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.
Plasminogen activator, urokinase, also known as PLAU and uPA, is a serine protease which converts plasminogen to plasmin, a broad-spectrum protease active on extracellular matrix (ECM) components. It is involved in complement activation, cell migration, wound healing, and generation of localized extracellular proteolysis during tissue remodelling, pro-hormone conversion, carcinogenesis and neoplasia. 、uPA and its receptor (uPAR) have been implicated in a broad spectrum of pathophysiological processes, including fibrinolysis, proteolysis, inflammation, atherogenesis and plaque destabilization, all of which are involved in the pathogenesis of MI (myocardial infarction). The role of uPA is not only linked to its action as an enzyme. In fact, the mere binding of uPA on the cell surface also brings about two events that broaden the spectrum of its biological functions: (1) a conformational change of the receptor, which, in turn, affects its interaction with other proteins, (2) a signal transduction which modulates the expression of apoptosis-related genes. Besides its applications as a thrombolytic agent and as a prognostic marker for tumors, uPA may provide the basis for other therapies, as the structure of the receptor-binding domain of uPA has become a model for the design of anti-cancer molecules. Because of the causal involvment of uPA in cancer invasion and metastasis, the blockade of uPA interactions and activity with specific inhibitors is of interest for novel strategies in cancer therapy.
Uroplakin-2 is a single-pass type I membrane protein that belongs to the uroplakin-2 family. Uroplakin-2 is a component of the asymmetric unit membrane (AUM) and expressed in the ureter, a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. Uroplakin-2 forms heterodimer with UPK1A that is necessary for exiting out of the endoplasmic reticulum (ER). Uroplakin-2 may play an important role in regulating the assembly of the AUM. AUM is believed to strengthen the urothelium by preventing cell rupture during bladder distention.
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