Synonyms for glypican or Related words with glypican

syndecan              testican              mimecan              attractin              neuropilin              prominin              desmocollin              versican              decysin              plexin              biglycan              alcam              semaphorin              neurofascin              emilin              cadherin              galectin              betaglycan              osteoglycin              claudin              nephronectin              antibodysanta              spondin              fibromodulin              ceacam              plakophilin              perlecan              lectican              neuroligin              nectin              desmoglein              tetraspanin              nidogen              meltrin              decorin              serglycin              tetraspan              brevican              cubilin              subfamilyb              nucleobindin              caldesmon              basigin              dystroglycan              protocadherin              dystonin              sortilin              osteoadherin              angiopoietin              lumican             



Examples of "glypican"
In humans, glypican-1 is overexpressed in breast and brain cancers (gliomas), while glypican-3 is overexpressed in liver cancers.
Glypican-3 is a protein that in humans is encoded by the "GPC3" gene. The protein encoded by this gene is a member of the glypican family.
Glypican 3 immunostaining has utility for differentiating hepatocellular carcinoma (HCC) and dysplastic changes in cirrhotic livers; HCC stains with glypican 3, while liver with dysplastic changes and/or cirrhotic changes does not.
Glypican-1 is a protein that in humans is encoded by the "GPC1" gene.
Glypican-4 is a protein that in humans is encoded by the "GPC4" gene.
Glypican-6 is a protein that in humans is encoded by the "GPC6" gene.
Glypican-5 is a protein that in humans is encoded by the "GPC5" gene.
Glypican 2 (GPC2), also known cerebroglycan, is a protein which in humans is encoded by the "GPC2" gene.
Gigantism is believed to be caused, in some cases, by a loss of function of the Glypican 3 co-receptor.
Sulf2’s role in HCC contrasted with Sulf1. Sulf2 was upregulated in a majority of HCCs and HCC cell lines, and Sulf2 knockdown eliminated migration and proliferation. Sulf2 also upregulated glypican-3, which is commonly overexpressed in HCC, by increasing ERK, AKT activation through enhanced FGF2 signaling. GPC3 is important in Sulf2-enhanced FGF signaling in vitro, so glypican-3 may mediate its own upregulation through Sulf2. Given that Sulf1 and Sulf2 have redundant functions, Sulf2 contrasting function in HCC was unexpected.
Glypicans can modify cell signaling pathways and contribute to cellular proliferation and tissue growth. In "Drosophila", the glypican "dally" assists diffusion of the BMP-family growth-promoting morphogen Decapentaplegic in the developing wing, while the developing haltere lacks "dally" and remains small. Extracellular localization of the other glypican in "Drosophila", "dally-like", is also required for the proper level of Hedgehog signaling in the developing wing.
Cell surface heparan sulfate proteoglycans are composed of a membrane-associated protein core substituted with a variable number of heparan sulfate chains. Members of the glypican-related integral membrane proteoglycan family (GRIPS) contain a core protein anchored to the cytoplasmic membrane via a glycosyl phosphatidylinositol linkage. These proteins may play a role in the control of cell division and growth regulation.
Cell surface heparan sulfate proteoglycans are composed of a membrane-associated protein core substituted with a variable number of heparan sulfate chains. Members of the glypican-related integral membrane proteoglycan family (GRIPS) contain a core protein anchored to the cytoplasmic membrane via a glycosyl phosphatidylinositol linkage. These proteins may play a role in the control of cell division and growth regulation.
Previous research had suggested the condition linked to PTEN on chromosome 10, while other research pointed to chromosome 16. Prior to the findings regarding AKT1 in 2011, other researchers expressed doubt regarding the involvement of PTEN or GPC3, which codes for glypican 3 and may play a role in regulating cell division and growth regulation.
An association between biliary atresia and the ADD3 gene was first detected in Chinese populations through a Genome-wide association study, and was confirmed in Thai Asians and Caucasians. A possible association with deletion of the gene GPC1, which encodes a glypican 1-a heparan sulfate proteoglycan, has been reported. This gene is located on the long arm of chromosome 2 (2q37) and is involved in the regulation of inflammation and the Hedgehog gene.
Heparan sulfate is a glycosaminoglycan (GAG) that is linked by xylose to serine residues of proteins such as perlecan, syndecan, or glypican. Sulfation of heparan sulfate GAGs helps give diversity to cell surface proteins and provides them with a unique sulfation pattern that allows them to specifically interact with other proteins. For example, in mast cells the AT-III-binding pentasaccharaide is synthesized with essential heparan sulfate sulfation steps. The binding of the heparan sulfate in this pentasaccharide to AT-III inactivates the blood-coagulation factors thrombin and Factor Xa. Heparan sulfates are also known to interact with growth factors, cytokines, chemokines, lipid and membrane binding proteins, and adhesion molecules.
For all members of the glypican family, the C-terminus of the protein is attached to the cell membrane covalently via a glycosylphosphatidylinositol (GPI) anchor. To allow for the addition of the GPI anchor, glypicans have a hydrophobic domain at the C-terminus of the protein. Within 50 amino acids of this GPI anchor, the heparan sulfate chains attach to the protein core. Therefore, unlike syndecans the heparan sulfate glycosaminoglycan chains attached to glypicans are located rather close to the cell-membrane. The glypicans found in vertebrates, "Drosophila", and "C. elegans" all have an N-terminal signal sequence.
Dally (division abnormally delayed) is the name of a gene that encodes a HS-modified-protein found in the fruit fly ("Drosophila melanogaster"). The protein has to be processed after being codified, and in its mature form it is composed by 626 amino acids, forming a proteoglycan rich in heparin sulfate which is anchored to the cell surface via covalent linkage to glycophosphatidylinositol (GPI), so we can define it as a glypican. For its normal biosynthesis it requires sugarless ("sgl"), a gene that encodes an enzyme which plays a critical role in the process of modification of dally.
Glypicans constitute one of the two major families of heparin sulfate proteoglycans, with the other major family being syndecans. Six glypicans have been identified in mammals, and are referred to as GPC1 through GPC6. In "Drosophila" two glypicans have been identified, and these are referred to as dally (division abnormally delayed) and dally-like. One additional glypican has been identified in "C. elegans". Glypicans seem to play a vital role in developmental morphogenesis, and have been suggested as regulators for the Wnt and Hedgehog cell signaling pathways. They have additionally been suggested as regulators for fibroblast growth factor and bone morphogenic protein signaling.
The C-terminal of Versican interacts with a variety of molecules in the matrix. One important family of ligands is the tenascin family. For example, The C-lectin domain of versican interacts with tenascin R through its fibronectin type III (FnIII) repeat 3-5 domain in a calcium dependent manner, "in vivo". Different tenascin domains interact with a wide range of cellular receptors, including integrins, cell adhesion molecules and members of the syndecan and glypican proteoglycan families. Versican’s C-terminal domain interacts with fibulin-2, a protein whose expression is associated with that of versican in the developing heart. The EGF domain of the C-terminal of versican also binds the EGF-receptor molecule "in vivo".