750.705.852.500.750 D12.776.543.750.705.852.583.750 D12.776. ... Estrogen Receptor alpha D12.776.260.698.750.350.174 D12.776.930.669.750.350.174 Estrogen Receptor beta D12.776.260.698.750.350. ... Thyroid Hormone Receptors alpha D12.776.260.698.850.500 D12.776.930.669.850.500 Thyroid Hormone Receptors beta D12.776.260.698. ... Tumor Necrosis Factor-alpha D12.644.276.972.626 D12.776.467.972.626 D23.529.972.626 Tumor Necrosis Factors D12.644.276.972 ...
Leukemia Inhibitory Factor Receptor alpha Subunit D12.776.543.750.705.852.500.750 D12.776.543.750.705.852.583.750 D12.776. ... Estrogen Receptor alpha D12.776.260.698.750.350.174 D12.776.930.669.750.350.174 Estrogen Receptor beta D12.776.260.698.750.350. ... Thyroid Hormone Receptors alpha D12.776.260.698.850.500 D12.776.930.669.850.500 Thyroid Hormone Receptors beta D12.776.260.698. ... Tumor Necrosis Factor-alpha D12.644.276.972.626 D12.776.467.972.626 D23.529.972.626 Tumor Necrosis Factors D12.644.276.972 ...
Leukemia Inhibitory Factor Receptor alpha Subunit D12.776.543.750.705.852.500.750 D12.776.543.750.705.852.583.750 D12.776. ... Estrogen Receptor alpha D12.776.260.698.750.350.174 D12.776.930.669.750.350.174 Estrogen Receptor beta D12.776.260.698.750.350. ... Thyroid Hormone Receptors alpha D12.776.260.698.850.500 D12.776.930.669.850.500 Thyroid Hormone Receptors beta D12.776.260.698. ... Tumor Necrosis Factor-alpha D12.644.276.972.626 D12.776.467.972.626 D23.529.972.626 Tumor Necrosis Factors D12.644.276.972 ...
Leukemia Inhibitory Factor Receptor alpha Subunit D12.776.543.750.705.852.500.750 D12.776.543.750.705.852.583.750 D12.776. ... Estrogen Receptor alpha D12.776.260.698.750.350.174 D12.776.930.669.750.350.174 Estrogen Receptor beta D12.776.260.698.750.350. ... Thyroid Hormone Receptors alpha D12.776.260.698.850.500 D12.776.930.669.850.500 Thyroid Hormone Receptors beta D12.776.260.698. ... Tumor Necrosis Factor-alpha D12.644.276.972.626 D12.776.467.972.626 D23.529.972.626 Tumor Necrosis Factors D12.644.276.972 ...
Leukemia Inhibitory Factor Receptor alpha Subunit D12.776.543.750.705.852.500.750 D12.776.543.750.705.852.583.750 D12.776. ... Estrogen Receptor alpha D12.776.260.698.750.350.174 D12.776.930.669.750.350.174 Estrogen Receptor beta D12.776.260.698.750.350. ... Thyroid Hormone Receptors alpha D12.776.260.698.850.500 D12.776.930.669.850.500 Thyroid Hormone Receptors beta D12.776.260.698. ... Tumor Necrosis Factor-alpha D12.644.276.972.626 D12.776.467.972.626 D23.529.972.626 Tumor Necrosis Factors D12.644.276.972 ...
leukemia inhibitory factor receptor alpha. 5p13-p12. PMID:cooccur. 1008. CDH10. -. cadherin 10. 5p14.2. CV:PGCnp. PMID:cooccur ... Sec61 translocon alpha 2 subunit. 10p14. CV:PGCnp. 22943. DKK1. DKK-1 , SK. dickkopf WNT signaling pathway inhibitor 1. 10q11.2 ... eukaryotic translation initiation factor 2 alpha kinase 3. 2p12. CV:PGCnp. DMG:Jaffe_2016. GO_Annotation. GSMA_I. ... prolyl 4-hydroxylase subunit alpha 2. 5q31. CV:PGCnp. DMG:Wockner_2014. GSMA_I. ...
