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IL-18 is a proinflammatory cytokine. This cytokine can induce the IFN-gamma production of T cells. The combination of this cytokine and IL12 has been shown to inhibit IL4 dependent IgE and IgG1 production, and enhance IgG2a production of B cells. IL-18 binding protein (IL18BP) can specifically interact with this cytokine, and thus negatively regulate its biological activity.

Obestatin is a hormone that is produced in the cells lining the stomach and small intestine of several mammals including humans; it drastically reduces appetite in mice and is expected to do the same in humans. Obestatin is a peptide hormone - a relatively small protein. It is encoded by the same gene that also encodes ghrelin, a peptide hormone that increases appetite. The protein produced by that gene breaks into two smaller peptides, ghrelin and obestatin. Ghrelin is an endogenous ligand for the growth hormone secretagogue receptor and is involved in regulating growth hormone release. Ghrelin is derived from a preprohormone called preproghrelin, which also generates a second peptide called obestatin. Ghrelin is an endogenous ligand for the orphan G protein-coupled receptor GPR39 and is involved in satiety and decreased food intake.

BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.

MANF is a 20kDa protein which belongs to the ARMET family. MANF was originally known as an arginine-rich region protein which was extremely mutated in a large number of tumors. MANF Expression is induced during ER stress, signifying that MANF takes part in protein quality control during ER stress.

Complement factor H (CFH) is an important regulatory component of the alternative pathway of complement. CFH is prevents complement activation on host cells and tissues, mainly the kidney. CFH controls the formation and decay of the alternative pathway C3/C5 convertase and acts as a cofactor for factor I which proteolytically inactivates C3b when C3b is bound to factor H. The N-terminal 5 domains of CFH bind to C3b and inhibit binding of factor B thus reducing the formation of C3/C5 convertase. CFH also binds to preformed C3/C5 convertases and causes quick release of the catalytic subunit Bb. These activities are necessary for controlling the spontaneous activation of the alternative pathway amplification process in plasma. In addition, CFH controls the formation and decay of these enzymes when C3b is attached to the surface of particles.

IL2 is a secreted cytokine that is important for the proliferation of T and B lymphocytes. The receptor of this cytokine is a heterotrimeric protein complex whose gamma chain is also shared by interleukin 4 (IL4) and interleukin 7 (IL7). The expression of this gene in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the precise expression of a single gene. The targeted disruption of a similar gene in mice leads to ulcerative colitis-like disease, which suggests an essential role of this gene in the immune response to antigenic stimuli.

IL2 is a secreted cytokine that is important for the proliferation of T and B lymphocytes. The receptor of this cytokine is a heterotrimeric protein complex whose gamma chain is also shared by interleukin 4 (IL4) and interleukin 7 (IL7). The expression of this gene in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the precise expression of a single gene. The targeted disruption of a similar gene in mice leads to ulcerative colitis-like disease, which suggests an essential role of this gene in the immune response to antigenic stimuli.

Tumor necrosis factor is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is involved in systemic inflammationand secreted mainly by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.

DFF is a heterodimeric protein of 40kDa (DFFB) and 45kDa (DFFA) subunits. DFFA (DNA fragmentation factor subunit alpha) is the substrate for caspase-3 and triggers DNA fragmentation during apoptosis. DFF is activated once DFFA is cleaved by caspase-3. The cleaved fragments of DFFA detach from DFFB (the active component of DFF), which in turn triggers DNA fragmentation as well as chromatin condensation during apoptosis. Apoptosis is accompanied by shrinkage and fragmentation of the cells and nuclei and degradation of the chromosomal DNA into nucleosomal units.
A reduced level of DFFA detected in ovarian endometriosis may be a part of an apoptosis-resistant mechanism enhancing the disease progression.
DFFA at chromosome 1 shows rare allelic variants in neuroblastoma tumors.

TCEB1 (elongin C) is a subunit of elongin, which is a common transcription elongation factor that increases the RNA polymerase II transcription elongation past template encoded arresting sites. The SIII complex is comprised of elongins A/A2, B and C. The SIII complex activates elongation by RNA polymerase II by curbing transient pausing of the polymerase at numerous sites within transcription units. Elongin A acts as the transcriptionally active component of the SIII complex, while elongins B and C are regulatory subunits. Elongin A2 is specifically expressed in the testis, and able to forming a stable complex with elongins B and C. The VHL (von Hippel-Lindau) tumor suppressor protein binds to elongins B and C, and thus inhibits transcription elongation.

Eukaryotic initiation factor 4A-III (EIF4A3) is a member of the DEAD box helicase family and eIF4A subfamily. DEAD box proteins, distinguished by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. These proteins are involved in several cellular processes including alteration of RNA secondary structure, such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. EIF4A3 is a part of a splicing-dependent multiprotein exon junction complex (EJC) accumulated at splice junction on mRNAs. Based upon their distribution patterns, some members of the DEAD box helicase family are thought to be involved in embryogenesis, spermatogenesis, and cellular growth and division.

EDF1 controls endothelial cell differentiation. EDF1 has a role as a bridging protein that interconnects regulatory proteins and the basal transcriptional machinery, thus modulating the transcription of genes that take part in endothelial differentiation. EDF1 binds calmodulin through its IQ domain and controls nitric oxide synthase activity via calmodulin sequestration in the cytoplasm. EDF1 is localized in adult liver, heart, adipose tissues, intestine and pancreas.

CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. 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. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription 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.
CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy.

MANF is a 20kDa protein which belongs to the ARMET family. MANF was originally known as an arginine-rich region protein which was extremely mutated in a large number of tumors. MANF Expression is induced during ER stress, signifying that MANF takes part in protein quality control during ER stress.

Chemokine (C-X-C motif) ligand (CXCL7) is a small cytokine belonging to the CXC chemokine family. It is a protein that is released in large amounts from platelets following their activation. It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.

Elongin B (Elob) is a subunit of the transcription factor B (SIII) complex. SIII complex is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. The SIII complex comprised of a transcriptionally active subunit (A) and 2 regulatory subunits (B and C). Subunit A is transcriptionally active and its transcription activity is enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C. The von Hippel-Lindau tumor suppressor protein binds to elongin B and C and inhibits transcription elongation.

NXT1 operates as a nuclear export factor in both RAN and CRM1 dependent pathways. NXT1 is known to stimulate the export of U1 snRNA in RAN (Ras-related nuclear protein) and CRM1 (chromosome region maintenance) dependent pathways and the export of tRNA and mRNA in a CRM1-independent pathway. This protein heterodimerizes with Tap protein and regulates the ability of Tap protein to intermediate nuclear mRNA export.

TNFRSF17 is a receptor for tnfsf13b/blys/baff and tnfsf13/april. TNFRSF17 promotes b-cell survival and plays a role in the regulation of humoral immunity. TNFRSF17 activates nf-kappa-b and jnk. TNFRSF17 is a member of the TNF-receptor superfamily. TNFRSF17 is expressed in mature B lymphocytes, and is invloved in B cell development and autoimmune response. TNFRSF17 specifically binds to the tumor TNFSF13B/TALL-1/BAFF, which causes NF-kappaB and MAPK8/JNK activation. TNFRSF17 binds to a variety of TRAF family members, and therefore transduces signals for cell survival and proliferation. TNFRSF17 is a type III membrane protein having 1 extracellular cysteine rich domain. Within the TNFRSF, it shares the highest homology with TACI. BCMA and TACI have both been shown to bind to APRIL and BAFF, members of the TNF ligand superfamily. BCMA expression has been found in immune organs. TNFRSF17 appears to be localized to the Golgi compartment. The binding of BCMA to APRIL or BAFF has been shown to stimulate IgM production in peripheral blood B cells and increase the survival of cultured B cells.

Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets. Its major physiologic role appears to be neutralization of molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemokine family. Furthermore it is used as an inhibitor in the angiogenesis during tumor therapy.

Eukaryotic translation initiation factor 3 subunit J (EIF3J) is a member of the EIF-3 subunit J family. EIF3 has a crucial role in binding of initiator methionyl-tRNA and mRNA to the 40S ribosomal subunit to produce the 40S initiation complex. EIF3J binds to the aminoacyl (A) site and mRNA access channel of the 40S subunit, setting EIF3J directly in the ribosomal decoding center. In addition, EIF3J interacts with eIF1A and reduces 40S subunit affinity for mRNA. An elevated affinity for mRNA is restored upon enlistment of initiator tRNA, despite the fact EIF3J remains in the mRNA-binding cleft in the presence of tRNA.

ARF6 is a part of the ADP ribosylation factor family of GTP-binding proteins. ARF6 is restricted to the plasma membrane, and controls vesicular trafficking, remodeling of membrane lipids, and signaling pathways which lead to actin remodeling. Furthermore, ARF6 is a key player in conservation of organelle integrity, assembly of coat proteins and activation of phospholipase D.

Eukaryotic Translation Elongation Factor 1 Gamma (EEF1G) takes part in anchoring the complex to additional cellular components. EEF1G is a multi-protein complex which is in charge of the delivery of aminoacyl-tRNAs to the ribosome. Over expression of EEF1G is linked with pancreatic cancer, due to the role of EEF1G protein in the oncogenic transformation process.

TNFR2 belongs to the TNF-receptor superfamily. TNFR2 is receptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. TNFR2 mediates the majority of the metabolic effects of TNF-alpha. In addition, knockout studies in mice propose a role for TNFR2 in protecting neurons from apoptosis by stimulating antioxidative pathways. TNFR2 expression might have a significant role in the angiogenesis, tumor cell proliferation and metastasis of Invasive micropapillary carcinoma of the breast.
There are 2 types of soluble TNF receptors: sTNFR-I and sTNFR-II, which act to neutralize the biological activities of TNF alpha and TNF beta. The levels of these soluble receptors seem to increase as a result of shedding of the extracellular domains of the membrane bound receptors. High levels of soluble TNF receptors are found in the amniotic fluid of pregnant women. TNFR2 and TNFR1 form a heterocomplex which mediates the recruitment of 2 anti-apoptotic proteins, c-IAP1 and c-IAP2, which possess E3 ubiquitin ligase activity. IAPs’ function in TNF-receptor signaling is unknown; nevertheless, c-IAP1 is believed to potentiate TNF-induced apoptosis by the ubiquitination and degradation of TNF-receptor-associated factor 2, which mediates anti-apoptotic signals. Oxidative stress promotes TNFR1 and TNFR2 self-interaction, ligand-independent and enhanced ligand-dependent TNF signaling. TNF-a, TNFR1 and TNFR2 have roles in cellular differentiation. TNFR1 and TNFR2 function in cell type-specific renal injury.