Search results

Ribosomes (the organelles that catalyze protein synthesis) consist of a small 40S subunit and a large 60S subunit. Jointly these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. RPS10 which is is located in the cytoplasm and a part of the S10E family of ribosomal proteins, is a ribosomal protein that is a component of the 40S subunit. Variable expression of this gene in colorectal cancers compared to adjacent normal tissues has been observed, although no correlation between the level of expression and the severity of the disease has been found.

Osteopontin is a glycoprotein that was primarilyfound in osteoblasts and takes part in bone remodeling, immune functions in fibroblasts, macrophages, & lymphocytes during inflammation and wound healing. SPP1 highlybinds to hydroxyapatite. SPP1 forms an integral part of the mineralized matrix. SPP1 is vital to cell-matrix interaction.
Secreted Phosphoprotein-1 protects against cardiac ischemia-reperfusion injury through late preconditioning. Expression of Ostepontin and CD44 in hepatocellular carcinoma is linked to advanced tumor stage &leads to prognosis information. SPP1 is the most over-expressed gene in intrahepatic cholangiocarcinoma. Secreted Phosphoprotein-1 overexpression is related with interstitial lung diseases.

Chemokine (C-C motif) ligand 2 (CCL2) is a small cytokine belonging to the CC chemokine family that is also known as monocyte chemotactic protein-1 (MCP-1). It is found at the site of tooth eruption and bone degradation. In the bone, CCL2 is expressed by mature osteoclasts and osteoblasts and is under the control of nuclear factor ?B (NF?B). CCL2 recruits immune cells, such as monocytes, to sites of tissue injury and infection. This chemokine is produced as a protein precursor containing signal peptide of 23 amino acids and a mature peptide of 76 amino acids. It is a monomeric polypeptide, with a molecular weightof approximately 13kDa. As with many other CC chemokines, CCL2 is located on chromosome 17 in humans. The cell surface receptors that bind CCL2 are CCR2 and CCR5.

MECP2 is the key modificator of eukaryotic genomes and has a crucial part in mammalian development.
Human proteins MECP2, MBD1, MBD2, MBD3, and MBD4 form a family of nuclear proteins linked by the existence in each of a methyl-CpG binding domain (MBD). Each one of these proteins, with the exception of MBD3, can bind specifically to methylated DNA. In addition, MECP2, MBD1 and MBD2 can inhibit transcription from methylated gene promoters. Unlike other MBD family members, MECP2 is X-linked and subject to X inactivation. MECP2 is expendable in stem cells, but is vital for embryonic development. MECP2 gene mutations are the cause of most cases of Rett syndrome, a progressive neurologic developmental disorder and one of the most common reasons of mental retardation in females.

lysozyme G-like 2 and LYGH (LYG2), is a member of the glycosyl hydrolase 23 family. Lysozyme takes part in human innate immunity by causing bacterial cell lysis. LYG2 contains a SLT domain, a protein domain present in bacterial lytic transglycosylase (SLT) and in eukaryotic lysozymes (GEWL). SLT domain catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyglucosamine (GlcNAc).

AHA1 is a cochaperone that stimulates hsp90 ATPase activity. AHSA1 binds the middle domain of Hsp90 (amino acid 272-627) and functions as an ATPase-activating protein that competes with p23 and other co-chaperones for Hsp90 binding.
AHA1 affects a step in the endoplasmic reticulum to golgi trafficking.

Endothelial sialomucin (Endomucin) interferes with the assembly of focal adhesion complexes and inhibits interaction between cells and the extracellular matrix. Endomucin is expressed in the heart, kidney and lung.

BMP2 belongs to the transforming growth factor-beta (TGFB) superfamily. Bone morphogenic protein induces bone formation. BMP2 is a candidate gene for the autosomal dominant disease of fibrodysplasia (myositis) ossificans progressiva.

Interleukin 11 Receptor Subunit Alpha (IL11RA) which belongs to the hematopoietic cytokine receptor family is a receptor for interleukin-11. Interleukin 11 is a stromal cell-derived cytokine which is a member of a family of pleiotropic and redundant cytokines that employ the gp130 transducing subunit in their high affinity receptors. This specific receptor is quite similar to ciliary neurotrophic factor, since both contain an extracellular region with a two-domain structure composed of an immunoglobulin-like domain and a cytokine receptor-like domain. The receptor systems for IL6, LIF, OSM, CNTF, IL11 and CT1 are able to utilize IL6ST for initiating signal transmission. The IL11/IL11RA/IL6ST complex is involved in the control of proliferation and/or differentiation of skeletogenic progenitor or additional mesenchymal cells.

Filamin binding LIM protein 1 (FBLIM1) plays a role as an anchoring site for cell-ECM adhesion proteins and filamin-containing actin filaments. FBLIM1 is involved in cell shape spreading and motility. FBLIM1 participates in the regulation of filamin-mediated cross-linking and stabilization of actin filaments. FBLIM1 promotes stimulation of integrins and regulates integrin-mediated cell-cell adhesion.

