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.
Vaspin (Visceral Adipose-Specific SERPIN) is a newly described adipokine. Vaspin has three β-sheets; nine α-helices; and one central loop; the structure is part of the set of distinctive features that are descriptive of Serpin family members. Vaspin is also a unique insulin sensitizing adipocytokine in obesity. A recent publication indicates that Vaspin mRNA expression in visceral fat is positively correlated with BMI and percent of body fat. and could be associated with parameters of obesity; insulin resistance; and glucose metabolism. These findings suggest a potential clinical use for Vaspin in ameliorating certain aberrations seen in the obesity metabolic syndrome.
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