IL-6 Receptor β chain, CD130), that is shared with the receptor complexes for Leukemia Inhibitory Factor (LIF), Ciliary ... M5 monoclonal antibody specifically binds to human CD126 which is also known as the alpha subunit of the human IL-6 Receptor ( ... IL-6 Receptor β chain, CD130), that is shared with the receptor complexes for Leukemia Inhibitory Factor (LIF), Ciliary ... also known as gp80 and B cell stimulatory factor-2 (BSF-2) Receptor. The IL-6Rα subunit associates with the 130-160 kDa gp130 ...
Leukemia Inhibitory Factor Receptor alpha Subunit. *Low Density Lipoprotein Receptor-Related Protein-1 ... A tumor necrosis factor receptor subtype that has specificity for TUMOR NECROSIS FACTOR ALPHA and LYMPHOTOXIN ALPHA. It is ... Receptors, Tumor Necrosis Factor [D12.776.543.750.705.852.760]. *Receptors, Tumor Necrosis Factor, Type I [D12.776.543.750. ... Receptors, Tumor Necrosis Factor, Type I*Receptors, Tumor Necrosis Factor, Type I ...
Leukemia Inhibitory Factor Receptor alpha Subunit. *Low Density Lipoprotein Receptor-Related Protein-1 ... Receptor, Macrophage Colony-Stimulating Factor*Receptor, Macrophage Colony-Stimulating Factor. *Receptor, Macrophage Colony ... Receptors, Colony-Stimulating Factor [D12.776.543.750.705.852.150]. *Receptor, Macrophage Colony-Stimulating Factor [D12.776. ... Receptors, Colony-Stimulating Factor [D12.776.543.750.750.400.200]. *Receptor, Macrophage Colony-Stimulating Factor [D12.776. ...
Interleukin 27 receptor, alpha subunit, PIAS1, BRCA1, Epidermal growth factor receptor,PTK2, Mammalian target of rapamycin ( ... Human T-cell leukemia virus type 2 induces survival and proliferation of CD34(+) TF-1 cells through activation of STAT1 and ... Consistent with the inhibitory effect of reactive oxygen species on STAT1 signaling, STAT1 inhibition by 15dPGJ(2) was ... Activation of JAK kinases and STAT proteins by interleukin-2 and interferon alpha, but not the T cell antigen receptor, in ...
2008) Inhibitory receptor signaling via tyrosine phosphorylation of the adaptor Crk. Immunity 29(4): 578-588. Carlo-Stella C et ... 2006) CCAAT/enhancer binding proteins alpha and epsilon cooperate with all-trans retinoic acid in therapy but differ in their ... 2006) The ETS factor TEL2 is a hematopoietic oncoprotein. Blood 107(3): 1124-1132. Carmen M et al. (2004) Interleukin-6 ... 2003) CCAAT/Enhancer binding proteins repress the leukemic phenotype of acute myeloid leukemia. Blood 101(3): 1141-1148. Jin H ...
... transducing receptor subunit for the IL-6-type cytokines consisting of interleukin (IL)-6, IL-11, leukemia inhibitory factor ( ... Glycoprotein 130 (gp130; also known as IL-6 signal transducer, IL-6 receptor beta, oncostatin-M alpha subunit) is a ... oncostatin M receptor); interleukin receptor beta chain; interleukin-6 receptor subunit beta; Interleukin-6 signal transducer; ... IL-6 receptor subunit beta; IL-6R subunit beta; IL-6RB; IL-6R-beta; IL6ST; interleukin 6 signal transducer (gp130, ...
Factor Inhibidor de Leucemia. Leukemia Inhibitory Factor Receptor alpha Subunit. Subunidade alfa de Receptor de Fator Inibidor ... Receptor Activador del Factor Nuclear kappa-B. Receptor, Interferon alpha-beta. Receptor de Interferon alfa e beta. Receptor de ... Factor Activador de Células B. B-Cell Activation Factor Receptor. Receptor do Fator Ativador de Células B. Receptor del Factor ... Ciliary Neurotrophic Factor Receptor alpha Subunit. Subunidade alfa do Receptor do Fator Neutrófico Ciliar. Subunidad alfa del ...