Prion protein (PRNP) is a ubiquitous membrane glycoprotein whose abnormal self-replicating, misfolded form is widely believed to cause several central nervous system disorders, together known as Transmissible Spongiform Encephalopathies (TSE). PRNP contains a highly unstable region of five tandem octapeptide repeat. Mutations in PRNP protein’s repeat region as well as elsewhere have been associated with Creutzfeldt-Jakob disease, fatal familial insomnia, Gerstmann-Straussler disease, Huntington disease-like 1, and kuru.

MAPK10 is part of the MAP kinase protein family. MAP Kinases perform as assimilation point for many biochemical pathways. The enzyme also takes part in wide range of cellular pathways: differentiation, proliferation, development and transcription regulation.

Macrophage Colony Stimulating Factor (M CSF) or colony stimulating factor 1, is a cytokine, that promoted differentiation in hematopoietic stem cells to macrophages. Another role of M CSF is to bind to its receptor (colony stimulating factor 1 receptor) and to take part in placenta growth and development.

YOD1 is a Hydrolase which removes conjugated ubiquitin from proteins and takes part in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. YOD1 is a highly conserved deubiquitinating enzyme belonging to the ovarian tumor (otubain) family, whose function has yet to be determined in mammalian cells. YOD1 is a component of a multiprotein complex with p97 as its nucleus, proposing a functional link to a pathway responsible for the dislocation of misfolded proteins from the endoplasmic reticulum. YOD1 variant xpression deprived of its deubiquitinating activity compels a halt on the dislocation reaction, as concluded by the stabilization of various dislocation substrates.

V-set and transmembrane domain containing 2 (VSTM2L) is a novel modulator of HN neuroprotective activity. VSTM2L colocalizes with HN in distinct brain areas as well as in primary cultured neurons, where it plays a part in the modulation of neuronal viability. When tested in HN neuroprotection bioassays, VSTM2L acts as a potent antagonist of HN neuroprotective activity. The VSTM2L protein is the first example of a secreted antagonist of HN and may have a role in the modulation of HN biological functions.

The secreted polypeptide noggin, encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may have a principal role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. Recently, several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) were identified; both SYM1 and SYNS1 have multiple joint fusion as their principal feature, and map to the same region (17q22) as NOG. All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.

Interleukin-6 Signal Transducer or IL6ST is a receptor, part of the family of class 1 cytokine receptor. IL6ST binds to IL-6 through membrane-anchored or soluble IL-6R starts a connection between another complex of IL6ST and IL-6 , thus forming a homo-dimer and a signal transduction occurs.

MMP-2 or gelatinase A, is secreted by fibroblasts, cardiomyocytes, and myofibroblasts. MMP-2 has a broad feild of substrates, that contain elastin, collagen, fibroblast growth factor, endothelin, MMP-9, plasminogen, MMP-13 and TGF-beta, pointing towards bread roles of MMP-2. MMP-2 activity boosts at day four post-MI and attains a maximum by day seven.

Interleukin-35 is a glycosylated, disulfide-linked, heterodimeric protein comprised of the p35 subunit of IL-12 (IL-12 alpha) and the beta subunit of IL-27 (EBI3). IL35 is expressed by regulatory T-cells (Tregs), macrophages and some trophoblast and dendritic cells. IL-35 is produced in response to inflammation and generally serves as an inflammation suppressor. Interleukin-35 curbs inflammation by applying multiple activities, including the stimulation of regulatory T-cells and the inhibition of Th17 cells.

Thrombospondin-4 (THBS4) is a member of the thrombospondin protein family. This family members are adhesive glycoproteins that mediate cell-to-cell and cell-to-matrix interactions. THBS4forms a pentamer and binds to heparin and calcium. Among them THBS4binds a variety of matrix proteins including Collagens I, II, III, V, Laminin‑1, Matrilin‑2 and Fibronectin. THBS4 is up‑regulated in the spinal cord following peripheral nerve injury where it contributes to presynaptic hypersensitivity and hyperalgesia and is also up‑regulated in muscle following denervation.

Cytokeratin 8 belongs to the type B (basic) subfamily of high molecular weight keratins and exists in combination with keratin 18. Cytokeratin 8 is primarily found in the non-squamous epithelia and is present in majority of adenocarcinomas and ductal carcinomas. It is absent in squamous cell carcinomas. Hepatocellular carcinomas are defined by the use of antibodies that recognize only cytokeratin polypeptides 8 and 18.

Mediator Complex Subunit 21 (MED21) belongs to the mediator complex subunit 21 family. MED21 interacts with the human RNA polymerase II holoenzyme and is participated in transcriptional regulation of RNA polymerase II transcribed genes. A pseudogene of MED21 can be found on chromosome 8. Alternative splicing results in multiple transcript variants.