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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.

The Epstein-Barr virus (EBV), also called Human herpes virus 4 (HHV-4), is a virusof the herpes family(which includes Herpes simplex virusand Cytomegalovirus. On infecting the B-lymphocyte, the linear virus genome circularizes and the virus subsequently persists within the cell as an episome. The virus can execute several distinct programs of gene expressionwhich can be broadly categorized as being lytic cycle or latent cycle. The lytic cycleor productive infection results in staged expression of a host of viral proteinswith the ultimate objective of producing infectious virions. Formally, this phase of infection does not inevitably lead to lysis of the host cellas EBV virions are produced by budding from the infected cell. The latent cycle(lysogenic) programs are those that do not result in production of virions. A very limited, distinct set of viral proteins are produced during latent cycle infection. These include Epstein-Barr nuclear antigen(EBNA)-1, EBNA-2, EBNA-3A, EBNA-3B, EBNA-3C, EBNA-leader protein (EBNA-LP) and latent membrane proteins(LMP)-1, LMP-2A and LMP-2B and the Epstein-Barr encoded RNAs(EBERs).

The protein encoded by this gene is a member of the glial cell line-derived neurotophic factor (GDNF) family of ligands which are a group of ligands within the TGF-beta superfamily of signaling molecules. GDNFs are unique in having neurotrophic properties and have potential use for gene therapy in neurodegenrative disease. Artemin has been shown in culture to support the survival of a number of periferal neuron populations and at least one population of dopaminergic CNS neurons. Its role in the PNS and CNS is further substantiated by its expression pattern in the proximity of these neurons. This protein is a ligand for the RET receptor and uses GFR-alpha 3 as a coreceptor. Four alternatively spliced transcripts have been described, two of which encode the same protein.

S100A9 is part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100A9 protein is localized in the cytoplasm and/or nucleus of a wide range of cells, and participates in the regulation of several cellular processes such as cell cycle progression and differentiation. S100 genes include no less than 13 proteins which are localized as a cluster on chromosome 1q21. S100A9 is involved in the inhibition of casein kinase and altered expression of this protein is associated with the disease cystic fibrosis.

GDF8 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. This gene is thought to encode a secreted protein which negatively regulates skeletal muscle growth.

Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.

IL18R1 (interleukin 18 receptor 1) is an interleukin receptor which is part of the immunoglobulin superfamily. IL18R1 comprises 3 Ig-like C2-type domains, on TIR domain IL18R1 shares many immuno-regulatory functions with IL12. IL12 and IFN-alpha are found to induce the expression of IL18 receptor in NK & T cells. Moreover, IL18R1 explicitly binds interleukin 18, and is vital for IL18 mediated signal transduction. IL18R1 does not bind IL1A or IL1B beta, however it does bind to the agonist which causes NF-kappa-B to become active.

CD18 (ITGB2 or integrin beta-2) is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. CD18 may be a member of an extended family of cell surface molecules including the fibronectin binding protein. In addition, CD18 is a complement receptor type 3 (CR3). CD18 triggers neutrophil transmigration during lung injury through PTK2B/PYK2-mediated activation.

UBE2K belongs to the ubiquitin-conjugating enzymes family which take part in many cellular processes such as selective protein degradation, DNA repair, cell cycle control, and sporulation. In this mechanism, the ATP-coupled activation and subsequent ligation of ubiquitin are catalyzed by separate enzymes functionally linked by ubiquitin carrier protein UBC1. In addition, UBE2K is involved in Alzheimer's disease, Huntington's disease and antigen processing through its interaction with amyloid-?, huntingtin, and MHC-heavy chain proteins.

Ubiquitin-conjugating enzyme E2 R2 (UBE2R2) is a member of the ubiquitin-conjugating enzyme family. Protein kinase CK2 is a ubiquitous and pleiotropic Ser/Thr protein kinase implicated in cell growth andtransformation. This protein is a protein similar to the E2 ubiquitin conjugating enzyme UBC3/CDC34. Studies propose that CK2-dependent phosphorylation of this ubiquitin-conjugating enzyme functions by regulating beta-TrCP substrate recognition and induces its interaction with beta-TrCP, enhancing beta-catenin degradation. UBE2R2 receives ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes monoubiquitination and 'Lys-48'-linked polyubiquitination. UBE2R2 may be implicated in degradation of katenin. Among the diseases associated with UBE2R2 are cblc, and herpes simplex.

IFN-Induced Protein With Tetratricopeptide Repeats 3, also known as IFIT3 is a member of the IFIT family. IFN-induced antiviral protein which performs as an inhibitor of cellular and viral processes, cell migration, proliferation, signaling, as well as viral replication. Furthermore, IFIT3 is significantly induced upon RNA virus infection. Ectopic expression or alternatively knockdown of IFIT3 might, respectively, enhance or impair IRF3-mediated gene expression.

