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Pathways

Signaling Pathways

Displaying 241 to 252 (of 533 pathways)

Our chemical senses, taste and smell, are our oldest senses. Long before organisms could hear or see, they needed to find nutrients, had to avoid toxic substances, and they were attracted by signaling molecules that were released by their mating partners. Right from the beginning of evolution, the task of our chemical senses was not to merely identify the chemical compounds encountered by the organism, but to directly initiate behavioral responses. This sense of smell has long remained the most enigmatic of our senses. The basic principles for recognizing and remembering about 10,000 different odors were not understood. To address the problem of olfactory perception at a molecular level, this year's Nobel Laureates Richard Axel (Howard Hughes Medical Institute,[..]

Neuronal growth cones in the developing nervous system are guided to their targets by attractive and repulsive guidance molecules, which include members of the Netrin, Semaphorin, Ephrin, and Slit protein families. Slit is a ~200 KD secretory protein originally shown to be expressed by neurons and glial cells. Slit was originally identified in Drosophila as an extracellular cue to guide axon pathfinding, to promote axon branching, and to control neuronal migration (Ref.1). Mammalian Slit consists of three members, Slit1, Slit2, and Slit3. All are expressed in the nervous system but Slit1 is specifically expressed in brain, whereas Slit2 and Slit3 are expressed in brain as well as kidney, lung, heart, spleen, and lymph nodes. A prototypical Slit protein contains an[..]

BMP (Bone Morphogenetic Protein) Receptors are essential, beyond the egg cylinder stage, for myocyte-dependent functions and signals in cardiac organogenesis. ALK3 (Activin Receptor-Like Kinase-3) is specifically required at mid-gestation for normal development of the trabeculae, compact myocardium, interventricular septum and endocardial cushion. The invariable defects in myocardium results from congenital deletion of ALK3 and this provide strong support for its assessment as a candidate gene in human congenital heart disease. BMPs like BMP2, BMP4 and BMP5, BMP7, BMP10, bind to Serine/threonine kinase receptors, Type-I (ALK3 and ALK6) and Type-II, BMPR2 (Bone Morphogenetic Protein Receptor Type-II), respectively, and form a heteromeric signaling complex acting in[..]

Cardiac myocyte proliferation and their differentiation early in development are dependent on the coordinate expression and action of SRF (Serum Response Factor), GATA4 (GATA Binding Protein-4) and the homeodomain factor NKX2.5 (NK2 Transcription Factor Related Locus-5). All three of these factors are expressed in developing cardiomyocytes and induce expression of cardiac genes. HOP (Homeodomain-Only Protein) physically interacts with SRF and inhibits activation of SRF-dependent transcription by inhibiting SRF binding to DNA. HOP gene encodes the smallest known homeodomain protein. HOP acts to modulate SRF-dependent transcription and cardiac-specific gene expression in the absence of intrinsic DNA binding capability. Although HOP is a homeodomain protein, it lacks a[..]

Neuronal growth cones in the developing nervous system are guided to their targets by attractive and repulsive guidance molecules, which include members of the netrin, semaphorin, ephrin, and Slit protein families. The Eph family forms the largest group of RTKs (Receptor Tyrosine Kinases) comprising 14 members in mammals that play critical roles in diverse biological processes during development as well as in the mature animal. They are activated by membrane-bound ligands called Ephrins, which are classified into two subclasses based on their modes of membrane anchorage. The EphrinA ligands are tethered to the plasma membrane by GPI (Glycosylphosphatidylinositol) anchor and prefer to bind to EphA Receptors. The EphrinB ligands (EphrinB1–B3), which possess a[..]

Yersinia pestis, is a facultative intracellular a gram-negative bacillus responsible for causing bubonic plague (Ref.1).  Apart from Y. pestis, two other pathogenic Yersinia species, Yersinia enterocolitica, Y. pseudotuberculosis, are known to infect human and animal hosts and cause a variety of intestinal and septicemic diseases.  All three species harbor a virulence plasmid, which encodes a type III secretion system (T3SS) for secreting Yop(Yersinia outer membrane proteins) protein substrates, to establish a successful infection (Ref.1). While Y. pestis is responsible for the outbreak of plague, infections with Y. enterocolitica and Y. pseudotuberculosis generally cause gastroenteritis and lymphadenitis (Ref.2). Infection is most often[..]

