Ubiquitin carboxyl-terminal hydrolase 5, also known as Deubiquitinating enzyme 5, Isopeptidase T, Ubiquitin thiolesterase 5, Ubiquitin-specific-processing protease 5, ISOT and USP5, is a member of the peptidase C19 family. USP5 contains 2UBA domains and one UBP-type zinc finger. The UBP-type zinc finger domain interacts selectively with an unmodified C-terminus of the proximal ubiquitin. Both UBA domains are involved in polyubiquitin recognition. The UBP-type zinc finger domain crystallizes as a dimer linked by a disulfide bond between the Cys-195 residues of both molecules, but there is no evidence that the full-length USP5 exists as a dimer. USP5 cleaves linear and branched multiubiquitin polymers with a marked preference for branched polymers. USP5 is involved in unanchored 'Lys-48'-linked polyubiquitin disassembly. It binds linear and 'Lys-63'-linked polyubiquitin with a lower affinity. Knock-down of USP5 causes the accumulation of p53/TP53 and an increase in p53/TP53 transcriptional activity because the unanchored polyubiquitin that accumulates is able to compete with ubiquitinated p53/TP53 but not with MDM2 for proteasomal recognition.
Ubiquitin carboxyl-terminal hydrolase 7, also known as Ubiquitin thioesterase 7, Herpesvirus-associated ubiquitin-specific protease, Ubiquitin-specific-processing protease 7, USP7 and HAUSP, is a widely expressed protein which belongs to thepeptidase C19 family. USP7 is a member of the family of deubiquitinating enzymes. It is involved in the regulation of stress response pathways, epigenetic silencing and the progress of infections by DNA viruses. USP7 is a protein with a cysteine peptidase core, N- and C-terminal domains required for protein-protein interactions. USP7 contributes to epigenetic silencing of homeotic genes by Polycomb (Pc). USP7 cleaves ubiquitin fusion protein substrates. It deubiquitinates TP53/p53 and MDM2 and strongly stabilizes TP53 even in the presence of excess MDM2. USP7 also induces TP53-dependent cell growth repression and apoptosis. USP7 has key roles in the p53 pathway whereby it stabilizes both p53 and MDM2. Herpes simplex virus type 1 (HSV-1) regulatory protein ICP0 stimulates lytic infection and the reactivation of quiescent viral genomes. ICP0 interacts very strongly with USP7. USP7-mediated stabilization of ICP0 is dominant over ICP0-induced degradation of USP7 during productive HSV-1 infection. The biological significance of the ICP0-USP7 interaction may be most pronounced in natural infection situations, in which limited amounts of ICP0 are expressed.
Uteroglobin (UG); also known as Secretoglobin 1A member 1 (SCGB1A1); Blastokinin; Clara cell secretor protein (CCSP) or Clara cell-specific 10-kDa protein (CC10); is the founding member of the secretoglobin family of small; secreted; disulfide-bridged dimeric proteins found only in mammals. This protein is mainly expressed in lung; with anti-inflammatory/immunomodulatory properties. Previous in vitro studies demonstrated that CCAAT/enhancer-binding proteins (C/EBPs) are the major transcription factors for the regulation of SCGB1A1 gene expression; whereas FOXA1 had a minimum effect on the transcription. Uteroglobin is a multifunctional protein with antiinflammatory/immunomodulatory properties. Uteroglobin inhibits soluble phospholipase A(2) activity and binds and perhaps sequesters hydrophobic ligands such as progesterone; retinols; polychlorinated biphenyls; phospholipids; and prostaglandins. In addition to its antiinflammatory activities; Uteroglobin manifests antichemotactic; antiallergic; antitumorigenic; and embryonic growth-stimulatory activities. The tissue-specific expression of the Uteroglobin gene is regulated by several steroid hormones; although a nonsteroid hormone; prolactin; further augments its expression in the uterus. Based on its anti-inflammatory and antiallergic properties; Uteroglobin is a potential drug target. The mechanism of Uteroglobin action is likely to be even more complex as it also functions via a putative receptor-mediated pathway.
Membrane primary amine oxidase(AOC3); also known as vascular adhesion protein (VAP-1) and HPAO; this protein is a member of the semicarbazide-sensitive amine oxidase (SSAO) family. VAP-1 is a type 1 membrane-bound glycoprotein that has a distal adhesion domain and an enzymatically active amine oxidase site outside of the membrane; VAP-1 has adhesive properties; functional monoamine oxidase activity; and possibly plays a role in glucose handling; leukocyte trafficking; and migration during inflammation. This rise in metabolic products contributes to generating advanced glycation end-products and oxidative stress along with the monoamine detoxification in the organism. It is highly expressed on the endothelium of the lung and trachea; and absent from leukocytes and epithelial cells. Membrane-bound VAP-1 releases an active; soluble form of the protein; which may be conducive to increased inflammation and the progression of many vascular disorders. In particular; elevation of VAP-1 activity and the increased enzymatic-mediated deamination is proposed to play a role in renal and vascular disease; oxidative stress; acute and chronic hyperglycemia; and diabetes complications.
Vascular adhesion protein-1(VAP-1) is a copper amine oxidase with a topaquinone cofactor.VAP-1 is a type II integral membrane protein; but a soluble form of the enzyme is present in human serum; and its level increases in diabetes and some inflammatory liver diseases. VAP-1 catalyzes the oxidative deamination of small primary amines such as methylamine; benzylamine; and aminoacetone in a reaction that produces an aldehyde; ammonia; and H2O2. VAP-1 vascular expression is regulated at sites of inflammation through its release from intracellular granules in which the protein is stored. The adhesive function of VAP-1 has been demonstrated in studies showing that the protein is important for the adherence of certain lymphocyte subtypes to inflamed endothelial tissues. VAP-1 mediated adhesion is involved in the process of leukocyte extravasation; an important feature of inflammatory responses. VAP-1 is considered to be a therapeutic target for diabetes; oxidative stress; and inflammatory diseases.
vesicle-associated membrane protein-associated protein B/C (VAPB) is presents in mitochondria-associated membranes that are endoplasmic reticulum membrane regions closely apposed to the outer mitochondrial membrane. It can form homodimer; and heterodimer with VAPA. It also interacts with VAMP1; VAMP2; HCV NS5A; NS5B; ZFYVE27 and RMDN3. VAPB participates in the endoplasmic reticulum unfolded protein response (UPR) by inducing ERN1/IRE1 activity. It is involved in cellular calcium homeostasis regulation.
Vasorin is a Type I membrane protein, which is predominantly expressed in vascular smooth muscle cells in a developmentally regulated pattern. The expression level of Vasorin can be down regulated during vessel repair after arterial injury. Vasorin binds to transforming growth factor beta (TGF-β) and attenuates TGF-β signaling in vitro.
Lascia la tua email e seleziona le aree che vuoi seguire per ricevere novita di prodotto, approfondimenti tecnici e promozioni piu pertinenti.
Puoi scegliere le macro-aree Life Science e Diagnostica oppure le singole specializzazioni.
Seleziona uno o piu ambiti di interesse per ricevere comunicazioni piu utili e mirate.
Aggiornamenti su ricerca, strumentazione e applicazioni per il mondo Life Science.
Novita, approfondimenti e promozioni per laboratori diagnostici e flussi operativi.
2025 TEMA Ricerca - All Rights Reserved.
