Search results

Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin binds directly to activin and functions as an activin antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).

GSTO1 belongs to the theta class glutathione S-transferase-like (GSTTL) protein family. GSTO1 is expressed in a broad array of human tissues and exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities as well as catalyzing the reduction of monomethylarsonate which is an intermediate in the pathway of arsenic biotransformation. Furthermore, GSTO1 shields from oxidative stress which is a risk factor for Alzheimer disease, vascular dementia and stroke. GSTO1 is abundant in alveolar macrophages and airway secretions, with the levels reduced in chronic obstructive pulmonary disease patients. In mouse, the GSTO1 protein acts as a small stress response protein, probably involved in cellular redox homeostasis.

Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin functions as an ACTV antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).

Dickkopf-related protein 3 (DKK3) belongs to the DKK protein family including Dkk-1, 2, 3 and -4. DKK3 is a 350 amino acid secreted glycoprotein which is comprised of an N-terminal signal peptide and 2 conserved cysteine-rich domains that are separated by a 12 amino acid linker region. DKK3 is involved in embryonic development through its inhibition of the WNT signaling pathway. DKK3 gene expression is decreased in a variety of cancer cell lines and it may act as a tumor suppressor gene.

Small Ubiquitin-like Modifiers (SUMOs) are a family of small, related proteins that can be enzymatically attached to a target protein by a post-translational modification process termed sumoylation. Unlike ubiquitination, which targets proteins for degradation, sumoylation participates in a number of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability. All SUMO proteins share the conserved ubiquitin domain and the C-terminal diglycine cleavage/attachment site. Human SUMO2, also known as Sentrin2 and SMT3B is synthesized as a 95 amino acid (aa), 11 kDa propeptide that contains a two aa C-terminal prosegment, and an 18 aa N-terminal protein interacting region (aa 33 -50). Following prosegment cleavage, the C-terminal glycine is enzymatically attached to a lysine on a target protein. Human SUMO2 shares 100% sequence identity to SUMO-2 from mouse. SUMO2 also has very high sequence homology to SUMO3 and SUMO4, 86 % and 85%, respectively. SUMO2 shares only 44% sequence identity to SUMO1.

Pyroglutamyl-Peptidase I (PGPEP1) is an omega peptidase which detaches pyroglutamyl residues from the amino termini of peptides and proteins. PGPEP1 is a cytosolic cysteine peptidase which is expressed in most cell types. PGPEP1 enzyme has need of s a thiol-reducing agent for activity. PGPEP1 is possibly involved in the inactivation of biologically active peptides which have an amino terminal pyroglutamyl group, for instance peptides as neurotensin, luteinizing hormone releasing hormone, and thyrotropinreleasing hormone.

GALE is an enzyme that participates as the third enzyme in the Leloir pathway of galactose metabolism. GALE is a homodimeric epimerase localized in bacterial, plant, and mammalian cells. GALE inhances the reverse chemical reaction, the conversion of UDP-glucose to UDP-galactose. UDP-galactose builds galactose-containing proteins and fats, which have a crucial part in chemical signaling, building cellular structures, transporting molecules, and producing energy.

GCSAM is a protein which functions in signal transduction pathways and whose expression raises in germinal cell lymphomas. GCSAM contains a putative PDZ-interacting domain, an immunoreceptor tyrosine-based activation motif (ITAM), and two putative SH2 binding sites. In B cells, GCSAM expression is particularly induced by interleukin-4.

PRKAB2 is a regulatory subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer contains an alpha catalytic subunit and non-catalytic beta and gamma subunits. AMPK is a significant energy-sensing enzyme that supervises cellular energy status. AMPK is activated as a reply to cellular metabolic stresses, therefore phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), vital enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. PRKAB2 is a positive regulator of AMPK activity and highly expressed in skeletal muscle.

CDKN2C is a member of the CDKN2 cyclin-dependent kinase inhibitor family. CDKN2C cooperates with CDK4 or CDK6, and inhibits the activation of the CDK kinases, therefore acts as a cell growth regulator which regulates cell cycle G1 progression. CDKN2C suppresses the cell growth and proliferation with a correlated dependency on endogenous retinoblastoma protein RB. Studies in the knockout mice show CDKN2C takes part in regulating spermatogenesis, in addition to suppressing tumorigenesis.

Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation.

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.

Creatine Kinase BB is a cytoplasmic enzyme involved in energy homeostasis. The encoded protein reversibly catalyzes the transfer of phosphate between ATP and various phosphogens such as creatine phosphate. It acts as a homodimer in brain as well as in other tissues, and as a heterodimer with a similar muscle isozyme in heart. The encoded protein is a member of the ATP:guanido phosphotransferase protein family. A pseudogene of this gene has been characterized.

GRHPR located in the cytosol, belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family of proteins. GRHPR is widely expressed in liver. GRHPR has widespread tissue expression and is involved in metabolism. GRHPR is an enzyme with hydroxypyruvate reductase, glyoxylate reductase, and D-glycerate dehydrogenase enzymatic activities.

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.

Gltathione S-transferase PI 2, also known as GSTP2 is multifunctional enzyme which is involved in the protection of cellular components against anti-cancer drugs or peroxidative stress. Furthermore, down regulation of GSTP2 induces an increase of oxidative damage in the pyramidal cells of the CA1&CA3 regions as well as in the granular layer of the dentate gyrus, which at the end leads to structural and functional damage.

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.

Dickkopf-related protein 2 (DKK2) is a member of the dickkopf family, which has a vital role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In adults, Dkks are involved in bone formation and bone disease, cancer and Alzheimer disease. DKK2 contains 2 cysteine rich regions and is implicated in embryonic development through its interactions with the Wnt signaling pathway. DKK2 may function as either an agonist or antagonist of Wnt/beta-catenin signaling, depending on the cellular environment and the presence of the co-factor kremen 2. DKK2 protein activity is also controlled by binding to the Wnt co-receptor LRP6 (LDL-receptor related protein 6).

TSSK2 is a testis-specific serine/threonine-protein kinase required during spermatid development which phosphorylates TSKS at 'Ser-288' and SPAG16. TSSK2 takes part in the late stages of spermatogenesis, during the reconstruction of the cytoplasm. During spermatogenesis, TSSK2 is necessary for the transformation of a ring-shaped structure around the base of the flagellum originating from the chromatoid body.

Gltathione S-transferase PI 2, also known as GSTP2 is multifunctional enzyme which is involved in theprotection of cellular components against anti-cancer drugs or peroxidative stress. Furthermore, down regulation of GSTP2induces an increase of oxidative damage in the pyramidal cells of the CA1&CA3 regions as well as in the granular layer ofthe dentate gyrus, which at the end leads to structural and functional damage.

CRK belongs to the signaling adapter protein family which binds to several tyrosine-phosphorylated proteins. CRK is involved in many cellular processes such as apoptosis, proliferation, and differentiation. CRK has a modular domain architecture consisting of an SH2 followed by two SH3 domains (src-homology domains). The N-terminal SH2 domain of the CRK protein functions as a positive regulator of transformation whereas the C-terminal SH3 domain functions as a negative regulator of transformation.

Glutathione peroxidase 2 (GPX2) is a member of the glutathione peroxidase family, consisting of 8 known glutathione peroxidases (Gpx1-8) in humans. Glutathione peroxidase functions in the detoxification of hydrogen peroxide, and is one of the most important antioxidant enzymes in humans. GPX2 may have a major role in protecting mammals from the toxicity of ingested organic hydroperoxides. GPX2 is one of only a few proteins known in higher vertebrates to contain selenocysteine, which appears at the active site of glutathione peroxidase and is coded by the nonsense (stop) codon TGA.

HBsAg is the surface antigenof the Hepatitis-B-Virus (HBV). The capsidof a virus has different surface proteins from the rest of the virus. The antigen is a protein that binds specifically on one of these surface proteins. It is commonly referred to as the Australian Antigen.

GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. 3 transcript variants encoding 3 different isoforms have been found for the GCSF gene. Granulocyte/macrophage colony-stimulating factors are cytokines that take part in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.