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Neuregulin is a signaling protein for ErbB2/ErbB4 receptor heterodimers on the cardiac muscle cells, playing an important role in heart structure and function through inducing ErbB2/ErbB4 receptor phosphorylation and cardiomyocyte differentiation. Research on molecular level discovered that neuregulin recombinant could make disturbed myocardial cell structure into order and strengthen the connection between myocardial cells by intercalated discs re-organization. Pharmacodynamic experiments in animals showed that neuregulin (NRG1) recombinant can reduce the degree of damage on myocardial cells caused by ischemia, hypoxia and viral infection.

The Fas receptor (CD95) mediates apoptotic signaling by Fas-ligand expressed on the surface of other cells. The Fas-FasL interaction plays an important role in the immune system and lack of this system leads to autoimmunity, indicating that Fas-mediated apoptosis removes self-reactive lymphocytes. Fas signaling is also involved in immune surveillance to remove transformed cells and virus infected cells. Binding of FAS to oligimerized FasL on another cell activates apoptotic signaling through a cytoplasmic domain termed the death domain that interacts with signaling adaptors including FAF, FADD and DAX to activate the caspase proteolytic cascade. Caspase-8 and caspase-10 are first activated, to then cleave and activate downstream caspases, and a variety of cellular substrates that lead to cell death. Caspases cleave nuclear lamins, causing the nucleus to break down and lose its normal structure and another caspase substrate is DFF, inducing cleavage and degradation of the genome. Other caspase substrates are involved in cytoskeletal structure, cell cycle regulation and signaling pathways. Activation of JNK kinase, activation of Jun, and production of ceramide may also play roles in Fas-mediated apoptosis. Activation of fas-mediated apoptosis is opposed by I-FLICE and FAP. Viruses and tumors may escape immune surveillance in part through suppression of fas-mediated apoptosis using similar mechanisms.

PRDX1 is part of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. PRDX1 is an important protector of red blood cells against reactive oxygen species and in tumor prevention.
PRDX1 is antioxidant protective in cells, and contributes to the antiviral activity of CD8(+) T-cells. PRDX1 has a proliferative effect and is involved in cancer development or progression.
Peroxiredoxin-1 is plays a role in redox regulation of the cell. Peroxiredoxin decreases peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. Peroxiredoxin is involved in eliminating peroxides generated during metabolism. Peroxiredoxin participates in the signaling cascades of growth factors and TNF-alpha by regulating the intracellular concentrations of h(2)o(2).

GOT1 is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, which participate in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and show close homology.

C-type lectin domain family 7 member A 1 or CLEC7A is a protein, that in the innate immune system, acts against fungal pathogens. CLEC7A can be found in the immune system response cells such as monocytes, macrophages & neutrophils, or in dendritic and T cells. The protein is enhanced by macrophages by using GM-CSF, IL-4, or IL-13, or diminishes by dexamethasone, IL-10 and LPS.

TARC cDNA encodes a 94 amino acid precursor protein with a 23 amino acid residue signal peptide that is cleaved off to generate the 71 amino acid residue mature secreted protein. Along with CC chemokine family members, CCL-17 has approximately 24-29% amino acid sequence identity with RANTES, MIP-1a, MIP-1b, MCP-1, MCP-2, MCP-3 and I-309. TARC is expressed in thymus, and at a lower level in the lung, colon, and small intestine. TARC is in addition transiently expressed in stimulated peripheral blood mononuclear cells. Recombinant TARC has been shown to be chemotactic for T cell lines but not monocytes or neutrophils. CCL-17 is a specific functional ligand for CCR4, a receptor that is selectively expressed on T cells. CCL17 is one of a few Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. CCL17 shows chemotactic activity for T lymphocytes, but not monocytes or granulocytes. CCL17 binds to chemokine receptors CCR4 and CCR8. This chemokine plays important roles in T cell development in thymus as well as in trafficking and activation of mature T cells.

Cytohesin 3 (CYTH3) belongs to the PSCD family, whose members have identical structural organization which consists of an N-terminal coiled-coil motif, a central Sec7 domain, and a C-terminal pleckstrin homology (PH) domain, and seem to mediate the regulation of protein sorting and membrane trafficking. CYTH3 is involved in the regulation of Golgi structure and function, and it might have a physiological role in regulating ADP-ribosylation factor protein 6 (ARF) functions, in addition to acting on ARF1.

Crk-like protein (CRKL) is a protein kinase containing SH2 and SH3 (src homology) domains which activates the RAS and JUN kinase signaling pathways and transforms fibroblasts in a RAS-dependent manner. CRKL is a substitute of the BCR-ABL tyrosine kinase, it also has a role in fibroblast transformation by BCR-ABL, and has oncogenic potential.

