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PSG5 belongs to the PSG family, which are a highly connected group of secreted glycoproteins, vastly expressed in fetal placental syncytiotrophoblast cells. PSGs are can be found in serum from the first 2-3 weeks of pregnancy and at higher levels as the pregnancy progresses, up to e point where they are the highest fetal protein found in maternal blood at term. PSG5’s role is inducing secretion of TH2-type cytokines from monocytes and modulating the maternal immune system throughout the pregnancy, thus defending the semi-allotypic fetus from rejection.

SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.

DIM1 dimethyladenosine transferase 1 homolog (DIMT1) is a member of the methyltransferase superfamily. The DIMT1 enzyme specifically dimethylates 2 adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle. DIMT1 is restricted to the nucleolus.

Complement C4c is a degradation product of C4b which is cleaved by C4b/C3b inactivator to yield C4d and C4c.
Complement C4c interacts with C1 and C2 to form C3 convertase of the classic activation pathway. Systemic lupus erythematosus (SLE) is often associated with congenital C4 deficiency. Reduced levels of components of the classic pathway (C1, C2, C4, C3) are common after such activation, e.g. in SLE, acute serum sickness and conditions associated with circulating immune complexes.

RRM2 catalyzes the formation of deoxyribonucleotides from ribonucleotides. Synthesis RRM2 is regulated in a cell-cycle dependent method. RRM2 supplies the precursors essential for DNA synthesis. RRM2 catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. RRM2 Inhibits Wnt signaling.

Histone deacetylase 8 (HDAC8) is a member of the class 1 of the histone deacetylase/acuc/apha family. HDAC8 is biologically involved in skull morphogenesis and metabolic control of the ERR-alpha/PGC1-alpha transcriptional complex. Histones play a key role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation modifies chromosome structure and affects transcription factor access to DNA.

Ectonucleoside Triphosphate Diphosphohydrolase 3, also known as ENTPD3, which owns a threefold preference for the hydrolysis of ATP over ADP is similar to E-type nucleotidases (NTPases). ENTPD3 is a protein coding gene which contains four apyrase-conserved areas which is characteristic of NTPases.

Syndecan-4 is a type I integral membrane heparan sulfate proteoglycan (HSPG), which was originally isolated from cloned rat microvascular endothelial cells as an antithrombin-binding molecule, and is now known to be a member of the syndecan family. Syndecan-4 binds to basic fibroblast growth factor (bFGF), midkine, and tissue factor pathway inhibitor via its heparan sulfate chains, and is thought to be involved in various biologic functions such as signaling of bFGF, anticoagulation, and focal adhesion formation. A previous study demonstrated that syndecan-4 is expressed in various tissues, and its level of expression in the kidney is stronger than those of other syndecan family members. Thus, syndecan-4 is thought to play certain roles in maintaining renal function. Moreover, it has been reported that proteoglycans, especially sulfated proteoglycans, are involved in organogenesis of the kidney.

Asparagine synthetase (ASNS) is a cytoplasmic enzyme that turns aspartate toasparagine and functions mostly in mammalian organs. ASNS is responsible for cell growthand its mRNA content is associated with changes in the cell cycle. ASNS may also play a role as a biomarker for ovarian cancer.

Activating transcription factor 4 (ATF4) is a member of a family of DNA-binding proteins which includes the AP-1 family of transcription factors, cAMP-response element binding proteins and CREB-like proteins. The ATF4 gene encodes a transcription factor which was initially identified as a widely expressed mammalian DNA binding protein that could bind a tax-responsive enhancer element in the LTR of HTLV-1.

SPARC protein, or secreted protein acidic and rich in cysteine, or osteonectin or basement-membrane protein 40 is a protein that is coded by the SPARC gene in humans. It is a glycoprotein located in bones, that binds to calcium. The osteonectin is secreted from osteoblasts cells when boas are formed, mineralized and promotes the formation and creation of mineral crystals. Asides from calcium, it has been shown that this protein can also bind to collagen.

GARS is an (alpha)2 dimer which is a member of the class II family of tRNA synthetases. GARS is a glycyl-tRNA synthetase, one of the aminoacyl-tRNA synthetases which charge tRNAs with their cognate amino acids. GARS catalyzes the attachment of glycine to tRNA(Gly). In addition, GARS is able to produce diadenosine tetraphosphate (Ap4A), which is a universal pleiotropic signaling molecule required for cell regulation pathways, by direct condensation of two ATPs. GARS has been demonstrated to be a target of autoantibodies in the human autoimmune diseases, polymyositis or dermatomyositis.

