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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. By injecting soluble RANKL, novel osteopenia model mice were established in only 50 hours. Degree of bone loss can be controlled by changing doses of sRANKL. RANKL can be used in establishing osteopenia model for in vivo screening of drugs for osteoporosis, determination of effect and mechanism, evaluation of bone anabolic drugs.

Leukocyte Cell-Derived Chemotaxin 2 (LECT2) functions as a chemotactic factor to neutrophils. LECT2 stimulates the proliferation of chondrocytes and osteoblasts. LECT2 is strongly expressed in the liver and weakly in the testis. LECT2 is a secreted, 16kDa protein which serves as a chemotactic factor to neutrophils and stimulates the growth of chondrocytes and osteoblasts. LECT2 protein has a high sequence similarity to the chondromodulin repeat regions of the chicken myb-induced myeloid 1 protein. A polymorphism in the LECT2 gene is linked with rheumatoid arthritis.

CMV is part of the Betaherpesvirinae subfamily of Herpesviridae; including herpes simplex virustypes 1 and 2, varicella-zoster virus, and Epstein-Barrvirus. The herpesviruses has the common ability to stay latentover long periods of time. CMV has the largest genome of the herpes viruses, ranging from 230-240 kilobase pairs. CMV is a double-stranded linear DNA virus with 162 hexagonal protein capsomeres surrounded by a lipid membrane. Human CMV is composed of unique and inverted repeats that include the existence of 4 genome isomers caused by inversion of L-S genome components (class E). Replication may be divided into immediate early, delayed early, and late gene expression based on time of synthesis after infection. The DNA is replicated by rolling circles. In vitro, CMV replicates in human fibroblasts.

CCL28 is part of the subfamily of small cytokine CC genes. CCL28 shows chemotactic activity for resting CD4 or CD8 T cells and eosinophils. CCL28 binds to chemokine receptors CCR3 and CCR10. CCL28 is involved in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs. CCL28 mediates mucosal immunity in HIV exposure and infection. CCL28 is involved in the pathogenesis of inflammatory skin diseases.
Human CCL28 cDNA encodes a 127 amino acid residue precursor protein with a putative 22 amino acid residue signal peptide that is cleaved to produce the 105 amino acid residue mature protein. Human and mouse CCL28 are highly conserved, sharing 83% amino acid identity in their mature regions. CCL28 shares the most homology with CCL27/CTACK. Human and mouse CCL28 RNA expression was found to be highest in normal and pathologic colon with the protein being expressed by epithelial cells. Human CCL28 RNA was also present in normal and asthmatic lung tissues.

GSTP1 is a polymorphic gene encoding active, functionally different GSTP1 variant proteins that are believed to function in xenobiotic metabolism and have a part in susceptibility to cancer, and other diseases. GSTP1 is a glutathione S-transferase belonging to the pi class. GST family enzymes play a significant role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. Based upon the biochemical, immunologic and structural properties of the soluble GSTs they are grouped into 4 main classes: alpha, mu, pi, and theta. The GSTP1 enzyme acts by catalyzing the reaction of glutathione with an acceptor molecule to form a Sulfur-substituted glutathione. The reactions employing glutathione contribute the transformation of a broad range of electrophiles, including reactive products of lipid, protein, carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress.
The GSTP1 inactivation through CpG hypermethylation is frequent in pituitary adenomas and may be a factor in aggressive pituitary tumor behavior. GSTP1 is may be a transcriptional target of the p53 tumor suppressor gene. Single-nucleotide polymorphism in GSTP1 is linked to modified protein binding, which influence GSTP1's contribution to carcinogen and drug metabolism, and possibly disease pathogenesis and/or drug response. GST-pi might have central roles in proliferation of androgen-independent human prostate cancer cells.

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.

CCNH is part of the cyclin family that is known for its protein abundance through the cell cycle. Cyclins act as regulators of CDK kinases. CCNH forms a complex with CDK7 kinase and ring finger protein MAT1. The kinase complex is able to phosphorylate CDK2 and CDC2 kinases, therefore it functions as a CDK-activating kinase (CAK). CCNH and its kinase collaborator are components of TFIIH, as well as RNA polymerase II protein complexes.

The MCFD2-LMAN1 complex forms an explicit cargo receptor for the ER-to-Golgi transport of selected proteins. MCFD2 is involved in the secretion of coagulation factors. MCFD2 is expressed by neural stem/progenitor cells of the hippocampus, and localized to region where neurogenesis persists throughout life. MCFD2 prevents NSC cell death and maintains stem cell characteristics. MCFD2 forms a complex with LAMN1 that facilitates the transport of coagulation factors V and VIII from the endoplasmic reticulum to the Golgi apparatus through an endoplasmic reticulum Golgi intermediate compartment. Mutations in the MCFD2 cause Factor V and Factor VIII combined deficiency.

Profilin1 (PFN1) is a ubiquitous actin monomer-binding protein which is a member of the profilin family. PFN1 significantly boosts skin wound healing in-vitro and in-vivo which may be mediated by purinergic receptors. PFN1 is also active in endothelial cell migration and vessel sprouting. PFN1 is thought to control actin polymerization in response to extracellular signals. PFN1 binds to actin and affects the formation of the cytoskeleton. In addition, PFN1 has an important role in the regulation of epithelial cell-cell adhesion. At high concentrations, profilin averts the polymerization of actin, while at low concentrations it enhances the polymerization. PFN1 gene deletion is linked to Miller-Dieker syndrome.

PPIF is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIF accelerates the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIF is key component of the mitochondrial permeability transition pore in the inner mitochondrial membrane. Activation of this pore is thought to be involved in the induction of apoptotic and necrotic cell death.

