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RANKL binds to tnfrsf11b/opg and to tnfrsf11a/rank. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive t-cell proliferation. May be an important regulator of interactions between t-cells and dendritic cells and may play a role in the regulation of the t-cell-dependent immune response. sRANKL may also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy.

Decay-Accelerating Factor Isoform 1 or CD55, is a protein that attached to the cell membrane through glycophosphatidylinositol (GPI) anchor. CD55 regulates the complement system in the outer membrane. The protein is a receptor to many types of enteroviruses such as coxsackieviruses. CD55 is widely scattered amidst hematopoietic & non-hematopoietic cells. The CD55 has a crucial part in tumorigenesis, autocrine loops for cell rescue and evasion of apoptosis, cell motility, invasiveness etc.

Stomatin (STOM) is a part of a highly conserved family of integral membrane proteins. STOM is a membrane protein involved in regulation of monovalent cation transport through lipid membranes which regulates ACCN1 and ACCN3 gating. STOM is a major lipid-raft component of erythrocytes and epithelial cells, and an abundant platelet protein which acts as a cytoskeletal anchor.

NDK (Nucleoside diphosphate kinase) exists as a hexamer composed of 'A' (encoded by NME1) and 'B' (encoded by NME2) isoforms. NME1 is involved in cell proliferation, differentiation and development, signal transduction, G protein-coupled receptor endocytosis, and gene expression. It also has tumor metastasis-suppressive capacity. NME1 has a key role in the synthesis of nucleoside triphosphates other than ATP. NME1 is essential for neural development including neural patterning and cell future determination.
The NME1 gene is expressed in various tumor types where its levels have been alternatively linked to reduced or increased metastatic potential.
Decrease in NME1 expression is notably connected to aggressive behavior in melanoma, breast, colon, and gastric carcinomas. In contrast, elevated levels of NME1 gene expression are noted in the advanced stage of thyroid carcinomas.
Somatic mutations of the NME1 gene are found in neuroblastoma. Increased NME1 in neuroblastoma is linked to features of the disease that are associated with aggressive tumors.

Follicular Dendritic Cell Secreted Protein (FDCSP) is a small secreted protein which is found in follicular dendritic cells. The FDCSP protein specifically binds to activated B cells, and serves as a regulator of antibody responses. In addition, FDCSP is assumed to contribute to tumor metastases by promoting cancer cell migration and invasion. FDCSP binds to the surface of B-lymphoma cells, but not T-lymphoma cells, which is consistent with a function as a secreted mediator acting upon B-cells. FDCSP is abundantly expressed in the tonsil, lymph node, and tracheam, having a strong expression in the prostate and a lower expression in the thyroid, stomach and colon.

Native human C4 is aglycosylated polypeptide containing 3 disulfide-linked chains. C4 is essential to the activation of both thelectin and the classical pathways of complement activation.Initiation of each pathway generates proteolytic enzyme complexes which are bound to the target surface. These enzymes cleave a peptide bond in C4 releasing the anaphylatoxin C4a and activating C4b. Like C3, the thioester of metastable C4b is highly reactive and is capable of reacting and covalently coupling C4b to amino or hydroxyl groups on the target surface. C4A and C4B are 2 variants of C4 that are common in manwhereas, in animals who have only 1 type usually have C4B.

CAMP belongs to the antimicrobial peptide family, contains highly conserved N-terminal signal peptide, a cathelin domain and a structurally variable cationic antimicrobial peptide that produced by extracellular proteolysis from the C-terminus. CAMP has numerous functions besides the antimicrobial activity such as: cell chemotaxis, immune mediator induction and inflammatory response regulation.

Acetoacetyl-CoA thiolase (ACAT1) is an enzyme member of the membrane-bound acyltransferase family and Sterol o-acyltransferase subfamily. The ACAT1 enzyme catalyzes the reversible formation of acetoacetyl-CoA from 2 molecules of acetyl-CoA. ACAT1 plays a part in lipoprotein compilation and dietary cholesterol absorption. Added to its acyltransferase activity, ACAT1 acts as a ligase.

PDCD1 is a cell surface membrane protein of the immunoglobulin superfamily. PDCD1 is expressed in pro-B-cells and is thought to have a role in their differentiation. In mice, expression of PDCD1 gene is induced in the thymus when anti-CD3 antibodies are injected and large numbers of thymocytes undergo apoptosis. Mice deficient for the PDCD1 gene bred on a BALB/c background developed dilated cardiomyopathy and died from congestive heart failure. These studies suggest that the PDCD1 gene product may also be important in T cell function and contribute to the prevention of autoimmune diseases.

