Human Vascular endothelial growth factor receptor 2(KDR, VEGFR-2) is a member of the class III subfamily of receptor tyrosine kinases (RTKs). KDR is involved in a number of fundamental biological processes such as the regulation of angiogenesis, vascular development, vascular permeability, and embryonic hematopoiesis. It also plays an essential role in promoting proliferation, survival, migration and differentiation of endothelial cells, reorganization of the actin cytoskeleton. VEGFR2 is identified as the receptor for VEGF and VEGFC and an early marker for endothelial cell progenitors, whose expression is restricted to endothelial cells in vivo.The adaptor protein SHB has been shown to interact with VEGFR2 in receptor tyrosine kinase signaling. In addition, VEGFR2 is able to interact with HIV-1 extracellular Tat protein upon VEGF activation, and seems to enhance angiogenesis in Kaposi's sarcoma lesions. VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis.
Vitronectin, also known as VTN, is a member of the pexin family. It is an abundant glycoprotein found in serum the extracellular matrix and promotes cell adhesion and spreading. Vitronectin is a secreted protein and exists in either a single chain form or a cleaved, two chain form held together by a disulfide bond. Vitronectin is a plasma glycoprotein implicated as a regulator of diverse physiological process, including blood coagulation, fibrinolysis, pericellular proteolysis, complement dependent immune responses, and cell attachment and spreading. Because of its ability to bind platelet glycoproteins and mediate platelet adhesion and aggregation at sites of vascular injury, vitronectin has become an important mediator in the pathogenesis of coronary atherosclerosis. As a multifunctional protein with a multiple binding domain, Vitronectin interacts with a variety of plasma and cell proteins. Vitronectin binds multiple ligands, including the soluble vitronectin receptor. It may be an independent predictor of adverse cardiovascular outcomes following acute stenting. Accordingly, Vitronectin is suggested to be involved in hemostasis, cell migration, as well as tumor malignancy.
Pantetheinase, also known as Pantetheine hydrolase, Vascular non-inflammatory molecule 1, Vanin-1, and VNN1, is a cell membrane protein which belongs to the CN hydrolase family and BTD/VNN subfamily. Vanin-1 contains one CN hydrolase domain. It is widely expressed with higher expression in spleen, kidney and blood. It is overexpressed in lesional psoriatic skin. Vanin-1 is also a member of the Vanin family of proteins which share extensive sequence similarity with each other, and also with biotinidase. The family includes secreted and membrane-associated proteins, a few of which have been reported to participate in hematopoietic cell trafficking. No biotinidase activity has been demonstrated for any of the vanin proteins, however, they possess pantetheinase activity, which may play a role in oxidative-stress response. Vanin-1 is an epithelial pantetheinase that provides cysteamine to tissue and regulates response to stress. Vanin-1 is expressed by enterocytes, and its absence limits intestinal epithelial cell production of proinflammatory signals. Vanin-1 regulates late adhesion steps of thymus homing under physiological, noninflammatory conditions. The early impact of vanin-1 deficiency on tumor induction was directly correlated to the amount of inflammation and subsequent epithelial proliferation rather than cell death rate. Vanin-1 molecule was shown to be involved in the control of thymus reconstitution following sublethal irradiation.
VSIG4 (V-set and immunoglobulin domain containing 4), also known as complement receptor of the immunoglobulin superfamily (CRIg) and Z39Ig, is a type I transmembrane glycoprotein. It is a B7 family-related protein and an Ig superfamily member. In contrast to the B7 family members which contain two IgG domains, VSIG4 contains one complete V-type Ig domain and a truncated C-type Ig domain. VSIG4 is exclusively expressed on tissue resident macrophages and binds to multimers of C3b and iC3b that are covalently attached to particle surfaces. No VSIG4 expression appears to be present in T and B cells. VSIG4 functions as a negative regulator of T cell activation, and may be involved in the maintenance of peripheral T cell tolerance, and is also identified as a potent suppressor of established inflammation. Mouse VSIG4 is synthesized as a 280 amino acid precursor that contains a signal sequence, an V-type Ig domain (aa 36-115), one potential N-linked glycosylation site, and a single transmembrane domain. The V-type Ig domain of mouse VSIG4 shares 86% and 80% aa sequence identity with the V-type Ig domains of rat and human VSIG4, respectively.
V-set and immunoglobulin domain containing 4 (VSIG4) is a type I transmembrane glycoprotein that is a B7 family-related protein and an Ig superfamily member. Mouse VSIG4 is synthesized as a 280 amino acid (aa) precursor that contains a signal sequence, an IgV-type immunological domain (aa 36-115),one potential N-linked glycosylation site, and a single transmembrane domain. The IgV domain of mouse VSIG4 shares 86% and 80% aa sequence identity with the IgV domains of rat and human VSIG4, respectively. VSIG4 functions as a negative regulator of mouse as well as human T cell activation, and may be involved in the maintenance of peripheral T cell tolerance and/or unresponsiveness. VSIG4 acts as a macrophage complement receptor by binding complement fragments C3b and iC3b. VSIG4 binding to C3b inhibits complement activation through the alternative pathway, making it a potent suppressor of established inflammation.
V-set and immunoglobulin domain-containing protein 8(VSIG8) is a single-pass type I membrane protein.The mouse VSIG8 cDNA encodes 417 amino acids (aa) including a 21 aa signal sequence, a 241 aa extracellular domain (ECD) containing 2 Ig-like V-type (immunoglobulin-like) domains, a 21 aa transmembrane domain and a 134 aa cytoplasmic domain. The function of VSIG8 is not clear.
Von Willebrand Factor (VWF) is a multimeric glycoprotein involved in hemostasis in blood, binds receptors on the surface of platelets and in connective tissue, thereby mediating the adhesion of platelets to sites of vascular injury. From studies it appears that VWF protein uncoils under these circumstances, decelerating passing platelets. VWF protein is deficient or defective in von Willebrand disease (VWD) and is involved in a large number of other diseases, including thrombosis, thrombotic thrombocytopenic purpura, Stroke, Heyde's syndrome, possibly hemolytic-uremic syndrome and so on.
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