Factor Inhibidor de Leucemia. Leukemia Inhibitory Factor Receptor alpha Subunit. Subunidade alfa de Receptor de Fator Inibidor ... Receptor Activador del Factor Nuclear kappa-B. Receptor, Interferon alpha-beta. Receptor de Interferon alfa e beta. Receptor de ... Factor Activador de Células B. B-Cell Activation Factor Receptor. Receptor do Fator Ativador de Células B. Receptor del Factor ... Ciliary Neurotrophic Factor Receptor alpha Subunit. Subunidade alfa do Receptor do Fator Neutrófico Ciliar. Subunidad alfa del ...
Factor Inhibidor de Leucemia. Leukemia Inhibitory Factor Receptor alpha Subunit. Subunidade alfa de Receptor de Fator Inibidor ... Receptor Activador del Factor Nuclear kappa-B. Receptor, Interferon alpha-beta. Receptor de Interferon alfa e beta. Receptor de ... Factor Activador de Células B. B-Cell Activation Factor Receptor. Receptor do Fator Ativador de Células B. Receptor del Factor ... Ciliary Neurotrophic Factor Receptor alpha Subunit. Subunidade alfa do Receptor do Fator Neutrófico Ciliar. Subunidad alfa del ...
Factor Inhibidor de Leucemia. Leukemia Inhibitory Factor Receptor alpha Subunit. Subunidade alfa de Receptor de Fator Inibidor ... Receptor Activador del Factor Nuclear kappa-B. Receptor, Interferon alpha-beta. Receptor de Interferon alfa e beta. Receptor de ... Factor Activador de Células B. B-Cell Activation Factor Receptor. Receptor do Fator Ativador de Células B. Receptor del Factor ... Ciliary Neurotrophic Factor Receptor alpha Subunit. Subunidade alfa do Receptor do Fator Neutrófico Ciliar. Subunidad alfa del ...
Factor Inhibidor de Leucemia. Leukemia Inhibitory Factor Receptor alpha Subunit. Subunidade alfa de Receptor de Fator Inibidor ... Receptor Activador del Factor Nuclear kappa-B. Receptor, Interferon alpha-beta. Receptor de Interferon alfa e beta. Receptor de ... Factor Activador de Células B. B-Cell Activation Factor Receptor. Receptor do Fator Ativador de Células B. Receptor del Factor ... Ciliary Neurotrophic Factor Receptor alpha Subunit. Subunidade alfa do Receptor do Fator Neutrófico Ciliar. Subunidad alfa del ...
Factor Inhibidor de Leucemia. Leukemia Inhibitory Factor Receptor alpha Subunit. Subunidade alfa de Receptor de Fator Inibidor ... Receptor Activador del Factor Nuclear kappa-B. Receptor, Interferon alpha-beta. Receptor de Interferon alfa e beta. Receptor de ... Factor Activador de Células B. B-Cell Activation Factor Receptor. Receptor do Fator Ativador de Células B. Receptor del Factor ... Ciliary Neurotrophic Factor Receptor alpha Subunit. Subunidade alfa do Receptor do Fator Neutrófico Ciliar. Subunidad alfa del ...
Factor Inhibidor de Leucemia. Leukemia Inhibitory Factor Receptor alpha Subunit. Subunidade alfa de Receptor de Fator Inibidor ... Receptor Activador del Factor Nuclear kappa-B. Receptor, Interferon alpha-beta. Receptor de Interferon alfa e beta. Receptor de ... Factor Activador de Células B. B-Cell Activation Factor Receptor. Receptor do Fator Ativador de Células B. Receptor del Factor ... Ciliary Neurotrophic Factor Receptor alpha Subunit. Subunidade alfa do Receptor do Fator Neutrófico Ciliar. Subunidad alfa del ...
