Search results

Osteoprotegerin, which is a member of the tumor necrosis factor receptor superfamily and is involved in the regulation of bone metabolism. OPGand its ligand (OPGL) are cytokines regulating osteoclasto-genesis. OPGL binds to receptors on the surface of preosteoclasts and stimulates their differentiation into active osteoclasts. This leads to osteoresorption. OPG inhibits this osteoclasto-genesis (OPG is secreted by osteoblasts, and binds to OPGL, thus inhibiting maturation of osteoclasts and osteoresorption). The degree and activity of osteoresorption depend mainly on the balance between OPG and its ligand (OPGL); factors increasing OPGL expression mostly reduce OPG expression and vice versa.

IFN Regulatory Factor-5, also known as IRF5 belongs to the IFN regulatory factor (IRF) family, a group of transcription factors with various functions, including virus-mediated activation of IFN, and modulation of cell growth, differentiation, apoptosis, and immune system activity. Members of the IRF family are characterized by a conserved N-terminal DNA-binding domain containing tryptophan (W) repeats. Multiple transcript variants encoding different isoforms have been found for this gene. In addition, IRF5 is implicated in the induction of IFNs IFNA and INFB and inflammatory cytokines upon virus infection. IRF5 is activated by TLR7 or TLR8 signaling.

Recombinant Galectin-13 is an E. coli expressed peptide, this protein is one of human placenta specific galectins, like all galectin family, it contains a carbohydrate recognition domain (CRD) as well. Increased blood concentration was found highly asscoaited with preeclampsia and HELLP syndrome in pregnant women. The molecular weight of galectin-13 is 16kDa.

Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.

IFN-alpha is produced by macrophages and has antiviral activities. IFN stimulates the production of two enzymes: protein kinase and an oligoadenylate synthetase.

sRANK Receptor is a part of of the TNF superfamily of ligands and receptors which participates in the regulation of specific immunity and bone turnover. sRANK Receptor was originally acknowledged as a dendritic-cell-membrane protein, which by interacting with RANKL augments the capacity of dendritic cells to stimulate naive T cell proliferation and to endorse the survival of RANK and T cells. The full length human RANK cDNA encodes a type I transmembrane protein of 616 amino acids with a predicted 183 amino acid extracellular domain and a 383 amino acid cytoplasmic domain. sRANK Receptor is also expressed in a various tissues including skeletal muscle, thymus, liver, colon, small intestine and adrenal gland.

AMTN is a member of the amelotin family. AMTN is a lately discovered secreted enamel protein. AMTN mainly expressed during the maturation stage of enamel formation. AMTN gathers in a basal lamina-like structure at the interface between ameloblasts and enamel mineral and it co-localizes with one more lately described enamel protein, odontogenic ameloblast- related protein (ODAM(.

NAPA is part of the SNAP (Soluble NSF Attachment Protein) family. SNAPs, acting together with SNAREs (SNAP receptors) and the N-ethylmaleimide-sensitive fusion protein (NSF), are necessary for the fusion of transport vesicles to their objective membranes in synaptic transmission, intra-Golgi transport, endosome-to-endosome fusion and transcytotic vesicles-to-plasma membrane transport. NAPA is in charge of the binding of NSF and therefore the formation of a 20S fusion particle.

BAK1 is a member of the BCL2 protein family. The BCL2 family members form oligomers or heterodimers and act as anti- or pro-apoptotic regulators which are involved in a wide variety of cellular activities. The BAK1 gene encodes a receptor-like kinase (RLK) with a putative extracellular domain, a single transmembrane domain, an intracellular-juxtamembrane domain, and a kinase domain. BAK1 localizes to mitochondria, and functions to induce apoptosis. BAK1 interacts with and accelerates the opening of the mitochondrial voltage-dependent anion channel, leading to a loss in membrane potential and the release of cytochrome c. Furthermore, BAK1 interacts with the tumor suppressor P53 after exposure to cell stress. BAK1 expression is linked to the progression of Prostate cancer.

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.

Clusterin also named Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices.
Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates.
Clusterin is up- or down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.

LRG1 belongs to the leucine-rich repeat (LRR) family of proteins, which have been shown to be involved in protein-protein interaction, signal transduction, and cell adhesion and development. The LRG1 is expressed during granulocyte differentiation.

Heparanase is an endo β-D-glucuronidase, which degrades heparan sulfate side chains of heparan sulfate proteoglycans (HSPGs) in the extracellular matrix. Heparanase plays an important role in ECM degradation, facilitating the migration and extravasation of tumor cells and inflammatory leukocytes (1,2,3). Upon degradation, heparanase releases growth factors and cytokines that stimulate cell proliferation and chemotaxis (4,5). Heparanase is a heterodimer comprised of a 50 kDa subunit harboring the active site and a 8 kDa subunit. It is produced as a latent 65 kDa precursor and proteolytically processed to its active form (1,6). Heparanase is highly expressed in myeloid leukocytes (i.e. neutrophils) in platelets and in human placenta. Human heparanase was found to be upregulated in various types of primary tumors, correlating in some cases with increased tumor invasiveness and vascularity and with poor prospective survival (7,8).

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.

The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.

H1N1 is a sub specie of the virus Influenza A. H1N1 Influenza Virus has evolved into many strains for example: the Spanish Flustrain, mild humanflu strains, endemic pigstrains & different strains found in birds.
The Virusis is a globular particle is sheathed in a lipid bilayer derived from the plasma membrane of its host and is about 100nm in diameter. In the lipid bilayer are two integral membrane antigens some 500 proteins of hemagglutinin ("H") and some 100 proteins of neuraminidase ("N").

Interleukin-21 isoform 1 or IL21, categorized as a T helper cytokine. IL21 is part of the regulation of immune responses, haematopoiesis and cell-mediated responses. IL21 takes a main part in haematopoiesis and immune responses regulation, therefore can affect lymphocyte development. Activation of T cells leads to production of the IL21 which has an important role in the viral infections persistence.

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.

Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. IL8 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.

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.

Il-6 is a cytokine with a wide variety of biological functions: it plays an essential role in the final differentiation of b-cells into ig-secreting cells, it induces myeloma and plasmacytoma growth, it induces nerve cells differentiation, in hepatocytes it induces acute phase reactants.

IL1B or Interleukin-1b is made and produced by activated macrophages, IL-1B stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1B proteins take part in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin from synovial cells.

IL-31 produced by activated Th2-type T cells, cooperates with a heterodimeric receptor consisting of IL-31 Receptor Anatagonist and Onconstatin-M Receptor that is continuesly expressed on epithelial cells and keratinocytes. IL-31 plays a role in the promotion of allergic skin disorders and in regulating other allergic diseases, such as asthma. IL-31 is involved in the itching sensation and endorses the scratching behavior in NC/Nga mice with atopic dermatitis. IL-31 expression is connectd with CLA(+) T cells and contributes to the development of atopic dermatitis-induced skin inflammation and pruritus. IL-31 is a powerful inducer of proinflammatory mediators in human colonic SEMFs. IL-31 takes part as a proinflammatory cytokine derived from Th2 cells.
Serum IL-31 level is higher in patients with atopic dermatitis. IL-31 is involved in a broad range of immune- & non-immune cells & possesses potential pleiotropic physiological functions, including regulating hematopoiesis & immune response, causing inflammatory bowel disease, airway hypersensitivity & dermatitis.