LYVE-1
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LYVE-1
Lymphatic vessel endothelial hyaluronan receptor 1 (LYVE1), also known as extracellular link domain containing 1 (XLKD1) is a Link domain-containing hyaladherin, a protein capable of binding to hyaluronic acid (HA), homologous to CD44, the main HA receptor. In humans it is encoded by the ''LYVE1'' gene. LYVE1 is a type I integral membrane glycoprotein Glycoproteins are proteins which contain oligosaccharide chains covalently attached to amino acid side-chains. The carbohydrate is attached to the protein in a cotranslational or posttranslational modification. This process is known as glycos .... It acts as a receptor and binds to both soluble and immobilized hyaluronan. This protein may function in lymphatic hyaluronan transport and have a role in tumor metastasis. LYVE-1 is a cell surface receptor on lymphatic endothelial cells that can be used as a lymphatic endothelial cell marker, allowing for the isolation of these cells for experimental purposes. The physiological rol ...
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Lymphatic Endothelium
The lymphatic endothelium is a specialised form of epithelium, distinct from but similar to vascular endothelium. A lymph capillary endothelial cell is distinct from other endothelial cells in that collagen fibers are directly attached to its plasma membrane. Although lymphatics were first described by Hippocrates in 400BC and rediscovered as "milky veins in the gut of a well fed dog" in the 17th century by Gasparo Aselli, they were ignored for centuries until in 1937 Howard Florey showed that lymphatics enlarge in inflammation. At this stage vascular and lymphatic endothelia were seen to be morphologically distinct and lymphatic vessels considered less important. Later it was discovered that VEGF-R3 and VEGF-C/VEGF-D were the key growth factors controlling lymphatic endothelial proliferation. Markers of lymphatic endolthelium were not discovered until relatively recently. These being LYVE-1 (Jackson et al., 1999) and podoplanin (Kerjaschki, 1999). See also Endothelium The e ...
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Link Domain
A Link domain or Link module, also known as Xlink domain (X for extracellular), is a protein domain that binds to hyaluronic acid. It is important in blood cell migration and apoptosis. The link domain is found in some extracellular proteins in vertebrates such as the hyalectans. It appears to be involved in extracellular matrix assembly and stability, cell adhesion, and migration. Structure The structure has been shown to consist of two alpha helices and two antiparallel beta sheets arranged around a large hydrophobic core similar to that of C-type lectin. This domain contains four conserved cysteines involved in two disulphide bonds. The link domain has also been termed HABM (hyaluronic acid binding module) and PTR (proteoglycan tandem repeat). Link domain proteins Proteins which contain the link domain include: * the hyalectans (a family of proteoglycans): aggrecan, brevican, neurocan and versican, which are expressed in the CNS; * the cartilage link protein (LP), a prot ...
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Hyaladherin
Hyaladherins, also known as hyaluronan-binding proteins, are proteins capable of binding to hyaluronic acid. Most hyaladherins belong to the Link module superfamily, including its main receptor CD44, hyalectans and TSG-6. In addition there is a diverse group of hyaladherins lacking a Link module; these include the receptor RHAMM, C1QBP (HABP1) and HABP2. The primary roles of hyaladherins are cell adhesion, structural support of the extracellular matrix (ECM) and cell signalling. Due to the role of aberrant hyaluronic acid synthesis and degradation in various cancers, hyaladherins, as well as hyaluronic acid, are considered a promising target for cancer therapy. See also *Hyaluronan synthase *Hyaluronidase Hyaluronidases are a family of enzymes that catalyse the degradation of hyaluronic acid (HA). Karl Meyer classified these enzymes in 1971, into three distinct groups, a scheme based on the enzyme reaction products. The three main types of hyal ... References {{reflist ...
