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Signaling Pathways

Displaying 313 to 324 (of 537 pathways)

NF-KappaB (Nuclear Factor-KappaB) is a heterodimeric protein composed of different combinations of members of the Rel family of transcription factors. The Rel/ NF-KappaB family of transcription factors are involved mainly in stress-induced, immune, and inflammatory responses. In addition, these molecules play important roles during the development of certain hemopoietic cells, keratinocytes, and lymphoid organ structures. More recently, NF-KappaB family members have been implicated in neoplastic progression and the formation of neuronal synapses. NF-KappaB is also an important regulator in cell fate decisions, such as programmed cell death and proliferation control, and is critical in tumorigenesis (Ref.1).NF-KappaB is composed of homo- and heterodimers of five members[..]

Interleukin 3 (IL3) is a T cell-derived glycoprotein involved in cell proliferation, survival and differentiation. It regulates haemopoiesis, the formation of blood cells in the body. IL3, also called multi-CSF (multi-lineage colony stimulating factor), is produced by T cells and mast cells, after activation with mitogens or antigens. It was first isolated from murine bone marrow cells and is also believed to be expressed in neurons and astrocytes of the hippocampus, suggesting an important role in central nervous system (Ref.1). It signals through interactions with cell surface receptors.    IL3 receptor (IL3R) is composed of two polypeptide chains, a unique alpha subunit and a common Beta subunit IL3RB (the common beta chain), which is shared by[..]

PKR (Protein kinase-R) is a ubiquitously expressed serine-threonine kinase that has been implicated as a signal integrator in translational and transcriptional control pathways.  PKR mediate apoptosis induced by many different stimuli, such as LPS (Lipopolysaccharides), IFN-Gamma (Interferon-Gamma), cytokines, growth factor, viral infection, or serum starvation.  PKR activity is regulated by external signals, which act on proteins, which interact with PKR. Among the proteins identified so far are p58, a cellular protein, K3L, the product of a gene of vaccinia virus,  PACT  (Protein Activator Of Interferon-Induced Protein Kinase) and p67, an interferon-induced glycoprotein (Ref.1). Human PKR is a 68 kDa with a 20 kDa N-terminal dsRBD[..]

Complement is a complex system containing more than 30 various glycoproteins present in serum in the form of components, factors, or other regulators and/or on the surface of different cells in the form of receptors. It is a highly sophisticated host defence system designed to destroy pathogens. Once the complement system is activated, a chain of reactions involving proteolysis and assembly occurs, resulting in destruction of the membranes of pathogens. The cascade up to the cleavage of C3 (Complement component 3), which plays a central role in the complement system, is called the activation pathway. There are three categories of complement pathway; the classical pathway, alternative pathway and lectin pathway (Ref.1).The recently discovered lectin pathway (also called[..]

Anthrax is a severe, although rather rare, infectious disease that is caused by the Gram-positive, spore-forming bacterium Bacillus anthracis. The infectious form is the spore and the major virulence factors of the bacterium are its poly-Gamma-D-glutamic acid capsule and the tripartite anthrax toxin. The discovery of the anthrax toxin receptors in the early 2000s has allowed in-depth studies on the mechanisms of anthrax toxin cellular entry and translocation from the endocytic compartment to the cytoplasm. There are three forms of anthrax disease defined by the route of spore entry into the body: cutaneous, gastrointestinal, and inhalational anthrax. Early studies showed that spores are phagocytosed by resident macrophages and dendritic cells, which may serve as a[..]

Reelin is a large extracellular glycoprotein involved in the development of architectonic patterns, particularly in the cerebral cortex and hippocampus, where primarily Cajal-Retzius cells synthesize it The Reelin signaling pathway controls neuronal migration and positioning in central nervous system (CNS) development, as well as synaptic plasticity and memory (Ref.1).  Reelin is localized to chromosome 7 in human with serine protease activity containing 3461 amino acids. It contains a signal peptide followed by an N-terminal sequence and a hinge region upstream from eight Reelin repeats of 350–390 amino acids. Each Reelin consists of a signal peptide (S), an F-spondin-like domain (SL), eight consecutive Reelin repeats (R) each harboring an epidermal growth[..]

