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This antigen is known for its role in tissue-specific adhesion of lymphocytes to high endothelium venules. [23] Through these interactions they play a crucial role in orchestrating circulating lymphocytes. CAM function in cancer metastasis, inflammation, and thrombosis makes it a viable therapeutic target that is currently being considered.
Many studies have postulated that increased production of cell adhesion molecules (CAMs) on the vascular endothelium (blood vessel lining) plays a role in the development of arterial plaque, with the suggestion from both in vitro and in vivo studies that the CAM production is increased by dyslipidemia (abnormal lipid levels in the blood). [3]
VCAM-1 is a member of the immunoglobulin superfamily, the superfamily of proteins including antibodies and T-cell receptors.The VCAM-1 gene contains six or seven immunoglobulin domains, and is expressed on both large and small blood vessels only after the endothelial cells are stimulated by cytokines.
Schematic of cell adhesion. Cell adhesion is the process by which cells interact and attach to neighbouring cells through specialised molecules of the cell surface. This process can occur either through direct contact between cell surfaces such as cell junctions or indirect interaction, where cells attach to surrounding extracellular matrix, a gel-like structure containing molecules released ...
P-selectin is a type-1 transmembrane protein that in humans is encoded by the SELP gene. [5] P-selectin functions as a cell adhesion molecule (CAM) on the surfaces of activated endothelial cells, which line the inner surface of blood vessels, and activated platelets. In unactivated endothelial cells, it is stored in granules called Weibel ...
The addition of RGD onto a cardiac tissue scaffold has been shown to promote cell adhesion, prevent apoptosis and enhance tissue regeneration. [33] RGD peptide has also been used to improve endothelial cell adhesion and proliferation on synthetic heart valves. [34] A titanium alloy hip joint replacement.
This transmembrane glycoprotein complex is composed of four subunits: GPIbα, GPIbβ, GPV and GPIX.Each of them has a variable number of leucine-rich repeats.GPIbα and GPIbβ are linked by disulfide bridges, while the GPV and GPIX associate non-covalently with the complex.
In the mid-region of the protein, family members have a proline-rich region that binds SH3 and WW domain-containing proteins. Their C-terminal EVH2 domain mediates tetramerization and binds both G and F actin. VASP is associated with filamentous actin formation and likely plays a widespread role in cell adhesion and motility.