The Urokinase Type Plasminogen Activator (uPA) receptor (uPAR) is a widely expressed receptor for urokinase plasminogen activator (uPA) and pro-uPA. uPAR / CD87 is a highly glycosylated, 55-60kDa integral membrane protein linked to the plasma membrane by a glycosylphosphatidylinositol (GPI) anchor. uPAR is expressed by T-cells, NK cells, monocytes, and neutrophils as well as non-hematopoietic cells that include vascular endothelial cells, fibroblasts, smooth muscle cells, keratinocytes, placental trophoblasts, hepatocytes, and a wide variety of tumor cells (including breast, colon, and prostate carcinoma, melanoma). It plays a critical role in the regulation of cell-surface plasminogen activation in physiological and pathological conditions, and it is also involved in cellular adhesion, the transmission of extracellular signals across the plasma membrane and the subsequent regulation of gene expression. uPAR has been implicated in several biological processes including angiogenesis, monocyte migration, cancer metastasis, trophoblast implantation, and wound healing. Human uPAR is encoded as a 313 amino acid residue polypeptide, excluding a 22 residue signal peptide and shows 60-70% similarity with the murine uPAR amino acid sequence although binding of uPA to uPAR shows strong species specificity.
Uridinephosphorylase 1 (UPP1) is a member of the family of pentosyltransferase. UPP1 catalyses the reversible phosphorolysis of uridine to uracil. The expression levels and the enzymatic activity of UPP1 are higher in human solid tumors than in adjacent normal tissues. The high level of UPP1 expression in some tumors makes it a potential prognosticfactor for some cancers, such as oral squamous cell carcinoma. UPP1 is important for the homeostatic regulation of intracellular and plasma uridine concentratios. UPP1 plays an important role in the pyrimidine salvage pathway through its catalysis of the reversible phosphorolysis of uridine to uracil.
UPRT is a cytoplasmic enzyme which belongs to the UPRTase family. UPRT is highly expressed in leukocytes, liver, spleen and thymus, with lower expression in brain, lung and skeletal muscle. UPRTcatalyzes the conversion of uracil and 5-phosphoribosyl-1-R-diphosphate to uridine monophosphate (UMP). This reaction is an important part of nucleotide metabolism, specifically the pyrimidine salvage pathway. UPRT is a potential target for rational design of drugs to treat parasitic infections and cancer
Cytochrome b-c1 complex subunit 6, mitochondrial (UQCRH) belongs to the UQCRH/QCR6 family, it is a subunit of the respiratory chain protein Ubiquinol Cytochrome c Reductase. This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. UQCRH may mediate formation of the complex between cytochromes c and c1. It may mediate formation of the complex between cytochromes c and c1.
Isoform 1 is widely expressed with the highest expression in skeletal muscle, heart and testicles. Isoform 2 has the highest expression levels in tissues containing proliferating cells. Uracil-DNA glycosylase exists in two forms: mitochondrial uracil-DNA glycosylase 1 (UNG1) and nuclear uracil-DNA glycosylase 2 (UNG2). uracil-DNA glycosylase. This gene encodes one of several uracil-DNA glycosylases. One important function of uracil-DNA glycosylases is to prevent mutagenesis by eliminating uracil from DNA molecules by cleaving the N-glycosylic bond and initiating the base-excision repair (BER) pathway. Uracil bases occur from cytosine deamination or misincorporation of dUMP residues. Alternative promoter usage and splicing of this gene leads to two different isoforms: the mitochondrial UNG1 and the nuclear UNG2. The UNG2 term was used as a previous symbol for the CCNO gene (GeneID 10309), which has been confused with this gene, in the literature and some databases. Defects in UNG are a cause of immunodeficiency with hyper-IgM type 5 (HIGM5). A rare immunodeficiency syndrome characterized by normal or elevated serum IgM levels with absence of IgG, IgA, and IgE. It results in a profound susceptibility to bacterial infections.
Uroporphyrinogen decarboxylase (UROD), is an enzyme of the heme biosynthetic pathway which belongs to the uroporphyrinogen decarboxylase family. This enzyme is responsible for catalyzing the conversion of uroporphyrinogen to coproporphyrinogen through the removal of four carboxymethyl side chains. UROD is a homodimeric enzyme that catalyzes the fifth step in heme biosynthesis: the elimination of carboxyl groups from the four acetate side chains of uroporphyrinogen III to yield coproporphyrinogen III. Defects in UROD are the cause of familial porphyria cutanea tarda (FPCT) and hepatoerythropoietic porphyria (HEP).
Recombinant Human Urokinase-Type Plasminogen Activator is a serine protease, which specifically cleaves the zymogen plasminogen to form the active enzyme plasmin. Urokinase-Type Plasminogen Activator is a potent marker of invasion and metastasis in many human cancers associated with breast, colon, stomach, bladder, brain, ovary and endometrium. Human Urokinase-Type Plasminogen Activator is initially synthesized as 431 amino acid precursor with a N-terminal signal peptide residues. The single chain molecule is processed into a disulfide-linked two-chain molecule. There exists two forms A chain, the long A chain contains an EGF-like domain that is responsible for binding of the uPA receptor. The B chain corresponds to the catalytic domain.
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