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Hyaluronic Acid
Hyaluronic acid (; abbreviated HA; conjugate base hyaluronate), also called hyaluronan, is an anionic, nonsulfated glycosaminoglycan distributed widely throughout connective, epithelial, and neural tissues. It is unique among glycosaminoglycans as it is non-sulfated, forms in the plasma membrane instead of the Golgi apparatus, and can be very large: human synovial HA averages about 7 million Da per molecule, or about 20,000 disaccharide monomers, while other sources mention 3–4 million Da. The average 70 kg (150 lb) person has roughly 15 grams of hyaluronan in the body, one-third of which is turned over (i.e., degraded and synthesized) per day. As one of the chief components of the extracellular matrix, it contributes significantly to cell proliferation and migration, and is involved in the progression of many malignant tumors. Hyaluronic acid is also a component of the group A streptococcal extracellular capsule, and is believed to play a role in virule ...
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CD44
The CD44 antigen is a cell-surface glycoprotein involved in cell–cell interactions, cell adhesion and migration. In humans, the CD44 antigen is encoded by the ''CD44'' gene on chromosome 11. CD44 has been referred to as HCAM (homing cell adhesion molecule), Pgp-1 (phagocytic glycoprotein-1), Hermes antigen, lymphocyte homing receptor, ECM-III, and HUTCH-1. Tissue distribution and isoforms CD44 is expressed in a large number of mammalian cell types. The standard isoform, designated CD44s, comprising exons 1–5 and 16–20 is expressed in most cell types. CD44 splice variants containing variable exons are designated CD44v. Some epithelial cells also express a larger isoform (CD44E), which includes exons v8–10. Function CD44 participates in a wide variety of cellular functions including lymphocyte activation, recirculation and homing, hematopoiesis, and tumor metastasis. CD44 is a receptor for hyaluronic acid and can also interact with other ligands, such as osteop ...
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Glycoprotein
Glycoproteins are proteins which contain oligosaccharide chains covalently attached to amino acid side-chains. The carbohydrate is attached to the protein in a cotranslational or posttranslational modification. This process is known as glycosylation. Secreted extracellular proteins are often glycosylated. In proteins that have segments extending extracellularly, the extracellular segments are also often glycosylated. Glycoproteins are also often important integral membrane proteins, where they play a role in cell–cell interactions. It is important to distinguish endoplasmic reticulum-based glycosylation of the secretory system from reversible cytosolic-nuclear glycosylation. Glycoproteins of the cytosol and nucleus can be modified through the reversible addition of a single GlcNAc residue that is considered reciprocal to phosphorylation and the functions of these are likely to be an additional regulatory mechanism that controls phosphorylation-based signalling. In contrast, ...
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Cell Sorting
Cell sorting is the process through which a particular cell type is separated from others contained in a sample on the basis of its physical or biological properties, such as size, morphological parameters, viability and both extracellular and intracellular protein expression. The homogeneous cell population obtained after sorting can be used for a variety of applications including research, diagnosis, and therapy. Methods Methods of cell sorting fall into two major categories: fluorescence activated cell sorting (FACS) and immunomagnetic cell sorting. Due to many years of refinement and increased demand for cell separation however, researchers are working to develop microfluidic sorting devices that have many benefits in comparison to the main types of fluorescence-activated cell sorting and immunomagnetic cell sorting methods. Fluorescence-activated Fluorescence-Activated Cell Sorting, is also known as flow cytometry cell sorting, or commonly known by the acronym FACS, wh ...
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Pleomorphism (cytology)
Pleomorphism is a term used in histology and cytopathology to describe variability in the size, shape and staining of cells and/or their nuclei. Several key determinants of cell and nuclear size, like ploidy and the regulation of cellular metabolism, are commonly disrupted in tumors. Therefore, cellular and nuclear pleomorphism is one of the earliest hallmarks of cancer progression and a feature characteristic of malignant neoplasms and dysplasia. Certain benign cell types may also exhibit pleomorphism, e.g. neuroendocrine cells, Arias-Stella reaction. A rare type of rhabdomyosarcoma that is found in adults is known as pleomorphic rhabdomyosarcoma. Despite the prevalence of pleomorphism in human pathology, its role in disease progression is unclear. In epithelial tissue, pleomorphism in cellular size can induce packing defects and disperse aberrant cells. But the consequence of atypical cell and nuclear morphology in other tissues is unknown. See also *Anaplasia *Cell growt ...
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