Leukemia Inhibitory Factor Receptor alpha Subunit. *Low Density Lipoprotein Receptor-Related Protein-1 ... Interleukin-3 Receptor alpha Subunit. *Interleukin-4 Receptor alpha Subunit. *Interleukin-5 Receptor alpha Subunit ... Interleukin-18 Receptor alpha Subunit. *Interleukin-18 Receptor beta Subunit. *Interleukin-2 Receptor alpha Subunit ... Interleukin Receptor Common gamma Subunit. *Interleukin-10 Receptor alpha Subunit. *Interleukin-10 Receptor beta Subunit ...
Leukemia Inhibitory Factor Receptor alpha Subunit. *Low Density Lipoprotein Receptor-Related Protein-1 ... It is now known that a variety of light chain subunits (ANTIGENS, CD98 LIGHT CHAINS) can dimerize with the heavy chain. ... Interleukin-3 Receptor alpha Subunit. *Interleukin-4 Receptor alpha Subunit. *Interleukin-5 Receptor alpha Subunit ... Interleukin-18 Receptor alpha Subunit. *Interleukin-18 Receptor beta Subunit. *Interleukin-2 Receptor alpha Subunit ...
Leukemia Inhibitory Factor Receptor alpha Subunit. *Low Density Lipoprotein Receptor-Related Protein-1 ... Interleukin-3 Receptor alpha Subunit. *Interleukin-4 Receptor alpha Subunit. *Interleukin-5 Receptor alpha Subunit ... Interleukin-18 Receptor alpha Subunit. *Interleukin-18 Receptor beta Subunit. *Interleukin-2 Receptor alpha Subunit ... Interleukin Receptor Common gamma Subunit. *Interleukin-10 Receptor alpha Subunit. *Interleukin-10 Receptor beta Subunit ...
Leukemia Inhibitory Factor Receptor alpha Subunit. *Low Density Lipoprotein Receptor-Related Protein-1 ... Interleukin-3 Receptor alpha Subunit. *Interleukin-4 Receptor alpha Subunit. *Interleukin-5 Receptor alpha Subunit ... Interleukin-18 Receptor alpha Subunit. *Interleukin-18 Receptor beta Subunit. *Interleukin-2 Receptor alpha Subunit ... Interleukin Receptor Common gamma Subunit. *Interleukin-10 Receptor alpha Subunit. *Interleukin-10 Receptor beta Subunit ...
6,156,733 Use of leukemia inhibitory factor and endothelin antagonists 6,156,569 Prolonged culturing of avian primordial germ ... coactivator 6,166,178 Telomerase catalytic subunit 6,165,755 Chicken neuropeptide gene useful for improved poultry production ... alpha.1 promotes tissue repair, angiogenesis and cell migration 6,197,578 Cells expressing both human CD4 and a human fusion ... 6,218,356 Neural receptor tyrosine kinase 6,218,181 Retroviral packaging cell line 6,218,162 SH2-containing inositol- ...
  • Leukemia Inhibitory Factor Receptor alpha (LIF R alpha ), also known as LIFR beta (due to its participation in signal transduction) and CD118, is a 190 kDa type I transmembrane protein in the Interleukin-6 receptor family. (rndsystems.com)
  • Interleukin-5 Receptor alpha Subunit" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (harvard.edu)
  • A low affinity interleukin-5 receptor subunit that combines with the CYTOKINE RECEPTOR COMMON BETA SUBUNIT to form a high affinity receptor for INTERLEUKIN-5. (harvard.edu)
  • Several isoforms of the interleukin-5 receptor alpha subunit exist due to multiple ALTERNATIVE SPLICING. (harvard.edu)
  • This graph shows the total number of publications written about "Interleukin-5 Receptor alpha Subunit" by people in Harvard Catalyst Profiles by year, and whether "Interleukin-5 Receptor alpha Subunit" was a major or minor topic of these publication. (harvard.edu)
  • Below are the most recent publications written about "Interleukin-5 Receptor alpha Subunit" by people in Profiles. (harvard.edu)
  • Gp130 serves as the signal transducing receptor subunit for the IL-6-type cytokines consisting of interleukin (IL)-6, IL-11, leukemia inhibitory factor (LIF), oncostatin M (OSM), ciliary neurotrophic factor (CNTF), new neurotrophin factor-1 (NNT-1), IL-27, cardiotrophin-1 (CT-1), and cardiotrophin like cytokine (CLC) (2 - 5). (rndsystems.com)
  • The interleukin 2 receptor, which is involved in T cell-mediated immune responses, is present in 3 forms with respect to ability to bind interleukin 2. (cancer-genetics.org)
  • Both the intermediate and high affinity forms of the receptor are involved in receptor-mediated endocytosis and transduction of mitogenic signals from interleukin 2. (cancer-genetics.org)