Mammalian crystallins which are water soluble structural proteins located in the vertebrate eye are classified in three forms, labeled alpha, beta and gamma. Crystallins, the primary components of the lens, raise the refractive index of the eye all through the accommodation by creating high-molecular weight aggregates that maintain transparency. CRYGS is a monomer that does not aggregate. CRYGS encodes the most substantial gamma-crystallin in adult eye lens tissue. Gamma-crystallins has a part in cataract formation due to aging or mutations in specific genes,

Cytokeratin 8 (KRT8) belongs to the type II keratin family clustered on the long arm of chromosome 12. Type I and type II keratins heteropolymerize to form intermediate-sized filaments in the cytoplasm of epithelial cells. KRT8 typically dimerizes with keratin 18 to form an intermediate filament in simple single-layered epithelial cells. KRT8 has a role in retaining cellular structural integrity and also functions in signal transduction and cellular differentiation. KRT8 gene mutations cause cryptogenic cirrhosis.

Chemokine (C-X-C motif) ligand 2 (CXCL2) is a small cytokine belonging to the CXC chemokine family that is also called macrophage inflammatory protein 2-alpha (MIP2-alpha), Growth-regulated protein beta (Gro-beta) and Gro oncogene-2 (Gro-2). CXCL2 is 90% identical in amino acid sequence as a related chemokine, CXCL1. This chemokine is secreted by monocytes and macrophages and is chemotactic for polymorphonuclear leukocytes and hematopoietic stem cells. The gene for CXCL2 is located on human chromosome 4 in a cluster of other CXC chemokines. CXCL2 mobilizes cells by interacting with a cell surface chemokine receptor called CXCR2.

The human cytomegalovirus UL99-encoded pp28 is a myristylated phosphoprotein that is a constituent of the virion. The pp28 protein is positioned within the tegument of the virus particle, a protein structure that resides between the capsid and envelope. In the infected cell, pp28 is found in a cytoplasmic compartment derived from the Golgi apparatus, where the virus buds into vesicles to acquire its final membrane.

CD30 Ligand (TNFSF8) is a cytokine which is a member of the tumor necrosis factor (TNF) ligand family. The TNFSF8 cytokine is a ligand for TNFRSF8/CD30, which is a cell surface antigen and a marker for Hodgkin lymphoma and related hematologic malignancies. The employment of the TNFSF8 cytokine expressed on B cell surface has an inhibitory role in modulating Ig class switch. TNFSF8 enhances cell proliferation of some lymphoma cell lines, while inducing cell death and reducing cell proliferation of other lymphoma cell lines. The pleiotropic biological activities of the TNFSF8 cytokine on different CD30+ lymphoma cell lines has a pathophysiologic role in Hodgkin's and some non-Hodgkin's lymphomas.

CD32a, also known as FCGR2A, belongs to a family of immunoglobulin Fc receptor genes located on the surface of various immune response cells. FCGR2A which is a cell surface receptor found on phagocytic cells like macrophages and neutrophils, takes part in the process of phagocytosis and clearing of immune complexes. FCGR2A initiates cellular responses against pathogens and soluble antigens by binding to IgG. FCGR2A, which is a low affinity receptor, binds to the Fc region of immunoglobulins gamma.

ITGB4 (integrin beta-4 isoform 1) belongs to the Integrin beta family. ITGB4 forms noncovalent heterodimers with Integrin alpha 6 and takes part in the formation of epithelial hemidesmosomes. ITGB4 has a vital structural role in the hemidesmosome of epithelial cells and is needed for the regulation of keratinocyte motility & polarity. ITGB4 leans towards the association with alpha 6 subunit and is expected to take a key role in the biology of invasive carcinoma.

BTB/POZ domain-containing protein KCTD5 (KCTD5), is a 234 amino acid protein which localizes mainly in the cytoplasm however translocates to the nucleus on interaction with REP proteins. The expression of KCTD5 is up regulated post-transcriptionally in peripheral blood lymphocytes stimulated via the T-cell receptor. KCTD5 interacts particularly with cullin3, attaches ubiquitinated proteins, and created oligomers through its BTB domain.

Fibroblast Growth Factors (FGFs) comprise a family of at least 18 structurally related proteins that take part in a multitude of physiological and pathological cellular processes, includingdifferentiation, cell growth, angiogenesis, wound healing and tumorgenesis. The biological activities of the FGFs are mediated by a family if type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. 4 different genes encoding related FGF receptors. Multiple forms of FGFR-1 to -3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII. Only the alpha isoform has been identified for FGFR-3 and FGFR-4. Additional splicing events for FGFR-1 to -3, involving the C-terminal half of the IgIII domain encoded by 2 mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). A IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGFR-1.

GDF15 is part of the TGF-Beta superfamily that is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.

Ara h 2 comprises of 2 isoforms: Ara h 2.0101 and Ara h 2.0201. Ara h 2.0201 is the most important peanut allergen which binds IgE. Ara h 2.0201 is a Weak inhibitor of trypsin and is a conglutin storage protein which accounts together with Ara h 6.0101 for the majority of the IgE immune response.

Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.

HSPA9 is part of the heat shock protein 70 family which contains both heat-inducible and constitutively expressed members that are also called heat-shock cognate proteins. HSPA9 encodes a heat-shock cognate protein that is involved in the control of cell proliferation and acts as a chaperone. HSPA9 was restricted to chromosome 5, band q31, a region that is often deleted in myeloid leukemias and myelodysplasia (MDS), making it a candidate tumor suppressor gene, which is consistent with the biological function of its murine homologue. HSPA9 supresses nuclear translocation, transcriptional activation, and control of centrosome-duplication functions of p53.