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.
Serpins are the largest and most diverse family of protease inhibitors. Most serpins control proteolytic cascades, certain serpins do not inhibit enzymes, but instead perform diverse functions such as storage (ovalbumin, in egg white), hormone carriage proteins (thyroxine-binding globulin, cortisol-binding globulin) and tumor suppressor genes (maspin). Most inhibitory serpins target chymotrypsin-like serine proteases. These enzymes are defined by the presence of a nucleophilic serine residue in their catalytic site. Some serpins inhibit other classes of protease. A number of such serpins have been shown to target cysteine proteases. These enzymes differ from serine proteases in that they are defined by the presence of a nucleophilic cysteine residue, rather than a serine residue, in their catalytic site. SerpinA12, also known as OL-64, Visceral adipose tissue-derived serine protease inhibitor, Vaspin, Visceral adipose-specific serpin and SERPINA12, is a secreted ,protein which belongs to the ,serpin family. SerpinA12 / Vaspin is expressed in visceral adipose tissues. It may modulates insulin action conceivably only in the presence of its yet undefined target proteases in white adipose tissues. SerpinA12 / Vaspin may be the compensatory molecule in the pathogenesis of metabolic syndrome and SerpinA12 / Vaspin recombinant protein or vaspin-mimicking agents such as vaspin analogs, antibodies or small molecule agents may be the link to drug discovery and development.
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