  • Receptor for interleukin-2. (cusabio.com)
  • Increased serum level of soluble interleukin-2 receptor is associated with a worse response of metastatic clear cell renal cell carcinoma to interferon alpha and sequential VEGF-targeting therapy. (cusabio.com)
  • Data show that interleukin-2 receptor alpha, tumor necrosis factor receptor 1, serum STimulation-2 (IL1RL1 gene product), and regenerating islet-derived 3-alpha were significantly associated with non-relapse mortality. (cusabio.com)
  • Human ciliary neurotrophic factor has been shown to interact with the Interleukin 6 receptor . (wikidoc.org)
  • It is now known that a variety of light chain subunits (ANTIGENS, CD98 LIGHT CHAINS) can dimerize with the heavy chain. (wakehealth.edu)
  • NK cells contribute to cancer immune surveillance not only by their direct natural cytotoxicity which is triggered rapidly upon stimulation through germline-encoded cell surface receptors, but also by modulating T-cell mediated antitumor immune responses through maintaining the quality of dendritic cells and enhancing the presentation of tumor antigens. (frontiersin.org)
  • Both LIFR and gp130 are members of a family of cytokine receptors that includes components of the receptors for the majority of hematopoietic cytokines and for cytokines that affect other systems, including the ciliary neurotrophic factor, growth hormone and prolactin. (wikipedia.org)
  • Sequence alignments for the functionally related molecules oncostatin M and ciliary neurotrophic factor, when mapped to the LIF structure, indicate regions of conserved surface character. (ox.ac.uk)
  • Our studies also show that these NPs have differential requirements for LIF and ciliary neurotrophic factor (CNTF) and for epidermal growth factor (EGF), fibroblast growth factor (FGF-2) and platelet-derived growth factor (PDGF) for their propagation in vitro. (karger.com)
  • Ciliary neurotrophic factor is a protein that in humans is encoded by the CNTF gene . (wikidoc.org)
  • A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease . (wikidoc.org)
  • Cotranscription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor. (wikidoc.org)
  • NT-501 is a product being developed by Neurotech that consists of encapsulated human cells genetically modified to secrete ciliary neurotrophic factor (CNTF). (wikidoc.org)
  • Its biological activities are shared by IL-6-family of cytokines such as leukemia inhibitory factor and oncostatin M. IL-6 exerts its biological activities through interaction with specific receptors expressed on the surface of target cells. (sbhsciences.com)
  • The pathogenesis of infiltrative ophthalmopathy (responsible for the exophthalmos in Graves disease) is poorly understood but may result from immunoglobulins directed to the TSH receptors in the orbital fibroblasts and fat that result in release of proinflammatory cytokines, inflammation, and accumulation of glycosaminoglycans. (msdmanuals.com)
  • DNA-dependent protein kinase catalytic subunit (DNA-PKcs), a key component of the non-homologous end-joining (NHEJ) pathway, is involved in DNA double-strand break repair, immunocompetence, genomic integrity, and epidermal growth factor receptor signaling. (amegroups.org)
  • The catalytic subunit of DNA-dependent protein kinase (DNA-PKcs) is the key component of the non-homologous end-joining (NHEJ) pathway for DNA double-strand break (DSB) repair and is required for cellular resistance to ionizing radiation (IR) ( 1 , 2 ). (amegroups.org)
  • LIF action appears to be mediated through a high-affinity receptor complex composed of a low-affinity LIF binding chain (LIF receptor) and a high-affinity converter subunit, glycoprotein 130 (IL6ST, gp130). (wikipedia.org)
  • Leukemia inhibitory factor receptor has been shown to interact with glycoprotein 130. (wikipedia.org)
  • IL-6 Receptor (IL-6R, gp80) is 80 kDa alpha subunit, transmembrane glycoprotein that is 449 aa long. (sbhsciences.com)
  • also known as IL-6 signal transducer, IL-6 receptor beta, oncostatin-M alpha subunit) is a ubiquitously expressed, 130 kDa type I transmembrane glycoprotein and member of the type II subfamily, type I cytokine receptor family. (rndsystems.com)