Tumor necrosis factor (TNF)-like weak inducer of apoptosis (TWEAK) is a member of the tumor necrosis factor (TNF) superfamily (TNFSF) that is induced in a variety of cell types in situations of tissue injury. It is expressed in various tissues including the intestine, pancreas, lung, brain, skeletal muscle, heart and vasculature. The 249 amino acid-comprising membrane-bound form of TWEAK consists extracellularly of the characteristic C-terminally located TNF homology domain (THD), which is separated from the transmembrane domain by a stalk region of about 55 amino acids. It can be cleaved by furin endoprotease into a soluble TWEAK (sTWEAK) (185 aa, 18 kDa) which then binds to the Fibroblast growth factor-inducible 14 (Fn14) receptor on the cell, the cognate receptor of[..]

Rap1 (Krev-1/smg p21), a small-molecular-weight GTP-binding protein that belongs to the Ras-like superfamily of GTPases, is involved in signal transduction cascades. It is highly homologous to Ras but it is down regulated by its own set of GAPs (GTPase-Activating Proteins). Rap1 is implicated in the regulation of a variety of cellular processes including the control of platelet activation, T-cell anergy, B-Cell activation, and neuronal differentiation. Very recently, Rap was shown to be involved in the control of cell adhesion, in particular the regulation of integrin activation by inside-out signaling. In humans, four isoforms of Rap, Rap1A, Rap1B, Rap2A, and Rap2B, exist. Rap1A  and Rap1B  share more than 90% sequence identity. Rap1A/B is the closest[..]

GPCRs (Guanine Nucleotide Binding–Protein Coupled Receptors) comprise large and diverse gene families in fungi, plants, and the animal kingdom. Also termed serpentine receptors, GPCRs are polytopic membrane proteins that share a common structure with seven transmembrane segments, but sequence similarity is minimal among the most distant GPCRs. Their principal function is to transmit information about the extracellular environment to the interior of the cell, and they do this by interacting with the G-proteins. GPCRs recognize a variety of ligands and stimuli including peptide and non-peptide hormones and neurotransmitters, chemokines, prostanoids and proteinases, biogenic amines, nucleosides, lipids, growth factors, odorant molecules and light. These receptors[..]

Tumor necrosis factor (TNF) superfamily proteins consisting of 19 members and 29 receptors regulate cell proliferation, cell death, and morphogenesis. The tumor necrosis factor superfamilies members provide key communication signals between various cell types during development, especially in the skin, bones, and lymphoid organs, and maintain organ homeostasis and initiate tissue responses. Because of these essential roles, TNFRSFs and the TNF superfamily (TNFSF) ligands are attractive targets for treating diverse diseases, such as autoimmunity, cancer, infectious diseases, and graft-versus-host disease (Ref.1 and 2). The TNF-related ligands assemble into trimers that form a highly efficient receptor-clustering and signal-initiating mechanism. TNF receptors share a[..]

TLRs (Toll-like receptors) are transmembrane proteins expressed by cells of the innate immune system, which recognize invading microbes and activate signaling pathways that launch immune and inflammatory responses to destroy the invaders. Toll receptors were first identified in Drosophila. In mammals, the TLR family includes eleven proteins (TLR1-TLR11). Recently, two new members, TLR12 and TLR13 have been discovered in mouse, but not much information is known about them. Mammalian TLRs consist of an extracellular portion containing Leucine-rich repeats, a transmembrane region and a cytoplasmic tail, called the TIR (Toll-IL-1R (Interleukin-1-Receptor)) homology domain. Different TLRs serve as receptors for diverse ligands including Bacterial cell wall components, viral[..]

TRAIL (TNF-Related Apoptosis-Inducing Ligand) is a protein consisting of 281 amino acids. It is also called Apo2L. Five proteins, TRAILR1 (DR4), TRAILR2 (DR5/ TRICK2 or KILLER), TRAILR3 (DcR1/ TRID or LIT), TRAILR4 (DcR2 or TRUNDD), and Opg (Osteoprotegerin), have been identified as TRAIL receptors. Both TRAILR1 and TRAILR2 contain the functional DD (Death Domain), capable of inducing apoptosis. The other three receptors DcR1, DcR2 and Opg serve as "decoy" receptors. These three receptors can bind to TRAIL, but cannot induce apoptosis. DcR1 is a glycosylphosphatidylinositol-anchored cell surface protein, which contains the TRAIL-binding region as well as a region that anchors the receptor to the membrane. But unlike the other receptors, DcR1 lacks an[..]

Displaying 313 to 324 (of 537 pathways)


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