Endophilin-B1 (SH3GLB1) is a part of the endophilin family and highly expresses in heart, skeletal muscle, kidney and placenta. Endophilin B1 belongs to the B subgroup of the endophilin family which is needed for preservation of mitochondrial morphology and for the regulation of the outer mitochondrial membrane dynamics. SH3GLB1 is required for normal outer mitochondrial membrane dynamics. Furthermore, SH3GLB1 is required for coatomer-mediated retrograde transport in certain cells. SH3GLB1 interacts with SH3GLB2 and Bcl-2-associated X protein and involved in regulating apoptotic signaling pathways.

Chemokine (C-X-C motif) ligand 11 (CXCL11) is a small cytokine belonging to the CXC chemokinen family. I-TAC is highly expressed in peripheral blood leukocytes, pancreas and liver, with moderate levels in thymus, spleen and lung and low expression levels were in small intestine, placenta and prostate. Gene expression of CXCL11 is strongly induced by IFN-g and IFN-b, and weakly induced by IFN-a. The I-TACchemokine elicits its effects on its target cells by interacting with the cell surface chemokine receptor CXCR3, with a higher affinity than do the other ligands for this receptor, CXCL9 and CXCL10. I-TAC is chemotactic for activated T cells.The CXCL11 gene is located on human chromosome 4 along with many other members of the CXC chemokine family.

Immunoglobulin Lambda-Like Polypeptide 1 (IGLL1) is one of the substitute light chain subunits and is a part of the immunoglobulin gene superfamily which does not undergo rearrangement. Two transcript variants encoding diverse isoforms have been found for IGLL1. Mutations in IGLL1 can bring about B cell deficiency and agammaglobulinemia, an autosomal recessive disease in which few or no gamma globulins or antibodies are made.

O-Sialoglycoprotein Endopeptidase, also known as OSGEP is a member of the KAE1 / TsaD family. OSGEP is essential for the formation of threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs which read codons beginning with adenine. OSGEP take a direct catalytic part in the above reaction, however other proteins of the complex are required to fulfill this activity.

OSTF1 is an intracellular protein produced by osteoclasts that induces bone resorption, via signaling cascade which results in the secretion of factors enhancing osteoclast formation and activity.

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.

PGK1 is an X-linked enzyme that has a major role in the glycolytic pathway. PGK1 is a glycolytic enzyme which catalyzes the conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate, generating an ATP molecule. PGK1 may also act as a cofactor for polymerase alpha. Defects in the PGK1 gene are usually associated with chronic hemolytic anemia, though it can be accompanied by either mental retardation or muscular disease (rhabdomyolysis). Overexpression of PGK1 and its signalling targets are possibly an expression-pathway in diffuse primary gastric carcinomas promoting peritoneal dissemination. It was shown that PGK1 is differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia.

CBR1 is one of numerous monomeric, NADPH-dependent oxidoreductases having ubiquistly specificity for carbonyl compounds. CBR1 is broadly distributed in human tissues. CBR1 metabolizes toxic environmental quinones and pharmacological relevant substrates. CBR1 converts prostaglandin E2 to prostaglandin F2-alpha.

GGCT is a member of the family of transferases, specifically the aminoacyltransferases. GGCT protein catalyzes the formation of 5-oxoproline from gamma-glutamyl dipeptides and takes an important part in glutathione homeostasis. GGCT induces release of cytochrome c from mitochondria with resultant induction of apoptosis.

Glucokinase also known as GLK is a member of the bacterial glucokinase family. GLK is not highly significant in E.coli since glucoseis already transported into the cell through the PTS system as glucose 6-phosphate.

TXNDC17 is a disulfide reductase that takes part in several redox reactions using the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. TXNDC17 has peroxidase activity and assists to eliminate cellular hydrogen peroxide.

Glutathione peroxidase 1 (GPX1) is a member of the glutathione peroxidase family, consisting of 8 identified glutathione peroxidases (Gpx1-8) in humans. Glutathione peroxidase serves in the detoxification of hydrogen peroxide, and is one of the most vital antioxidant enzymes in humans. The GPX1 is a component of the enzymatic antioxidant defense, preventing oxidative damage to DNA, proteins and lipids by detoxifying hydrogen and lipid peroxides which may contribute to prostate cancer development. GPX1 is one of only a small number of proteins known in higher vertebrates to contain selenocysteine, which occurs at the active site of glutathione peroxidase and is coded by the nonsense (stop) codon TGA. Furthermore, the GPX1 protein is characterized in a polyalanine sequence polymorphism in the N-terminal region, which includes 3 alleles with 5, 6 or 7 alanine (ALA) repeats in this sequence. The allele with 5 ALA repeats is significantly linked to breast cancer risk.

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.

Cullin1, is an essential component of multiple cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, that facilitate the ubiquitination of proteins which take part in cell cycle progression, signal transduction and transcription. In the SCF complex. Cullin1 assists in a rigid scaffold which organizes the SKP1-F-box protein and RBX1 subunits. Cullin1 contributes to catalysis by positioning of the substrate and the ubiquitin-conjugating enzyme.