Search results

PRDX2 is part of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. PRDX2 takes part as an antioxidant protective role in cells, and contributes to the antiviral activity of CD8(+) T-cells. PRDX2 has proliferative effect in cancer development or progression.
If PRDX2 protection is insufficient against peroxidases, the DNA damage results in neurological disease such as Alzheimer's or DNA damage leading to cancer.

Cyclophilin B (also known as PPIB, peptidylpropyl isomerase B) is a cyclosporine-binding protein and is mainly located within the endoplasmic reticulum. It is associated with the secretory pathway and released in biological fluids. This protein can bind to cells derived from T- and B-lymphocytes, and may regulate cyclosporine A-mediated immunosuppression.

Cyclophilin-C belongs to the peptidyl-prolyl cis-trans isomerase (PPIase)) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Like other PPIases, the Cyclophilin-C protein can bind immunosuppressant cyclosporin A.

MRPL28 is found in a variety of normal tissues such as spleen, testis, thymus, liver, kidney, brain, adrenal, lung and retinal tissue. 39S ribosomal protein L28, mitochondrial (MRPL28), is a part of the ribosomal protein L28P family. Mammalian mitochondrial ribosomal proteins encoded by nuclear genes and helps in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPL28 is an important therapeutic reagent for HLA-A24 (A24) patients since this antigen is distinguished by tumor-infiltrating lymphocyte (TIL) 1290, which targets the A24 serotype.

Aldo-keto reductase family 1 member C1 or AKR1C1 is an enzyme, part of the aldo/keto reductase family that holds over 40 familiar proteins. AKR1C1 promotes the conversion of ketones & aldehydes to their alcohol forms by using cofactors such as NADH & NADPH. AKR1C1 promotes the progesterone reduction to its inactive molecule form 20-alpha-hydroxy-progesterone.

AKR7A3, takes part in the detoxification of aldehydes and ketones. AKR7A3 reduces the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. AKR7A3 participates in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen.

Chemokine (C-C motif) ligand 1 (CCL1) is a small glycoprotein secreted by activated T cells that belongs to a family inflammatory cytokines known as chemokines. CCL1 attracts monocytes, NK cells, and immature B cells and dendritic cells by interacting with a cell surface chemokine receptor called CCR8. This chemokine resides in a large cluster of CC chemokines on human chromosome 17.

Indoleamine 2,3-Dioxygenase 1 (IDO1) catalyzes the primary and rate-limiting stage in tryptophan catabolism to N-formyl-kynurenine. IDO1 affects on various tryptophan substrates including D-tryptophan, and serotonin and is expressed in dendritic cells, monocytes, and macrophages. IDO1 takes part in a range of pathophysiological processes like neuropathology, antimicrobial and antitumor defense, immunoregulation, and antioxidant activity. IDO1 regulates T-cell behavior by its pericellular catabolization of the necessary amino acid tryptophan.

TP53-induced glycolysis and apoptosis regulator (TIGAR or C12ORF5), is a 270 amino acid protein induced by the p53 tumor suppressor pathway that functions to protect against oxidative stress. C12ORF5 specifically functions to block glycolysis, leading the pathway to the pentose phosphate shunt and decreasing the intracellular concentration of reactive oxygen species. Therefore, it is thought that C12ORF5 may act to modulate the apoptotic response to p53, thus allowing cells to survive mild or transient stresses.

The peroxisome proliferator activated receptors (PPARs) are ligandactivated transcription factors within the nuclear receptor superfamily, which play important roles in adipogenesis, glucose homeostasis andinflammation. Three different isotypes can be distinguished; alpha, beta and gamma. PPARg, is mainly expressed in adipose tissue and to lesser extent in colon, the immune system and the retina. Whereas PPARg operates in the catabolism of fatty acids in the liver, PPARg influences the storage of fatty acids in the adipose tissue and plays a role in adipocyte differentiation. PPARg binds to DNA as a heterodimer with retinoid X receptor (RXR), activating expression of target genes after binding ligand.

Lysosomal-Associated Membrane Protein 3, also known as LAMP3 is part of the lysosome-associated membrane protein family. LAMP3 and CD68 share an extremely similar predicted structure. LAMP3 performs in dendritic cell function and in adaptive immunity as well. Furthermore, LAMP3 overexpression is actively involved in tumor invasion via increased migration into lymph-vascular spaces.

CDC37, His protein is extremely parallel to Cdc 37, a cell division cycle control protein of Sacchromyces cerevisiae. CDC37 is a molecular chaperone with a detailed role in cell signal transduction. CDC37 forms a complex with Hsp90 and several protein kinases including CDK4, CDK6, SRC, RAF-1, MOK, and eIF2 alpha kinases CDC37 has a vital part in directing Hsp90 to its target kinases.