IL-29 is distantly related to type I IFNs and the IL-10 family. Expression of IL-29 is induced by viral infection which interacts with a heterodimeric class II cytokine receptor that consists of interleukin 10 receptor, beta (IL10RB) and interleukin 28 receptor, alpha. IL-29 exhibits common features with type I IFNs such as antiviral activity, antiproliferative activity and in vivo antitumour activity.
IL-29 acts similarly to IFNs, but is less effective generally and has activity in a more limited range of cell lines. IFN-ambda 1, IFN-lambda 2 and IFN-lambda3 are closely positioned genes on human chromosome 19.
IL-29 induces ELR(-) CXC chemokine mRNA in human peripheral blood mononuclear cells, in an IFN-gamma-independent manner.
IL-29 is able to generate tolerogenic DCs, an activity that could thwart IFN-beta functions. IL-29 produced in response to viral infection, activates both monocytes and macrophages producing a restricted panel of cytokines and therefore is an important factor in activating innate immune responses at the site of viral infection.
IFN-Lambda 1 antiviral and antiproliferative activity requires IFN-Lambda 2 receptor tyrosine residues.

PFKM is a regulatory glycolytic enzyme that converts fructose 6-phosphate and ATP into fructose 1,6-bisphosphate (through PFK-1), fructose 2,6-bisphosphate (through PFK-2) and ADP. Three phosphofructokinase isozymes exist in humans: muscle, liver and platelet. Mutations in PFKM gene have been related with glycogen storage disease type VII, also identified as Tarui disease.

Fas and Fas Ligand (FasL) are members of the TNF superfamily and are type I and type II transmembrane proteins, respectively. Binding of FasL to Fas initiates apoptosis in Fas-bearing cells. The apoptosis mechanism involves the recruitment of pro-caspase 8 through an adaptor molecule named FADD followed by processing of the pro-enzyme to active forms. These active caspases subsequently cleave a variety of cellular substrates leading to the eventual cell death. sFasR is able to inhibit FasL-induced apoptosis by acting as a decoy receptor whicht serves as a sink for FasL. The full length Fas Receptor is a 319 a.a type I transmembrane protein, which contains a 157 a.a extracellular domain, a 17 a.a transmembrane domain, and 145 a.a cytoplasmic domain. The mature human Fas ECD shares 55%, 58%, a.a sequence identity with the mouse, rat, Fas, respectively.

Human AIF1 protein shares 98% homology/identity with that of rat. AIF1 is expressed in macrophages and neutrophils. The expression of AIF1 transcripts is upregulated by IFN-g in rat macrophages. AIF1 is expressed selectively in human macrophage-like cell lines, and in a subset of CD68(+) macrophages in the interstitial and perivascular spaces of human heart allografts. In quiescent cultured human vascular smooth muscle cells synthesis of AIF1 is induced by IFN-g, IL1b, and conditioned medium of T-cells. Overexpression of AIF1 in human VSMCs results in enhanced growth of these cells. AIF1 is expressed during apoptosis rat mammary gland and ventral prostate tissues. Allograft Inflammatory Factor 1 is expressed by several tumor-associated activated macrophages and microglial cells in rat and human gliomas. There is an evident relationship of AIF1-expressing activated macrophages and microglial cells with tumor malignancy in humans.

The protein encoded by this gene is a cytokine that acts as a growth and differentiation factor for both B cells and eosinophils. This cytokine is a main regulator of eosinopoiesis, eosinophil maturation and activation. The elevated production of this cytokine is reported to be related to asthma or hypereosinophilic syndromes. The receptor of this cytokine is a heterodimer, whose beta subunit is shared with the receptors for interleukine 3 (IL3) and colony stimulating factor 2 (CSF2/GM-CSF). This gene, together with those for interleukin 4 (IL4), interleukin 13 (IL13), and CSF2, form a cytokine gene cluster on chromosome 5. This cytokine, IL4, and IL13 are found to be regulated coordinately by long-range regulatory elements spread over 120 kilobases on chromosome 5q31.