Much of the efficiency of the immune system is attributed to the high degree of spatial and temporal organization in the secondary lymphoid organs. Signaling through the LT-BetaR (Lymphotoxin-Beta Receptor) pathway is a crucial element in the maintenance of this organised microenvironment (Ref.1). LT-BetaR, a member of the TNFR (Tumor Necrosis Factor Receptor) superfamily, plays important roles in embryonic development and organization of secondary lymphoid tissues and maintenance of their architecture in adults (Ref. 2). LT-BetaR is expressed on most cell types including cells of fibroblast, epithelial, and myeloid lineages but not on T or B lymphocytes. It can bind to specific ligands, such as: the membrane form of lymphotoxin heterotrimmer, LT-Alpha1Beta2[..]

BTG2 (BTG Family Member-2) is endowed with antiproliferative activity. The expression of BTG2 in cycling cells induces accumulation of hypophosphorylated, growth-inhibitory forms of Rb (Retinoblastoma) and led to G1 arrest through impairment of DNA synthesis. Overexpression of CcnD1 (Cyclin-D1) counteracts G1 arrest. Rb is a nuclear phosphoprotein whose phosphorylation state oscillates regularly during the cell cycle. Its under-phosphorylated forms predominate in G0 and G1, while highly phosphorylated forms exist in S, G2 and M phases (Ref.1). The primary biological function of under-phosphorylated Rb is to inhibit progression toward S phase by controlling a checkpoint in late G1. In fact, under-phosphorylated Rb associates with members of the E2F family of[..]

In response to a variety of extracellular stimuli, actin filament assembly at the leading edge of motile cells causes protrusion during cell crawling and chemotaxis, nerve growth and cell spreading. The actin filament network immediately under the plasma membrane in regions of rapid cellular protrusion consists of short, branched filaments while those deeper in the cortex, as well as at focal adhesions, stress fibers and in microvilli, are much longer and rarely branched (Ref.1). The dynamic organization of the actin cytoskeleton provides the force for cell motility and is regulated by small GTPases of the Rho family, in particular Rac1, RhoA and CDC42. The microtubule cytoskeleton is also polarized in a migrating cell, and in addition to organizing the actin[..]

Tumor necrosis factor (TNF) is a pro-inflammatory cytokine with the capacity to induce apoptosis. It is enriched in the tumor microenvironment, promotes tumor growth and subverts innate immune responses to cancer cells. TNF is the best studied member of the TNF superfamily. TNF-alpha can bind to two related receptors, TNF receptors 1 and 2 (TNFR1 and TNFR2), which are also used by other, similar ligands. By binding to TNFR1 and TNFR2, TNF activates distinct signaling pathways important for cell proliferation, cell death and immune responses (Ref.1 and 2). TNFR1 is constitutively expressed in most cell types (Ref.3).The default effect of TNF stimulation is to activate the nuclear factor-kappaB (NF-kappaB) pathway and mediate inflammation. TNFR1 mediates the cytotoxic[..]

Tumor necrosis factor (TNF) is a pro-inflammatory cytokine with the capacity to induce apoptosis. It is enriched in the tumor microenvironment, promotes tumor growth and subverts innate immune responses to cancer cells. TNF is the best studied member of the TNF superfamily. TNF-alpha can bind to two related receptors, TNF receptors 1 and 2 (TNFR1 and TNFR2), which are also used by other, similar ligands. By binding to TNFR1 and TNFR2, TNF activates distinct signaling pathways important for cell proliferation, cell death and immune responses (Ref.1 and 2). TNFR2 is typically restricted to certain subpopulations of immune cells such as CD4+ or CD8+ T cells and a few other cell types such as oligodendrocytes and endothelial cells (Ref.3).TNFR2 signaling has significant[..]

UV radiation induces two of the most abundant mutagenic and cytotoxic DNA lesions such as  CPD  (Cyclobutane-Pyrimidine Dimers) or 6-4PPs (6-4 Pyrimidine Pyrimidone). The most common covalently linked adjoining pyrimidines are TT(Thymine dimers), T-C (Thymine-Cytosine dimers) and C-C (Cytosine-Cytosine dimers). T-T dimers cause kinks in the DNA strand that prevent both replication and transcription of that part of the DNA. Because they block DNA replication (and therefore prevent cells from reproducing), T-T dimers and other forms of UV damage cannot be inherited, and thus do not constitute mutations. Such kinds of DNA damage are known as premutational lesions because they prevent both transcription and replication of the genes in which they are present and[..]

Displaying 241 to 252 (of 533 pathways)
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