PRKAG1 is a regulatory subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer comprised of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is a vital energy-sensing enzyme which supervises cellular energy status. PRKAG1 is one of the gamma regulatory subunits of AMPK. Alternatively spliced transcript variants encoding dissimilar isoforms were found.

ATP-dependent Clp protease proteolytic subunit (CLPP) is a member of the peptidase family S14. CLPP cleaves peptides in a variety of proteins in a manner which requires ATP hydrolysis. CLPP being the catalytic core of the Clp proteolytic complex is commonly involved in many cellular processes via the regulation of intracellular protein quality. CLPP is responsible for a somewhat general and central housekeeping function rather than for the degradation of specific substrates.

Mannose-6-Phosphate Receptor (M6PR) belongs to the P-type lectin family. P-type lectins play a vital role in lysosome function through the specific transport of mannose-6-phosphate-containing acid hydrolases from the Golgi complex to lysosomes. The M6PR protein functions as a homodimer and needs divalent cations for ligand binding. Lysosomal enzymes carrying phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the ensuing receptor-ligand complex is transferred to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex.

MMP-1 (interstitial collagenase) can break down a wide range of substrates including types I, II, III, VII, VIII, and X collagens as well as L-Selectin, pro-TNF, IL-1?, IGFBP-3, IGFBP-5, casein, gelatin, ?1 antitrypsin, myelin basic protein, pro-MMP2 and pro-MMP9. A significant function of MMP-1 is the degradation of fibrillar collagens in extracellular matrix remodeling. MMP-1 is expressed in fibroblasts, keratinocytes, endothelial cells, monocytes and macrophages. MMP1 can be divided into a number of distinct domains: a prodomain which is cleaved on activation, a catalytic domain containing the zinc binding site and a short hinge region with a carboxyl terminal domain. MMP1 is part of a cluster of MMP genes which localize to chromosome 11q22.3.

NAA10 is a member of the acetyltransferase family. NAA10 interacts with NAA15, HIF-1 and with the ribosome. In its binding to HIF-1, NAA10 functions as a protein acetyltransferase by regulating its stability. In various cell lines, NAA10 is downregulated in response to hypoxia. NAA10 is expressed during the course of the development of the brain.

HPRT1 has a main part in the generation of purine nucleotides through the purine salvage pathway. HPRT1 primarily functions to salvage purines from degraded DNA to renewed purine synthesis. Therefore, it performs as a catalyst in the reaction between guanine and phosphoribosyl pyrophosphate to form GMP.

Histidine NADH Dehydrogenase Fe-S Protein 5 (NDUFS5) belongs to the NADH dehydrogenase (ubiquinone) iron-sulfur protein family. NDUFS5 is a subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which doesn’t take part in catalysis. Complex I is transferring the electrons from NADH to the respiratory chain.

ADP-ribosylation factor-like 14 (ARL14) is a developmentally regulated member of the ADP-ribosylation factor/ARF-like protein (ARF/ARL) family of Ras-related GTPases. ARL14 is GTPase which recruits MYO1E to MHC class II-containing vesicles via the effector protein C11orf46/ARF7EP and thus controls the movement of these vesicles along the actin cytoskeleton in dendritic cells. MHC-II transport was controlled by the GTPase ARL14/ARF7, which recruits the motor myosin 1E via an effector protein ARF7EP.

ARL15 is a member of the ARF family which are essential in eukaryotic vesicular trafficking pathways and have a vital part in the activation of phospholipase D. ARL15 variants influence levels of Acrp30, an adipocyte-derived protein that is extremely genetic and inversely related to the prospect of type 2 diabetes mellitus and coronary heart disease.

TIGAR is a p53-inducible enzyme which catalyzes the hydrolysis of fructose-2-6 bisphosphate (F-2-6-BP) to fructose-6-phosphate and inorganic phosphate. F-2-6-BP is an influential activator of 6-phosphofructose-1 kinase (the rate limiting enzyme of glycolysis). By lowering the intracellular level of F-2-6-BP, TIGAR expression leads to increased glucose processing through the pentose phosphate pathway, the main cellular source for NADPH.

D-lactate dehydrogenase (ldha) is a member of the D-isomer specific 2-hydroxyacid dehydrogenase family. In enzymology, an ldha (cytochrome) is an enzyme which catalyzes the chemical reaction. Therefore, the 2 substrates of the ldha enzyme are (D)-lactate and ferricytochrome c, whereas its 2 products are pyruvate and ferrocytochrome c.

cAMP-dependent protein kinase type II-alpha regulatory subunit (PRKAR2A) can be phosphorylated by the activated catalytic subunit. PRKAR2A interacts with numerous A-kinase anchoring proteins and regulates the subcellular localization of cAMP-dependent protein kinase.