CDHR5, also referred to ascadherin-related family member 5, is a calcium-dependent cell adhesion protein. CDHR5 is located in coated pits, and is expressed during lung and kidney developmentat at the lateral and basal surfaces of epithelia.

Glycophorin C, also known as GYPC, is an integral membrane glycoprotein. GYPC is a minor species which is carried by human erythrocytes, however plays an important role in regulating the mechanical stability of red cells. Numeral glycophorin C mutations have been described. The Gerbich and Yus phenotypes are due to deletion of exon 3 & 2, respectively. The Webb & Duch antigens, also identified as glycophorin D, result from single point mutations of the glycophorin C gene. The glycophorin C protein has very slight homology with glycophorins A & B.

COPZ1 is a member of the adaptor complexes small subunit family. Coatomer is an oligomeric complex which contains as a minimum the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. The zeta subunit has a part in regulating the coat assembly and, therefore, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.

AASDHPPT is a member of the P-Pant transferase superfamily. AASDHPPT catalyzes the post-translational modification of target proteins by phosphopantetheine and can transfer the 4'-phosphopantetheine moiety from coenzyme A to a serine residue of a broad range of acceptors, such as the acyl carrier domain of FASN (in vitro). AASDHPPT is similar to Saccharomyces cerevisiae LYS5, which is required for the activation of the alpha-aminoadipate dehydrogenase in the biosynthetic pathway of lysine. AASDHPPT is found in the heart, skeletal muscle, placenta, testis, brain, pancreas, liver and kidney. It’s been suggested that defects in the human AASDHPPT gene result in pipecolic acidemia.

Cathepsin-E also known as CTSE is a gastric aspartyl protease which functions as a disulfide-linked homodimer. CTSE belongs to the peptidase C1 family; furthermore it has specificity similar to pepsin A and cathepsin D. CTSE is an intracellular proteinase which does not seem to be involved in the digestion of dietary protein and is found in the uppermost concentration in the surface of epithelial mucus-producing cells of the stomach. CTSE is the first aspartic proteinaseexpressed in the fetal stomach and is discovered in more than half of gastric cancers. For that reason CTSE is anoncofetal antigen. In addition, transcript variants utilizing alternative polyadenylation signals and two transcript variantsencoding different isoforms exist for this gene.

PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Cyclophilin-A is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. Cyclophilin-A can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported.

Cyclophilin-D is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and speeds up the protein folding. Cyclophilin-D possess PPIase activity and binds to the immunosuppressant cyclosporin-A. Cyclophilin-D is very well known that its overexpression suppresses the apoptosis in cancer cell. Cyclophilin-D suppresses apoptotic cell death by the use of mitochondrial hexokinase-2 dependent mechanism in cancer cells.

MRPS25, a 28S subunit protein, is a member of the ribosomal protein S5P family. An equivalent pseudogene is located on chromosome 4.

NDUFS4 is a subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), the primary multi-subunit enzyme complex of the mitochondrial respiratory chain. Complex I is involved in cellular ATP production, the main source of energy for numerous vital processes in living cells. NDUFS4 removes electrons from NADH and passes them by a series of diverse protein-coupled redox centers to the electron acceptor ubiquinone. NDUFS4 presents a hotspot of mutations in the genetic apparatus of oxidative phosphorylation and the correct assembly of the subunit it encodes is essential for completion of the assembly of complex I.

Dynein light chain roadblock-type 2 (DYNLRB2) functions as one of several non-catalytic accessory components of the cytoplasmic dynein complex which are considered to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein functions as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules.

Human Cu/Zn Superoxide Dismutase (SOD1) catalyzes the reaction between superoxide anions and hydrogen to yield molecular oxygen and hydrogen peroxide. The enzyme protects the cell against dangerous levels of superoxide. SOD1 binds copper and zinc ions and is 1 of 3 isozymes accountable for destroying free superoxide radicals in the body. The encoded protein neutralizes supercharged oxygen molecules, which can damage cells if their levels are not controlled. Mutations in SOD1 cause a form of familial amyotrophic lateral sclerosis.

SOD2 is part of the iron/manganese superoxide dismutase family. It encodes a mitochondrial protein that forms a homotetramer and binds one manganese ion per subunit. SOD2 binds to the superoxide byproducts of oxidative phosphorylation and converts them to hydrogen peroxide and diatomic oxygen. Mutations in SOD2 gene have been associated with idiopathic cardiomyopathy (IDC), premature aging, sporadic motor neuron disease, and cancer. SOD2 destroys radicals which are usually produced within the cells and which are toxic to biological systems.