VCAM-1 is a single-pass type I membrane protein, contains 7 Ig-like C2-type domains. It is an endothelial ligand for very late antigen-4 (VLA-4) and α4β7 integrin expressed on leukocytes, and thus mediates leukocyte-endothelial cell adhesion and signal transduction. VCAM-1 expression is induced on endothelial cells during inflammatory bowel disease, atherosclerosis, allograft rejection, infection, and asthmatic responses. During these responses, VCAM-1 forms a scaffold for leukocyte migration. VCAM-1 also activates signals within endothelial cells resulting in the opening of an "endothelial cell gate" through which leukocytes migrate. VCAM-1 has been identified as a potential anti-inflammatory therapeutic target, the hypothesis being that reduced expression of VCAM-1 will slow the development of atherosclerosis. In addition, VCAM-1-activated signals in endothelial cells are regulated by cytokines indicating that it is important to consider both endothelial cell adhesion molecule expression and function during inflammatory processes.
Vascular cell adhesion molecule 1 (VCAM1),also known as CD106,is a transmembrane glycoprotein belonging to the immunoglobulin gene superfamily. VCAM1 is expressed by cytokine-activated endothelium,interacts with integrin VLA4 (α4β1) present on the surface of leukocytes,and mediates both adhesion and signal transduction. It is also expressed either constitutively or inducibly in a variety of other cell types,including vascular smooth muscle cells,differentiating skeletal muscle cells,renal and neural epithelial cells,macrophages (Kupffer cells),dendritic cells,and bone marrow stromal cells .
Vascular cell adhesion molecule 1 (VCAM-1), also known as CD106, is a cell surface sialoglycoprotein belonging to the immunoglobulin superfamily. Two forms of VCAM-1 with either six or seven extracellular Ig-like domains are generated by alternative splicing, with the longer form predominant. VCAM-1 is an endothelial ligand for very late antigen-4 (VLA-4) and α4ß7 integrin expressed on leukocytes, and thus mediates leukocyte-endothelial cell adhesion and signal transduction. VCAM-1 expression is induced on endothelial cells during inflammatory bowel disease, atherosclerosis, allograft rejection, infection, and asthmatic responses. During these responses, VCAM-1 forms a scaffold for leukocyte migration. VCAM-1 also activates signals within endothelial cells resulting in the opening of an "endothelial cell gate" through which leukocytes migrate. VCAM-1 has been identified as a potential anti-inflammatory therapeutic target, the hypothesis being that reduced expression of VCAM-1 will slow the development of atherosclerosis. In addition, VCAM-1-activated signals in endothelial cells are regulated by cytokines indicating that it is important to consider both endothelial cell adhesion molecule expression and function during inflammatory processes.
Vinculin is a focal adhesion and cytoskeletal protein that distributed mainly at cell-cell junctions and cell-extracellular matrix (ECM) adhesion that belongs to the Vinculin/α-Catenin family. Vinculin is an Actin-binding protein and component of the Actin-Linking Functional module that senses and feels the mechanical properties of the extracellular environment. Vinculin is also a key factor that couples, transmits, transduces, and regulates mechanical force between the cytoskeleton and adhesion receptors. Vinculin generally forms two structural states, an open (active) and closed (inactive) state, which are controlled by conformational interaction(s) between the head and tail domains. Vinculin is involved in the mechano-chemical signal transmission of cells by binding to a variety of focal adhesion or cytoskeletal proteins, and plays important roles in cell adhesion, extension, motion, proliferation and survival.
Vinculin (VCL) is a cytoskeletal protein that is closely related to both cell-matrix interactions and cell-cell junctions. VCL is a membrane-cytoskeletal protein in focal adhesion plaques that is involved in linkage of integrin adhesion molecules to the actin cytoskeleton. The protein contains an acidic N-terminal domain and a basic C-terminal domain separated by a proline-rich middle segment. This protein has multi-ligand properties and has been found to interact with a number of microfilament associated proteins, such as talin, a-actinin, and paxillin, which reportedly bind to either the head or tail domains of vinculin.
Valosin-Containing Protein (VCP) is a nuclear protein that belongs to the AAA ATPase family. VCP is a putative ATP-binding protein involved in vesicle transport and fusion, 26S proteasome function, and assembly of peroxisomes. It is necessary for the fragmentation of Golgi stacks during mitosis and their reassembly after mitosis. VCP has been implicated in a number of cellular events that are regulated during mitosis, including homotypic membrane fusion, spindle pole body function, and ubiquitin-dependent protein degradation. VCP participates in the formation of the transitional endoplasmic reticulum (tER) and regulates E3 ubiquitin-protein ligase activity of RNF19A.
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