  • Fibronectin is a dimeric glycoprotein composed of disulfide-linked subunits with a molecular weight of 220-250kDa each. (embl.de)
  • Mature mouse LIF R alpha consists of a 785 amino acid (aa) extracellular domain (ECD) with two cytokine receptor homology domains, one WSxWS motif, and three fibronectin type III repeats, followed by a 25 aa transmembrane segment and a 239 aa cytoplasmic domain (2, 3). (rndsystems.com)
  • The ECD also contains an N terminal immunoglobulin (Ig)-like C2-type domain, followed by the cytokine receptor homology region (CHR) which is made up of two fibronectin type III-like domains and a WSXWS motif, and three additional fibronectin type III-like domains (2). (rndsystems.com)
  • When activated the receptor undergoes autophosphorylation, phosphorylation of down-stream signaling molecules and rapid down-regulation. (rush.edu)
  • Upon binding of IL-6 to the receptor (alpha subunit), gp130 is homodimerized and is subsequently involved in down-stream signal processes binding tyrosine kinases and activating STAT1 and STAT3 transcriptional factors. (sbhsciences.com)
  • Interestingly, the association of IL-6 with the soluble form of IL-6R alpha is capable of eliciting a biological response in cells that express only the membrane gp130. (sbhsciences.com)
  • Binding affinity is increased by the ligand-induced association of LIF R alpha with the signal transducing subunit gp130 (6, 7). (rndsystems.com)
  • The LIF R alpha /gp130 receptor complex also transduces Oncostatin M signals, although LIF R alpha alone does not interact with Oncostatin M (6). (rndsystems.com)
  • gp130 associates with different ligand-specific receptors to form signaling receptor complexes for the other IL-6 family ligands (1). (rndsystems.com)
  • The CNTF receptor is a ternary complex that contains CNTF R alpha and gp130 as well as LIF R alpha (8, 9). (rndsystems.com)
  • Receptors, Tumor Necrosis Factor, Type I" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (childrensmercy.org)
  • A tumor necrosis factor receptor subtype that has specificity for TUMOR NECROSIS FACTOR ALPHA and LYMPHOTOXIN ALPHA. (childrensmercy.org)
  • It is constitutively expressed in most tissues and is a key mediator of tumor necrosis factor signaling in the vast majority of cells. (childrensmercy.org)
  • This graph shows the total number of publications written about "Receptors, Tumor Necrosis Factor, Type I" by people in this website by year, and whether "Receptors, Tumor Necrosis Factor, Type I" was a major or minor topic of these publications. (childrensmercy.org)
  • Below are the most recent publications written about "Receptors, Tumor Necrosis Factor, Type I" by people in Profiles. (childrensmercy.org)
  • Progressive biliary destruction is independent of a functional tumor necrosis factor-alpha pathway in a rhesus rotavirus-induced murine model of biliary atresia. (childrensmercy.org)
  • Multiple mechanisms are implicated in such dysfunction, spanning from inhibition of recruitment to the tumor bed, activation of inhibitory processes, blowing up of activation signals, and deregulation of metabolism ( Figure 1 ). (encyclopedia.pub)
  • Soluble factors released by immune, tumor, and stromal cells, including transforming growth factor (TGF)-β, adenosine, and prostaglandin E 2 (PGE 2 ), not only inhibit NK cell functionality, but they additionally determine their conversion toward a non-cytolytic phenotype. (encyclopedia.pub)
  • An additional inhibitory mechanism exploited by the tumor microenvironment is represented by the imbalance in immune checkpoint molecules, responsible for NK cell exhausted status. (encyclopedia.pub)
  • NK cells express a heterogeneous repertoire of chemoattractant receptors that are distinct for each cell subset, and thus differentially regulate the recruitment of each population to the tumor bed. (encyclopedia.pub)
  • The intracellular domain of the p75 neurotrophin receptor (p75ICD) lacks catalytic activity but contains a motif similar to death domains found in the cytoplasmic regions of members of the tumor necrosis factor receptor family and their downstream targets. (embl-heidelberg.de)