BCL2 gene encodes an integral outer mitochondrial membrane protein that blocks the apoptotic death of some cells such as lymphocytes. Constitutive expression of BCL2, such as in the case of translocation of BCL2 to Ig heavy chain locus, is thought to be the cause of follicular lymphoma. Two transcript variants, produced by alternate splicing, differ in their C-terminal ends.

BCL2 Like 10 (BCL2L10) is a member of the BCL-2 protein family. BCL2 family members form hetero or homodimers and serve as anti or pro-apoptotic regulators which are involved in a wide variety of cellular activities. BCL2L10 includes the conserved BH4, BH1 and BH2 domains. BCL2L10 interacts with other members of BCL2 protein family including BCL2, BCL2L1/BCL-X(L), and BAX. BCL2L10 overexpression suppresses cell apoptosis possibly through the prevention of cytochrome C release from the mitochondria, and consequently activating caspase-3 activation.

BCL2L2 promotes cell survival. BCL2L2 mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX. BCL2L2 is part of the BCL-2 protein family which form hetero- or homodimers and play an important role as anti and proapoptotic regulators. BCL2L2 causes reduced cell apoptosis under cytotoxic conditions. BCL2L2 is involved in the survival of NGF- and BDNF-dependent neurons. BCL2L2 plays an important role in adult spermatogenesis.

BLNK is a cytoplasmic linker or adaptor protein which has a significant role in B cell development. B-cell linker (BLNK) is essential for normal B-cell development. BLNK bridges B cell receptor-associated kinase activation with downstream signaling pathways, thus affecting different biological functions. BLNK associates with the effector proteins GRB2, Vav, NCK and PLC-g following activation of the B cell receptor. BLNK is phosphorylated by the Syk tyrosine kinase, which in turn permits activation of downstream effector proteins including GRB2 and PLC-g. Mutations in the BLNK gene cause hypoglobulinemia and absent B cells, a disease in which the pro- to pre-B-cell transition is developmentally blocked. Deficiency in the BLNK protein is seen in some cases of pre-B acute lymphoblastic leukemia.

THYN1, is greatly conserved among vertebrates and plant types. TYHN1 takes part in the induction of apoptosis. THYN1 in the thymocytes was primarily found in the nucleus, as shown in lymphoma cells, demonstrating that the THYN1 is localized in the nucleus, regardless of the cyclic or resting stage of the cell cycle.

UBE2D2 belongs to the E2 ubiquitin-conjugating enzyme family. UBE2D2 takes part in the ubiquitination of the tumor-suppressor protein p53, which is induced by an E3 ubiquitin-protein ligase. UBE2D2 catalyzes ubiquitination of IkB-alpha in a SCFB-TRCP and phosphorylation dependent method.

Protein modification with ubiquitin is an essential cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least 3 classes of enzymes: ubiquitin-activating enzymes (E1s) ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). Ubiquitin-Conjugating Enzyme E2G (UBE2G1) belongs to the E2 ubiquitin-conjugating enzyme family and catalyzes the covalent attachment of ubiquitin to other proteins. UE2G1 protein is involved in degradation of muscle-specific proteins.

Ubiquilin-2, also known as UBQLN2 contains an N-terminal ubiquitin-like domain and a C-terminal ubiquitin-associated domain. UBQLN2 is physically linked with proteasomes as well as ubiquitin ligases, and therefore is considered to functionally connect the ubiquitination machinery to the proteasome in order to affect in vivo protein degradation. Furthermore, UBQLN2 binds the ATPase domain of the Hsp70-like Stch protein. Among the diseases which are associated with UBQLN2: Amyotrophic lateral sclerosis 15, with or without frontotemporal dementia as well as Amyotrophic lateral sclerosis type 15.

Cytotoxic and Regulatory T Cell Molecule, also known as CRTAM belongs to the immunoglobulin superfamily which complies with the structural characteristics of the JAM family and is phylogenetically more closely related to nectin-like proteins. CRTAM is implicated in epithelial cell adhesion. Furthermore, CRTAM interacts with CADM1 as well as promotes natural killer (NK) cell cytotoxicity.

Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.

Adiponectin is a hormone exclusively expressed from adipose tissue.
Many studies demonstrate that Adiponectin has direct anti-diabetic, anti-atherogenic and anti-inflammatory functions. APM-1 can increase insulin sensitivity of skeletal muscle. Attenuate hepatic lipogenesis and gluconeogenesis, regulate NO production in endothelial cells, inhibit proliferation of smooth muscle cells and prevent lipid accumulation of macrophage cells.
In the circulation, Adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (MMW, also called trimer) forms 8. Different oligomeric complex of Adiponectin activates different signaling pathways and exerts distinct functions.

Adiponectin is an important negative regulator in hematopoiesis and immune systems. It may be involved in ending inflammatory responses through its inhibitory functions. Inhibits endothelial nf-kappa-b signaling through a camp-dependent pathway. Inhibits tnf-alpha- induced expression of endothelial adhesion molecules. Involved in the control of fat metabolism and insulin sensitivity.