ACP1 is part of the phosphotyrosine protein. ACP1 functions as an acid phosphatase and a protein tyrosine phosphatase (PTPase) existing in all human tissues, including adipocytes. ACP1 enzyme hydrolyzes protein tyrosine phosphate to protein tyrosine and orthophosphate, and also orthophosphoric monoesters to alcohol and orthophosphate. ACP1 is present in adipocytes, thus playing a specific role in the regulation of adipose tissue. High levels of the ACP1 negatively regulate cell proliferation and growth of leiomyomas during dephosphorylation of the PDGF receptor. High significant differences in birth weight-placental weight relationships were observed among acid phosphatase locus 1 phenotypes.

AXIN1 is a cytoplasmic protein, which contains a regulation of G-protein signaling (RGS) domain and a dishevelled and axin (DIX) domain. Axin1 is has been characterized as a tumor suppressor. In addition, Axin1 has an essential role in the formation of the embryonic neural axis. It has also been reported that Axin is found in mitotic spindles and centrosomes. AXIN1 interacts with adenomatosis polyposis coli, catenin beta-1, glycogen synthase kinase 3 beta, protein phosphate 2, and itself. AXIN1 functions as a negative regulator of the WNT1 signaling pathway and is able to induce apoptosis. Axin can be identified in a mouse mutant strain, created by random integration of a transgene. Mutations in the AXIN1 gene are linked to hepatocellular carcinoma, hepatoblastomas, ovarian endometriod adenocarcinomas, and medullablastomas.

S100A4 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 belongs to the family of calcium binding proteins such as calmodulin and troponin C. S100A is composed of an alpha and beta chain whereas S100B is composed of two beta chains. S100 protein is also expressed in the antigen presenting cells such as the Langerhans cells in skin and interdigitating reticulum cells in the paracortex of lymph nodes. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. S100 proteins are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100A4 may function in motility, invasion, and tubulin polymerization. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21. Chromosomal rearrangements and altered expression of the S100A4 gene have been implicated in tumor metastasis.

CD2 which is also known as E-rosette receptor, T11 and lymphocytefunction antigen-2 (LFA-2) is expressed on T cells, thymocytes, and subset of natural killer cells. Human CD2 functions as the receptor for sheep erythrocytes, human CD58 (LFA-3), and CD15s (Sialyl Lewis X). p56lck, p59fyn, CD3eta and CD3epsilon are tyrosine-phosphorylated after CD2 stimulation. CD2 plays a role in T cell activation, T- or NK-cell-mediated cytolysis, apoptosis in activated peripheral T cells, and regulation of T cell anergy.

IL4I1 is a secreted L-amino acid oxidase protein that mainly catabolizes L-phenylalanine. IL4I1 eexpression is induced by the IL4 in B cells.IL4I1 is expressed in dendritic cells & macrophagesIL4I1 takes part in the immune system since it is expressed in tumor-associated macrophages and suppresses T-cell responses. IL4I1 plays a role in the binding of flavin adenine dinucleotide cofactor.

Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Long EGF is a recombinant analog of Human EGF developed as a replacement for use in therapeutic cell culture applications as a like-for-like supplement for Recombinant Human or native EGF. It includes the Human EGF amino acid sequence plus a 53 amino acid N-terminal extension peptide.

ATG5 is a member of the autophagy-related (ATG) genes family. Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents. ATG5 protein is essential for autophagy. It conjugates to ATG12 and associates with isolation membrane to form autophagosomes. In addition ATG5 takes a vital part in the apoptotic process and it is expressed relatively late in the apoptotic process, downstream of caspase activity.

Cyclin-dependent kinase 4 combines with the protein cyclin D to form a protein complex that promotes the passage of cells through the G1 checkpoint in the cell growth cycle. This cellular activity is regulated by the protein p16 produced by p16INK4a. Normally, p16 controls cell growth by inhibiting the activity of the CDK4–cyclin D complex and stopping cells at the G1 checkpoint.

Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.

NRG1 is one of 4 proteins in the neuregulin family which act on the EGFR family of receptors. NRG1 was initially identified as a 44kDa glycoprotein that interacts with the ERBB2 receptor tyrosine kinase to increase its phosphorylation on tyrosine residues. In various brain areas, NRG1 is expressed at synaptic regions and its processing can be regulated by neuronal activity. The HRG-beta3variant of NRG1, along with HRG-alpha, beta1 and beta2 variants, was identified in various normal tissues and cancer cell lines.