  • Analysis of the biological function and receptor specificity of a series of human-mouse LIF chimeras implicate two regions of receptor interaction that are located in the fourth helix and the preceding loop. (ox.ac.uk)
  • Furthermore, similar to T cells, specific recognition and elimination of cancer cells by NK cells can be markedly enhanced through expression of chimeric antigen receptors (CARs), which provides an opportunity to generate NK-cell therapeutics of defined specificity for cancer immunotherapy. (frontiersin.org)
  • The protein encoded by this gene represents the beta subunit and is a type I membrane protein. (cancer-genetics.org)
  • This gene encodes a transcription factor that regulates MHC class II genes by binding to a promoter element referred to as an X box. (cancerindex.org)
  • This gene product is a bZIP protein, which was also identified as a cellular transcription factor that binds to an enhancer in the promoter of the T cell leukemia virus type 1 promoter. (cancerindex.org)
  • The protein encoded by this gene is a polypeptide hormone and neurotrophic factor whose actions have mainly been studied in the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neural populations including astrocytes . (wikidoc.org)
  • Congenital FXIII deficiency is due principally to defects in the catalytic A subunit of FXIII, with more than 100 mutations throughout the factor XIII A gene identified. (medscape.com)
  • [6] Like CNTF it is a neurotrophic factor , and may stimulate nerve cells to survive. (wikidoc.org)
  • The main chain fold conforms to the four alpha-helix bundle topology previously observed for several members of the hematopoietic cytokine family. (ox.ac.uk)
  • The domains in the CHR are the structural hallmarks of the hematopoietic cytokine receptor family (2). (rndsystems.com)
  • Alpha-helical domain present in a variety of proteins with apoptotic functions. (embl-heidelberg.de)
  • Activation of Rho proteins through release of bound GDP and subsequent binding of GTP, is catalysed by guanine nucleotide exchange factors (GEFs) in the Dbl family. (embl-heidelberg.de)
  • The guanine nucleotide exchange factor (GEF) Dbl targets Rho family proteins thereby stimulating their GDP/GTP exchange, and thus is believed to be involved in receptor-mediated regulation of the proteins. (embl-heidelberg.de)
  • Of these, LIF shows closest structural homology to granulocyte colony-stimulating factor and growth hormone (GH). (ox.ac.uk)
  • LIFR also known as CD118 (Cluster of Differentiation 118), is a subunit of a receptor for leukemia inhibitory factor. (wikipedia.org)
  • [ 1 ] Acquired FXIII deficiencies, which result from autoantibodies against FXIII subunits, are extremely rare but may produce severe bleeding diatheses. (medscape.com)
  • unlike most autoantibodies, which are inhibitory, this autoantibody is stimulatory, thus causing continuous synthesis and secretion of excess T4 and T3. (msdmanuals.com)
  • The resulting loss of 26 nt from the spliced mRNA causes a frame-shift and an isoform XBP1(S), which is the functionally active transcription factor. (cancerindex.org)
  • Developmental up-regulation and agonist-dependent down-regulation of GABA(A) receptor subunit messenger RNAs in chick cortical neurons. (ntu.ac.uk)
  • The leukemia inhibitory factor (LIF) is a polyfunctional cytokine that affects the differentiation, survival, and proliferation of a wide variety of cells in the adult and the embryo. (wikipedia.org)
  • LIF R alpha is widely expressed, and LIF induces the proliferation, differentiation, and activation of cells in many tissues (10, 11). (rndsystems.com)
  • LIF R alpha binds the pleiotropic cytokine LIF with low affinity, and the soluble isoform retains LIF-binding activity (5). (rndsystems.com)
  • The structure of murine leukemia inhibitory factor (LIF) has been determined by X-ray crystallography at 2.0 A resolution. (ox.ac.uk)
  • Characterization of murine pregnancy decidua transforming growth factor beta. (mcmaster.ca)
  • Initial clinical studies indicate the levels of sIL-6R, the alpha subunit, in the serum of patients with various diseases as summarized in table1. (sbhsciences.com)
  • Description: A sandwich ELISA kit for detection of Serine Palmitoyltransferase, Long Chain Base Subunit 3 from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (1elisakits.com)
  • The death domain (DD) is a homotypic protein interaction module composed of a bundle of six alpha-helices. (embl-heidelberg.de)
  • Recent evidence showed that PF-429242, a membrane-bound transcription factor site-1 protease (MBTPS1) inhibitor, exhibited anticancer activities against glioblastomas, renal cell carcinoma, and pancreatic cancer. (bvsalud.org)
  • The DD mediates self-association of these receptors, thus giving the signal to downstream events that lead to apoptosis. (embl-heidelberg.de)
  • TRAIL, also called Apo2L, is a cytotoxic protein that induces apoptosis of many transformed cell lines but not of normal tissues, even though its death domain-containing receptor, DR4, is expressed on both cell types. (embl-heidelberg.de)
  • An antagonist decoy receptor (designated as TRID for TRAIL receptor without an intracellular domain) that may explain the resistant phenotype of normal tissues was identified. (embl-heidelberg.de)
  • It is a hypothalamic neuropeptide that is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks . (wikidoc.org)
  • We performed gain and loss of function studies for leukemia inhibitory factor (LIF) and showed a depletion of NSCs, a subset of multipotential neural precursors and immature oligodendrocytes in LIF null mice. (karger.com)
  • The activated receptor signals via a conserved death domain that associates with specific TNF RECEPTOR-ASSOCIATED FACTORS in the CYTOPLASM. (childrensmercy.org)
  • Its activity is directed by intracellular signals mediated by various types of receptors such as G protein-coupled receptors. (embl-heidelberg.de)
  • Description: A sandwich quantitative ELISA assay kit for detection of Mouse Serine Palmitoyltransferase, Long Chain Base Subunit 3 (SPTLC3) in samples from tissue homogenates, cell lysates or other biological fluids. (1elisakits.com)
  • Association of the proto-oncogene product dbl with G protein betagamma subunits. (embl-heidelberg.de)
  • several of these TNF receptors use caspase activation as a signalling mechanism. (embl-heidelberg.de)
  • An antagonist decoy receptor and a death domain-containing receptor for TRAIL. (embl-heidelberg.de)
  • Here, we demonstrate that the endoplasmic reticulum stress sensor inositol-requiring enzyme 1 (IRE1α) and its substrate transcription factor X-box-binding protein 1 (XBP1) drive NK cell responses against viral infection and tumors in vivo. (cancerindex.org)
  • This type of activation, called "trans-signalling", renders virtually all cells capable of responding to IL-6/sIL-6R alpha complexes, making for a large new spectrum of IL-6 activities, ranging from the control of the immune response to involvement in pathological states. (sbhsciences.com)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Serine Palmitoyltransferase, Long Chain Base Subunit 3 (SPTLC3) in tissue homogenates, cell lysates and other biological fluids. (1elisakits.com)
  • Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Serine Palmitoyltransferase, Long Chain Base Subunit 3 (SPTLC3) in samples from tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species. (1elisakits.com)
  • High IL2RA expression is associated with CRLF2-rearranged acute lymphoblastic leukemia. (cusabio.com)
  • Coagulation reactions leading to thrombin generation and activation of factor XIII. (medscape.com)
  • Programmed death ligand 1 (PD-L1), a mediator of the PD-1 receptor, plays an inhibitory role in cancer immune responses. (cancer-genetics.org)
  • The receptor is involved in the regulation of immune tolerance by controlling regulatory T cells (TREGs) activity. (cusabio.com)
  • Finally, we show that LIF increases the expression of the core transcription factors: Klf4, Fbx15, Nanog, Sox2 and c-Myc. (karger.com)